(en)Zymomonas is unable to synthesize pantothenic acid and requires this essential vitamin in growth medium. Zymomonas strains transformed with an operon for expression of 2-dehydropantoate reductase and aspartate 1-decarboxylase were able to grow in medium lacking pantothenic acid. These strains may be used for ethanol production without pantothenic acid supplementation in seed culture and fermentation media.

1.ApplicationNumber: US-201213433343-A
1.PublishNumber: US-8765426-B2
2.Date Publish: 20140701
3.Inventor: TAO LUAN
TOMB JEAN-FRANCOIS
VIITANEN PAUL V.

4.Inventor Harmonized: TAO LUAN(US)
TOMB JEAN-FRANCOIS(US)
VIITANEN PAUL V(US)

5.Country: US
6.Claims:
(en)Zymomonas is unable to synthesize pantothenic acid and requires this essential vitamin in growth medium. Zymomonas strains transformed with an operon for expression of 2-dehydropantoate reductase and aspartate 1-decarboxylase were able to grow in medium lacking pantothenic acid. These strains may be used for ethanol production without pantothenic acid supplementation in seed culture and fermentation media.

7.Description:
(en)This application claims the benefit of U.S. Provisional Application 61/472,664, filed Apr. 7, 2011, and is incorporated by reference in its entirety.


STATEMENT OF GOVERNMENT RIGHTS
This invention was made with United States government support under Contract No. DE-FC36-07GO17056 awarded by the Department of Energy. The government has certain rights in this invention.


FIELD OF THE INVENTION
The invention relates to the fields of microbiology and genetic engineering. More specifically, Zymomonas was engineered for expression of enzymes to provide a pathway for pantothenate biosynthesis.
BACKGROUND OF THE INVENTION
Production of ethanol by microorganisms provides an alternative energy source to fossil fuels and is therefore an important area of current research. The bacteria Zymomonas naturally produces ethanol, and has been genetically engineered for improved ethanol production. Improvements include elimination of competing pathways, utilization of xylose, and better performance in medium containing biomass hydrolysate (for example: U.S. Pat. No. 7,741,119, U.S. Pat. No. 5,514,583, U.S. Pat. No. 5,712,133, WO 95/28476, Feldmann et al. (1992) Appl. Microbiol. Biotechnol. 38: 354-361, Zhang et al. (1995) Science 267:240-243, and US 2009-0203099 A1). The hydrolysate produced from lignocellulosic and cellulosic biomass can provide an abundantly available, low cost source of carbon substrates for biocatalyst fermentation to produce desired products. Biomass hydrolysate typically includes xylose, as well as inhibitors of fermentation.
For economical fermentative production, it is desired that a biocatalyst does not require addition of any costly nutrients to growth and production media. In particular, it is desired that no vitamin supplements be required for seed or production biocatalyst cultures. Zymomonas requires supplementation of pantothenic acid (PA; also pantothenate, vitamin B 5 , 3-[(2,4-dihydroxy-3,3-dimethylbutanoyl)amino]propanoic acid) in growth medium, being unable to synthesize this nutrient (Seo et al. (2005) Nat. Biotechnol. 23:63-68; Nipkow et al. (1984) Appl. Microbiol. Biotechnol. 19:237-240 and references therein). PA is an important cellular component as it is required for the synthesis of coenzyme-A (CoA), a compound with many important cellular functions. For many animals it is an essential nutrient, while many plants express enzymes for the synthesis of PA.
E. coli is able to synthesize PA and the biosynthetic pathway is known. E. coli genes encoding enzymes of the pathway have been identified. Increased production of pantothenate has been achieved by overexpressing genes in the biosynthetic pathway of microorganisms that naturally produce pantothenate. Disclosed in WO 2003006664 is increasing expression of coding regions in a Bacillus that naturally produces D-pantothenic acid, such as ybbT, ywkA, yjmC, ytsJ, mdh, cysK, iolJ, pdhD, yuiE, dhas, adk, yusH, yqhJ, yqhK, and/or yqh-I for increased pantothenic acid production. In addition, panE, ylbQ, panB, panD, panC, ilvB, ilvN, alsS, ilvC, ilvD, serA, serC, ywpJ, and/or glyA may be increased in expression. U.S. Pat. No. 6,171,845 discloses amplification of nucleotide sequences encoding keptopantoate reductase, in particular panE, in pantothenic acid producing microorganisms. It was shown that the Saccharomyces cerevisiae YRH063c ORF encodes a protein having ketopantoate reductase activity by complementation of a panE-ilvC mutant in E. coli . US 20050089973 discloses producing panto-compounds in microorganisms where existing biosynthetic pathways are manipulated, such as by overexpressing ketopantoate reductase and aspartate alpha-decarboxylase.
US 2005221466 discloses the use of cells with alanine 2,3-aminomutase activity, which converts alpha-alanine to beta-alanine, for production of pantothenate.
There remains a need for creating Zymomonas strains that are able to grow and produce ethanol in the absence of externally supplied PA. These Zymomonas strains may be used to improve and reduce the cost of ethanol production using this biocatalyst.
SUMMARY OF THE INVENTION
The invention provides recombinant Zymomonas cells that express heterologous enzymes to provide a PA biosynthetic pathway.
Accordingly, the invention provides a bacterial strain of the genus Zymomonas comprising a heterologous nucleic acid molecule encoding a polypeptide having 2-dehydropantoate reductase activity and a heterologous nucleic acid molecule encoding a polypeptide having aspartate 1-decarboxylase activity.
In another embodiment the invention provides a process for producing a Zymomonas strain that synthesizes pantothenic acid comprising:
a) providing a bacterial strain of the genus Zymomonas;
b) introducing a heterologous nucleic acid molecule encoding a polypeptide having 2-dehydropantoate reductase activity; and
c) introducing a heterologous nucleic acid molecule encoding a polypeptide having aspartate 1-decarboxylase activity;
wherein steps b) and c) may be in either order or simultaneous and wherein 2-dehydropantoate reductase and aspartate 1-decarboxylase activities are expressed in the strain.
In yet another embodiment the invention provides a method for producing ethanol comprising:
a) providing the recombinant bacterial strain of the genus Zymomonas comprising a heterologous nucleic acid molecule encoding a polypeptide having 2-dehydropantoate reductase activity and a heterologous nucleic acid molecule encoding a polypeptide having aspartate 1-decarboxylase activity; and
b) contacting the strain of (a) with fermentation medium under conditions whereby the strain produces ethanol.



BRIEF DESCRIPTION OF THE FIGURES, BIOLOGICAL DEPOSITS AND SEQUENCE DESCRIPTIONS
Applicants have made the following biological deposits under the terms of the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purposes of Patent Procedure:
Information on Deposited Strains









Depositor
International


Identification
Depository
Date of

Reference
Designation
Deposit



Zymomonas ZW658
ATCC No PTA-7858
Sep. 12, 2006


















FIG. 1 is a diagram of a pantothenic acid biosynthetic pathway with bold arrows marking activities that may be present in Zymomonas and arrows with “X” marking absent activities. The numbers with the arrows are EC numbers of enzymes that perform the shown reaction. Gene names associated with the EC numbers are given in some cases.
FIG. 2 shows conserved amino acid positions, using one letter abbreviations, of aspartate 1-decarboxylase polypeptides in a general structure diagram (A), in a representative sequence (B), and in the E. coli aspartate 1-decarboxylase amino acid sequence (C).
FIG. 3 shows conserved amino acid positions, using one letter abbreviations, of 2-dehydropantoate reductase polypeptides in a general structure diagram (A), in a representative sequence (B), in the E. coli 2-dehydropantoate reductase amino acid sequence based on a ten sequence alignment (C), and in the E. coli 2-dehydropantoate reductase amino acid sequence based on a 648 sequence alignment (D).
FIG. 4 shows a graph of growth curves of wild type Zymomonas strain ZW1 grown in minimal medium supplemented with different concentrations of pantothenic acid (PA), after a PA-depletion step.
FIG. 5 shows a graph of growth curves of wild type Zymomonas strain ZW1(A) and strain ZW1/PanED#1 (also referred to as ZED#1) (B) grown in minimal medium with or without 2.5 mg/L pantothenic acid supplementation, after a PA-depletion step.
FIG. 6 shows a graph of growth curves of Zymomonas strain ZW801-4 in (A) minimal medium with and without 2.5 mg/L pantothenic acid supplementation, after a PA-depletion step, and in (B) minimal medium containing 15 mg/L p-aminobenzoic acid and different concentrations of pantothenic acid, after a PA-depletion step.
FIG. 7 shows a graph of growth curves of Zymomonas strains ZW801-4 (A) and ZW801-4/PanED#1(B) grown in minimal medium supplemented with 15 mg/L p-aminobenzoic acid (PABA), 2.5 mg/L pantothenic acid, both compounds, or neither, after a PA-depletion step.



The invention can be more fully understood from the following detailed description and the accompanying sequence descriptions which form a part of this application.
The following sequences conform with 37 C.F.R. 1.821-1.825 (“Requirements for Patent Applications Containing Nucleotide Sequences and/or Amino Acid Sequence Disclosures—the Sequence Rules”) and are consistent with World Intellectual Property Organization (WIPO) Standard ST.25 (2009) and the sequence listing requirements of the EPO and PCT (Rules 5.2 and 49.5 (a-bis), and Section 208 and Annex C of the Administrative Instructions). The symbols and format used for nucleotide and amino acid sequence data comply with the rules set forth in 37 C.F.R. §1.822.
SEQ ID NO:1 is the nucleotide sequence of a synthetic chimeric E. coli panE and panD operon.
SEQ ID NO:2 is the nucleotide sequence of the GI promoter from the Actinoplanes missouriensis xylose isomerase gene.
SEQ ID NO:3 is the nucleotide sequence of the E. coli panE open reading frame encoding 2-dehydropantoate reductase.
SEQ ID NO:4 is the amino acid sequence of the E. coli panE encoded 2-dehydropantoate reductase (strain K-12 substr. MG1655; gi|16128410|ref|NP — 414959.1|).
SEQ ID NO:5 is the nucleotide sequence of a stretch of DNA that is upstream from the start codon for the Z. mobilis glyceraldehyde 3-phosphate dehydrogenase gene that includes the Shine-Delgarno sequence
SEQ ID NO:6 is the nucleotide sequence of the E. coli panD open reading frame encoding aspartate 1-decarboxylase.
SEQ ID NO:7 is the amino acid sequence of the E. coli panD encoded aspartate 1-decarboxylase.
SEQ ID NO:8 is the nucleotide sequence of a stretch of DNA that corresponds to the small, stabilizing stem-loop sequence that immediately follows the xylose isomerase (xylA) stop codon in the E. coli XylA/B operon.





TABLE 1



2-dehydropantoate reductases used in first alignment







SEQ ID

Accession number
Organism
NO







gi|53803269|ref|YP_114934.1|

Methylococcus capsulatus

9

gi|78223840|ref|YP_385587.1|

Geobacter metallireducens

10


GS-15


gi|19113647|ref|NP_596855.1|

Schizosaccharomyces pombe

11

gi|6321854|ref|NP_011930.1|

Saccharomyces cerevisiae

12


S288c


gi|73538792|ref|YP_299159.1|
Ralstonia eutropha JMP134
13

gi|207722086|ref|YP_002252524.

Ralstonia solanacearum

14


MolK2


gi|194367655|ref|YP_002030265.

Stenotrophomonas

15


maltophilia R551-3


gi|29376939|ref|NP_816093.1|
Enterococcus faecalis V583
16

gi|16078575|ref|NP_389394.1|
Bacillus subtilis subsp. subtilis



str. 168]






































SEQ ID NO:18 is a representation of a conserved amino acid sequence for aspartate 1-decarboxylase showing the highly conserved amino acid positions, without notation of less conserved amino acid positions and with insertion positions omitted.
SEQ ID NO:19 is a representation of a conserved amino acid sequence for 2-dehydropantoate reductase showing the highly conserved amino acid positions, without notation of less conserved amino acid positions and with insertion positions omitted.
DETAILED DESCRIPTION
The following definitions may be used for the interpretation of the claims and specification:
As used herein, the terms “comprises,” “comprising,” “includes,” “including,” “has,” “having,” “contains” or “containing,” or any other variation thereof, are intended to cover a non-exclusive inclusion. For example, a composition, a mixture, process, method, article, or apparatus that comprises a list of elements is not necessarily limited to only those elements but may include other elements not expressly listed or inherent to such composition, mixture, process, method, article, or apparatus. Further, unless expressly stated to the contrary, “or” refers to an inclusive or and not to an exclusive or. For example, a condition A or B is satisfied by any one of the following: A is true (or present) and B is false (or not present), A is false (or not present) and B is true (or present), and both A and B are true (or present).
Also, the indefinite articles “a” and “an” preceding an element or component of the invention are intended to be nonrestrictive regarding the number of instances (i.e. occurrences) of the element or component. Therefore “a” or “an” should be read to include one or at least one, and the singular word form of the element or component also includes the plural unless the number is obviously meant to be singular.
The term “invention” or “present invention” as used herein is a non-limiting term and is not intended to refer to any single embodiment of the particular invention but encompasses all possible embodiments as described in the specification and the claims.
As used herein, the term “about” modifying the quantity of an ingredient or reactant of the invention employed refers to variation in the numerical quantity that can occur, for example, through typical measuring and liquid handling procedures used for making concentrates or use solutions in the real world; through inadvertent error in these procedures; through differences in the manufacture, source, or purity of the ingredients employed to make the compositions or carry out the methods; and the like. The term “about” also encompasses amounts that differ due to different equilibrium conditions for a composition resulting from a particular initial mixture. Whether or not modified by the term “about”, the claims include equivalents to the quantities. In one embodiment, the term “about” means within 10% of the reported numerical value, preferably within 5% of the reported numerical value.
“Gene” refers to a nucleic acid fragment that expresses a specific protein or functional RNA molecule, which may optionally include regulatory sequences preceding (5′ non-coding sequences) and following (3′ non-coding sequences) the coding sequence. “Native gene” or “wild type gene” refers to a gene as found in nature with its own regulatory sequences. “Chimeric gene” refers to any gene that is not a native gene, comprising regulatory and coding sequences that are not found together in nature. Accordingly, a chimeric gene may comprise regulatory sequences and coding sequences that are derived from different sources, or regulatory sequences and coding sequences derived from the same source, but arranged in a manner different than that found in nature. “Endogenous gene” refers to a native gene in its natural location in the genome of an organism. A “foreign” gene refers to a gene not normally found in the host organism, but that is introduced into the host organism by gene transfer. Foreign genes can comprise native genes inserted into a non-native organism, or chimeric genes.
“Promoter” or “Initiation control regions” refers to a DNA sequence capable of controlling the expression of a coding sequence or functional RNA. In general, a coding sequence is located 3′ to a promoter sequence. Promoters may be derived in their entirety from a native gene, or be composed of different elements derived from different promoters found in nature, or even comprise synthetic DNA segments. It is understood by those skilled in the art that different promoters may direct the expression of a gene in different tissues or cell types, or at different stages of development, or in response to different environmental conditions. Promoters which cause a gene to be expressed in most cell types at most times are commonly referred to as “constitutive promoters”.
The term “expression”, as used herein, refers to the transcription and stable accumulation of coding (mRNA) or functional RNA derived from a gene. Expression may also refer to translation of mRNA into a polypeptide. “Overexpression” refers to the production of a gene product in transgenic organisms that exceeds levels of production in normal or non-transformed organisms.
The term “transformation” as used herein, refers to the transfer of a nucleic acid fragment into a host organism, resulting in genetically stable inheritance. The transferred nucleic acid may be in the form of a plasmid maintained in the host cell, or some transferred nucleic acid may be integrated into the genome of the host cell. Host organisms containing the transformed nucleic acid fragments are referred to as “transgenic” or “recombinant” or “transformed” organisms.
The terms “plasmid” and “vector” as used herein, refer to an extra chromosomal element often carrying genes which are not part of the central metabolism of the cell, and usually in the form of circular double-stranded DNA molecules. Such elements may be autonomously replicating sequences, genome integrating sequences, phage or nucleotide sequences, linear or circular, of a single- or double-stranded DNA or RNA, derived from any source, in which a number of nucleotide sequences have been joined or recombined into a unique construction which is capable of introducing a promoter fragment and DNA sequence for a selected gene product along with appropriate 3′ untranslated sequence into a cell.
The term “operably linked” refers to the association of nucleic acid sequences on a single nucleic acid fragment so that the function of one is affected by the other. For example, a promoter is operably linked with a coding sequence when it is capable of affecting the expression of that coding sequence (i.e., that the coding sequence is under the transcriptional control of the promoter). Coding sequences can be operably linked to regulatory sequences in sense or antisense orientation.
The term “selectable marker” means an identifying factor, usually an antibiotic or chemical resistance gene, that is able to be selected for based upon the marker gene's effect, i.e., resistance to an antibiotic, wherein the effect is used to track the inheritance of a nucleic acid of interest and/or to identify a cell or organism that has inherited the nucleic acid of interest.
As used herein the term “codon degeneracy” refers to the nature in the genetic code permitting variation of the nucleotide sequence without affecting the amino acid sequence of an encoded polypeptide. The skilled artisan is well aware of the “codon-bias” exhibited by a specific host cell in usage of nucleotide codons to specify a given amino acid. Therefore, when synthesizing a gene for improved expression in a host cell, it is desirable to design the gene such that its frequency of codon usage approaches the frequency of preferred codon usage of the host cell.
The term “codon-optimized” as it refers to genes or coding regions of nucleic acid molecules for transformation of various hosts, refers to the alteration of codons in the gene or coding regions of the nucleic acid molecules to reflect the typical codon usage of the host organism without altering the polypeptide encoded by the DNA.
The term “carbon substrate” or “fermentable carbon substrate” refers to a carbon source capable of being metabolized by microorganisms. A type of carbon substrate is “fermentable sugars” which refers to oligosaccharides and monosaccharides that can be used as a carbon source by a microorganism in a fermentation process.
The term “lignocellulosic” refers to a composition comprising both lignin and cellulose. Lignocellulosic material may also comprise hemicellulose.
The term “cellulosic” refers to a composition comprising cellulose and additional components, which may include hemicellulose and lignin.
The term “saccharification” refers to the production of fermentable sugars from polysaccharides.
The term “pretreated biomass” means biomass that has been subjected to thermal, physical and/or chemical pretreatment to increase the availability of polysaccharides in the biomass to saccharification enzymes.
“Biomass” refers to any cellulosic or lignocellulosic material and includes materials comprising cellulose, and optionally further comprising hemicellulose, lignin, starch, oligosaccharides and/or monosaccharides. Biomass may also comprise additional components, such as protein and/or lipid. Biomass may be derived from a single source, or biomass can comprise a mixture derived from more than one source; for example, biomass could comprise a mixture of corn cobs and corn stover, or a mixture of grass and leaves. Biomass includes, but is not limited to, bioenergy crops, agricultural residues, municipal solid waste, industrial solid waste, sludge from paper manufacture, yard waste, wood and forestry waste. Examples of biomass include, but are not limited to, corn cobs, crop residues such as corn husks, corn stover, grasses, wheat, wheat straw, barley straw, hay, rice straw, switchgrass, waste paper, sugar cane bagasse, sorghum, components obtained from milling of grains, trees, branches, roots, leaves, wood chips, sawdust, shrubs and bushes, vegetables, fruits, flowers and animal manure.
“Biomass hydrolysate” refers to the product resulting from saccharification of biomass. The biomass may also be pretreated or pre-processed prior to saccharification.
The term “heterologous” means not naturally found in the location of interest. For example, a heterologous gene refers to a gene that is not naturally found in the host organism, but that is introduced into the host organism by gene transfer. For example, a heterologous nucleic acid molecule that is present in a chimeric gene is a nucleic acid molecule that is not naturally found associated with the other segments of the chimeric gene, such as the nucleic acid molecules having the coding region and promoter segments not naturally being associated with each other.
As used herein, an “isolated nucleic acid molecule” is a polymer of RNA or DNA that is single- or double-stranded, optionally containing synthetic, non-natural or altered nucleotide bases. An isolated nucleic acid molecule in the form of a polymer of DNA may be comprised of one or more segments of cDNA, genomic DNA or synthetic DNA.
A nucleic acid fragment is “hybridizable” to another nucleic acid fragment, such as a cDNA, genomic DNA, or RNA molecule, when a single-stranded form of the nucleic acid fragment can anneal to the other nucleic acid fragment under the appropriate conditions of temperature and solution ionic strength. Hybridization and washing conditions are well known and exemplified in Sambrook, J., Fritsch, E. F. and Maniatis, T. Molecular Cloning: A Laboratory Manual, 2 nd ed., Cold Spring Harbor Laboratory: Cold Spring Harbor, N.Y. (1989), particularly Chapter 11 and Table 11.1 therein (entirely incorporated herein by reference). The conditions of temperature and ionic strength determine the “stringency” of the hybridization. Stringency conditions can be adjusted to screen for moderately similar fragments (such as homologous sequences from distantly related organisms), to highly similar fragments (such as genes that duplicate functional enzymes from closely related organisms). Post-hybridization washes determine stringency conditions. One set of preferred conditions uses a series of washes starting with 6×SSC, 0.5% SDS at room temperature for 15 min, then repeated with 2×SSC, 0.5% SDS at 45° C. for 30 min, and then repeated twice with 0.2×SSC, 0.5% SDS at 50° C. for 30 min. A more preferred set of stringent conditions uses higher temperatures in which the washes are identical to those above except for the temperature of the final two 30 min washes in 0.2×SSC, 0.5% SDS was increased to 60° C. Another preferred set of highly stringent conditions uses two final washes in 0.1×SSC, 0.1% SDS at 65° C. An additional set of stringent conditions include hybridization at 0.1×SSC, 0.1% SDS, 65° C. and washes with 2×SSC, 0.1% SDS followed by 0.1×SSC, 0.1% SDS, for example.
Hybridization requires that the two nucleic acids contain complementary sequences, although depending on the stringency of the hybridization, mismatches between bases are possible. The appropriate stringency for hybridizing nucleic acids depends on the length of the nucleic acids and the degree of complementation, variables well known in the art. The greater the degree of similarity or homology between two nucleotide sequences, the greater the value of Tm for hybrids of nucleic acids having those sequences. The relative stability (corresponding to higher Tm) of nucleic acid hybridizations decreases in the following order: RNA:RNA, DNA:RNA, DNA:DNA. For hybrids of greater than 100 nucleotides in length, equations for calculating Tm have been derived (see Sambrook et al., supra, 9.50-9.51). For hybridizations with shorter nucleic acids, i.e., oligonucleotides, the position of mismatches becomes more important, and the length of the oligonucleotide determines its specificity (see Sambrook et al., supra, 11.7-11.8). In one embodiment the length for a hybridizable nucleic acid is at least about 10 nucleotides. Preferably a minimum length for a hybridizable nucleic acid is at least about 15 nucleotides; more preferably at least about 20 nucleotides; and most preferably the length is at least about 30 nucleotides. Furthermore, the skilled artisan will recognize that the temperature and wash solution salt concentration may be adjusted as necessary according to factors such as length of the probe.
The term “complementary” is used to describe the relationship between nucleotide bases that are capable of hybridizing to one another. For example, with respect to DNA, adenosine is complementary to thymine and cytosine is complementary to guanine.
The term “percent identity”, as known in the art, is a relationship between two or more polypeptide sequences or two or more polynucleotide sequences, as determined by comparing the sequences. In the art, “identity” also means the degree of sequence relatedness between polypeptide or polynucleotide sequences, as the case may be, as determined by the match between strings of such sequences. “Identity” and “similarity” can be readily calculated by known methods, including but not limited to those described in: 1.) Computational Molecular Biology (Lesk, A. M., Ed.) Oxford University: NY (1988); 2.) Biocomputing: Informatics and Genome Projects (Smith, D. W., Ed.) Academic: NY (1993); 3.) Computer Analysis of Sequence Data, Part I (Griffin, A. M., and Griffin, H. G., Eds.) Humania: NJ (1994); 4.) Sequence Analysis in Molecular Biology (von Heinje, G., Ed.) Academic (1987); and 5.) Sequence Analysis Primer (Gribskov, M. and Devereux, J., Eds.) Stockton: NY (1991).
Preferred methods to determine identity are designed to give the best match between the sequences tested. Methods to determine identity and similarity are codified in publicly available computer programs. Sequence alignments and percent identity calculations may be performed using the MegAlign program of the LASERGENE bioinformatics computing suite (DNASTAR Inc., Madison, Wis.).
Multiple alignment of the sequences is performed using the “Clustal method of alignment” which encompasses several varieties of the algorithm including the “Clustal V method of alignment” corresponding to the alignment method labeled Clustal V (described by Higgins and Sharp, CABIOS. 5:151-153 (1989); Higgins, D. G. et al., Comput. Appl. Biosci., 8:189-191 (1992)) and found in the MegAlign v8.0 program of the LASERGENE bioinformatics computing suite (DNASTAR Inc.). For multiple alignments, the default values correspond to GAP PENALTY=10 and GAP LENGTH PENALTY=10. Default parameters for pairwise alignments and calculation of percent identity of protein sequences using the Clustal method are KTUPLE=1, GAP PENALTY=3, WINDOW=5 and DIAGONALS SAVED=5. For nucleic acids these parameters are KTUPLE=2, GAP PENALTY=5, WINDOW=4 and DIAGONALS SAVED=4. After alignment of the sequences using the Clustal V program, it is possible to obtain a “percent identity” by viewing the “sequence distances” table in the same program.
Additionally the “Clustal W method of alignment” is available and corresponds to the alignment method labeled Clustal W (described by Higgins and Sharp, CABIOS. 5:151-153 (1989); Higgins, D. G. et al., Comput. Appl. Biosci. 8:189-191 (1992); Thompson, J. D. et al, Nucleic Acid Research, 22 (22): 4673-4680, 1994) and found in the MegAlign v8.0 program of the LASERGENE bioinformatics computing suite (DNASTAR Inc.). Default parameters for multiple alignment (stated as protein/nucleic acid (GAP PENALTY=10/15, GAP LENGTH PENALTY=0.2/6.66, Delay Divergen Seqs (%)=30/30, DNA Transition Weight=0.5, Protein Weight Matrix=Gonnet Series, DNA Weight Matrix=IUB). After alignment of the sequences using the Clustal W program, it is possible to obtain a “percent identity” by viewing the “sequence distances” table in the same program.
It is well understood by one skilled in the art that many levels of sequence identity are useful in identifying polypeptides, from other species, wherein such polypeptides have the same or similar function or activity. Useful examples of percent identities include, but are not limited to: 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, or 95%, or any integer percentage from 50% to 100% may be useful in identifying polypeptides of interest, such as 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99%. Suitable nucleic acid fragments not only have the above identities but typically encode a polypeptide having at least 50 amino acids, preferably at least 100 amino acids, and more preferably at least 125 amino acids.
The term “sequence analysis software” refers to any computer algorithm or software program that is useful for the analysis of nucleotide or amino acid sequences. “Sequence analysis software” may be commercially available or independently developed. Typical sequence analysis software will include, but is not limited to: 1.) the GCG suite of programs (Wisconsin Package Version 9.0, Genetics Computer Group (GCG), Madison, Wis.); 2.) BLASTP, BLASTN, BLASTX (Altschul et al., J. Mol. Biol., 215:403-410 (1990)); 3.) DNASTAR (DNASTAR, Inc. Madison, Wis.); 4.) Sequencher (Gene Codes Corporation, Ann Arbor, Mich.); and 5.) the FASTA program incorporating the Smith-Waterman algorithm (W. R. Pearson, Comput. Methods Genome Res., [Proc. Int. Symp.] (1994), Meeting Date 1992, 111-20. Editor(s): Suhai, Sandor. Plenum: New York, N.Y.). Within the context of this application it will be understood that where sequence analysis software is used for analysis, that the results of the analysis will be based on the “default values” of the program referenced, unless otherwise specified. As used herein “default values” will mean any set of values or parameters that originally load with the software when first initialized.
The term “E-value”, as known in the art of bioinformatics, is “Expect-value” which provides the probability that a match will occur by chance. It provides the statistical significance of the match to a sequence. The lower the E-value, the more significant the hit.
Standard recombinant DNA and molecular cloning techniques used herein are well known in the art and are described by Sambrook, J. and Russell, D., Molecular Cloning: A Laboratory Manual , Third Edition, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y. (2001); and by Silhavy, T. J., Bennan, M. L. and Enquist, L. W., Experiments with Gene Fusions , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y. (1984); and by Ausubel, F. M. et. al., Short Protocols in Molecular Biology, 5 th Ed. Current Protocols, John Wiley and Sons, Inc., N.Y., 2002.
Appendix 1, which is incorporated herein by reference, is a listing of Accession numbers and annotated identities of 648 2-dehydropantoate reductases of 250-350 amino acids that have an E-value of 0.00001 or smaller to the E. coli 2-dehydropantoate reductase of SEQ ID NO:4, with 95% identity and 95% overlap redundancy cutoffs.
Appendix 2, which is incorporated herein by reference, is a listing of Accession numbers and annotated identities of 693 aspartate 1-decarboxylases of 120-150 amino acids that have an E-value of 0.00001 or smaller to the E. coli aspartate 1-decarboxylase of SEQ ID NO:7, with 95% identity and 95% overlap redundancy cutoffs.
The present invention relates to engineered strains of Zymomonas that have the ability to grow without pantothenic acid (PA; also called pantothenate and vitamin B 5 ) supplementation in growth and production medium. A challenge for providing an economical process for fermentation by Zymomonas to produce ethanol is to reduce the requirement for vitamin supplementation in the medium, specifically of PA, thereby reducing the cost of growth and/or production medium. Zymomonas strains disclosed herein are genetically engineered to synthesize pantothenic acid.
Pantothenic Acid Biosynthesis
Zymomonas is known to lack the natural ability to synthesize pantothenic acid and therefore requires the presence of this vitamin in medium used for growth of this bacteria. PA is require for CoA (Coenzyme A) production, and is therefore critical for carbohydrate, protein and fatty acid metabolism.
Applicants analyzed the Zymomonas genome for the potential to encode enzymes of a pantothenic acid biosynthetic pathway. The complete sequence of the Zymomonas genome is known (Seo et al. (2005) Nat. Biotechnol. 23:63-68; NCBI Reference: NC — 006526.2) and open reading frames (ORFs) have been annotated as encoding proteins with defined function where possible, based on sequence analysis. The presence of ORFs potentially encoding enzymes that could function in a pantothenic acid biosynthetic pathway was analyzed using KEGG analysis (Kyoto Encyclopedia of Genes and Genomes; Kanehisa et al. (2002) Nucleic Acids Res. 30:42-46; Kanehisa and Goto (2000) Nucleic Acids Res. 28:27-30; Kanehisa et al. (2006) Nucleic Acids Res. 34:D354-357). KEGG provides knowledge-based methods for uncovering higher-order systemic behaviors of the cell and the organism from genomic and molecular information, as stated by KEGG.
The KEGG analysis showed that the Zymomonas genome has the potential for encoding proteins with activities for some steps in a pantothenic acid biosynthetic pathway (see FIG. 1 , bold arrows). The genome includes ORFs predicted to encode proteins with activities that may produce 2-dehydropantoate and L-aspartate. The EC group to which each enzyme activity in the pathway belongs, and in some cases the name of the gene encoding the enzyme, is shown in the pathway diagram of FIG. 1 .
No ORF was found with the potential to encode a protein with activity that would convert 2-dehydropantoate to pantoate, and no ORF was found with the potential to encode a protein with activity that would convert L-aspartate to beta-alanine. These two steps are marked with an X in the FIG. 1 diagram. Pantoate and beta-alanine are ligated together to produce pantothenic acid in a known pantothenic acid biosynthetic pathway, such as from E. coli . Pantoate-beta-alanine ligase is encoded by the panC gene in many organisms, including in E. coli . The Zymomonas genome does have the potential for encoding a pantoate-beta-alanine ligase. However, the protein encoded by the ORF annotated as panC has only 46% amino acid sequence identity with the E. coli panC gene encoded pantoate-beta-alanine ligase. With presumably no pantoate and beta-alanine substrates available in the cell, the native function of the protein encoded by the ORF annotated as panC is unknown.
Conversion of 2-dehydropantoate to pantoate in E. coli is catalyzed by 2-dehydropantoate reductase, which is encoded by the panE ORF in many organisms including in E. coli (SEQ ID NO:3). Conversion of L-aspartate to beta-alanine is catalyzed by aspartate 1-decarboxylase, which is encoded by the panD ORF in many organisms including in E. coli (SEQ ID NO:6). Whether expression of these two activities in Zymomonas cells would confer the ability to synthesize PA was unknown, since that outcome necessitates the assumption that the presumed existing native enzymes, that sequence analysis speculates can participate in PA biosynthesis, actually do encode functional enzymes that do catalyze reactions of a portion of a PA biosynthetic pathway in Zymomonas.
Upon experimental analysis as disclosed herein, Applicants have discovered that Zymomonas cells engineered for expression of the E. coli panE and panD coding regions are able to grow in medium that does not contain PA. This result suggests that said Zymomonas cells have a complete functional PA biosynthetic pathway and synthesize PA. Further, the engineered wild type Zymomonas cells grow as well in medium that does not contain PA as wild type Zymomonas cells grow in the same medium supplemented with a non-limiting amount of PA.
In the present recombinant Zymomonas bacterial strains, a nucleic acid molecule encoding a polypeptide having 2-dehydropantoate reductase activity and a nucleic acid molecule encoding a polypeptide having aspartate 1-decarboxylase activity are introduced. These polypeptides are encoded by heterologous nucleic acid molecules that are introduced into the Zymomonas cell.
Host Zymomonas Cells
Heterologous nucleic acid molecules encoding polypeptides with 2-dehydropantoate reductase activity and aspartate 1-decarboxylase activity may be introduced into any strain of Zymomonas , such as Zymomonas mobilis, to create a pantothenic acid biosynthesis pathway. Wild type Zymomonas strains naturally produce ethanol and may be used as a host for introduction of said nucleic acid molecules. In other embodiments the Zymomonas host strains are recombinant strains engineered to be improved biocatalysts for ethanol production and comprise a number of genetic modifications that enhance the production of ethanol. Host strains may be strains engineered in one or more of the following ways, in any combination. Z. mobilis strains have been engineered to utilize xylose, a sugar found in biomass hydrolysate, for ethanol production (U.S. Pat. No. 5,514,583, U.S. Pat. No. 5,712,133, WO 95/28476, Feldmann et al. (1992) Appl. Microbiol. Biotechnol. 38: 354-361, Zhang et al. (1995) Science 267:240-243). Ethanol has been produced by genetically modified Zymomonas in lignocellulosic biomass hydrolysate fermentation media (U.S. Pat. No. 7,932,063). Genetically modified strains of Z. mobilis with improved xylose utilization and/or production of ethanol are disclosed in U.S. Pat. No. 7,223,575, U.S. Pat. No. 7,741,119, U.S. Pat. No. 7,897,396, U.S. Pat. No. 7,998,722, and WO2010/075241 (US 2011/0014670), which are herein incorporated by reference. Any of the disclosed strains, including for example ATCC31821/pZB5, ZW658 (ATCC #PTA-7858), ZW800, ZW801-4, ZW801-4::ΔhimA, AcR#3, ZW705, or other ethanol-producing strains of Zymomonas , may be used as host cells for expression of heterologous nucleic acid molecules encoding a polypeptide having 2-dehydropantoate reductase activity and encoding a polypeptide having aspartate 1-decarboxylase activity, which enables pantothenic acid biosynthesis.
Enzyme Activities
Any nucleic acid molecule encoding a polypeptide having 2-dehydropantoate reductase activity may be used in the present strains. Enzymes with 2-dehydropantoate reductase activity are also called 2-dehydropantoate 2-reductase, 2-oxopantoate reductase, ketopantoate reductase, ketopantoic acid reductase, KPA reductase, and KPR. The reaction catalyzed by this enzyme activity is:

(R)-pantoate+NADP + ←→2-dehydropantoate+NADPH+H +

The 2-dehydropantoate reductase enzyme is classified as EC 1.1.1.169. A nucleic acid molecule encoding any enzyme belonging to this EC group having 2-dehydropantoate reductase activity may be used in the present strains.
Any nucleic acid molecule encoding a polypeptide having aspartate 1-decarboxylase activity may be used in the present strains. Enzymes with aspartate 1-decarboxylase activity are also called aspartate alpha-decarboxylase, L-aspartate alpha-decarboxylase, aspartic alpha-decarboxylase, L-aspartate 1-carboxy-lyase, ADC, AspDC, and Dgad2. The reaction catalyzed by this enzyme activity is:

L-aspartate←→beta-alanine+CO 2

The aspartate 1-decarboxylase enzyme is classified as EC 4.1.1.11. A nucleic acid molecule encoding any enzyme belonging to this EC group having aspartate 1-decarboxylase activity may be used in the present strains. The protein translated from the E. coli panD gene is an inactive protein called the pi-protein (Ramjee et al (1997) Biochem. J. 323:661-669). This protein is autocatalytically self-processed into two subunits (alpha and beta) that form the active enzyme.
Polypeptides with 2-dehydropantoate reductase activity or aspartate 1-decarboxylase activity may be identified using bioinformatics and/or experimental methods. Amino acid sequences of these polypeptides can be readily found by EC number, gene name, and/or enzyme name using databases that are well known to one of skill in the art including NCBI (National Center for Biotechnology Information; Bethesda, Md.), BRENDA (The Comprehensive Enzyme Information System; Technical University of Braunschweig Dept. of Bioinformatics), and Swiss-Prot (Swiss Institute of Bioinformatics; Lausanne, Switzerland). In addition, amino acid sequences of these polypeptides can be readily found based on a known sequence using bioinformatics, including sequence analysis software such as BLAST sequence analysis using for example the E. coli sequences (2-dehydropantoate reductase: SEQ ID NO:4; aspartate 1-decarboxylase: SEQ ID NO:7).
The following analysis of polypeptide sequences identified a structure that is common to 2-dehydropantoate reductases belonging to EC 1.1.1.169. First the amino acid sequences of ten 2-dehydropantoate reductases (SEQ ID NOs: 9-17 and 4) with experimentally verified function and/or characterized structure as identified in the BRENDA database (BRaunschweig ENzyme Database; Cologne University BioInformatics Center; Scheer et al. (2011) Nucleic Acids Res. 39:670-676) and the Protein Data Bank database (RCSB PDB; Berman et al. (2000) Nucleic Acids Res. 28:235-242) were aligned using Clustal W with the following parameters: Slow/Accurate Pairwise Parameters: Gap Opening=10, Gap Extend=0.1, Protein weight matrix Gonnet 250; Multiple Parameters: Gap Opening=10, Gap Extension=0.2, Protein Weight Matrix=Gonnet series. From this multiple sequence alignment, the amino acid positions with 90% to 100% conservation as a single amino acid among the ten sequences were identified and used to provide the conserved structure diagram shown in FIG. 3A . In this figure the conserved amino acids are indicated as G (glycine), L (leucine), K (lysine), N (asparagine), E (glutamic acid), S (serine), and D (aspartic acid). All of the amino acids shown are 100% conserved except the two asparagines (N) which are each 90% conserved. The dashed lines represent positions in the multiple sequence alignment where insertions and deletions, including N-terminal and C-terminal extensions, occur in one or more of the ten analyzed 2-dehydropantoate reductase amino acid sequences belonging to EC 1.1.1.169. The conserved structure of FIG. 3A is represented as a sequence in FIG. 3B (SEQ ID NO:19). In this sequence the dashed positions are omitted, and notation of other conserved amino acids, which are not as highly conserved, is omitted.
The amino acids at the conserved positions are highlighted in the E. coli 2-dehydropantoate reductase amino acid sequence (SEQ ID NO:4) in FIG. 3C and are G at position 7, G at position 9, G at position 12, L at position 19, K at position 72, N at position 98, G at position 99, K at position 176, N at position 180, N at position 184, E at position 210, S at position 244, D at position 248, and E at position 256. One of skill in the art will be readily able to align a candidate sequence with SEQ ID NO:4, allowing for extensions, insertions and deletions such as in positions indicated in the structure diagram of FIG. 3A , such that the presence of the conserved amino acids highlighted in FIG. 3C can be determined. Any polypeptide having at least 10, at least 11, at least 12, at least 13, or all 14 of these 14 conserved amino acids when compared to SEQ ID NO:4 and having 2-dehydropantoate reductase activity may be used in the present strains.
A BLAST search was performed using the E. coli 2-dehydropantoate reductase (SEQ ID NO:4) against publicly available sequences, and protein sequence matches with an E-value of 0.00001 or smaller were extracted. Matched protein sequences in the range of 250-350 amino acids were retained. Sequence redundancy was reduced to 95% identity and 95% overlap. This filtering resulted in 648 sequences, which are listed in Appendix 1 by their accession numbers. A multiple sequence alignment was performed using Clustal W with the same parameters used above. All of the amino acid positions identified above in the ten sequence alignment were also highly conserved among the 648 sequences except the L at position 19. In addition D at position 248 is replaced with S in about 4% of the sequences and the Ns at positions 180 and 184 have some variation. Thus characterization of the broader group of 2-dehydropantoate reductases provided a structure with conserved amino acids highlighted in the E. coli 2-dehydropantoate reductase amino acid sequence (SEQ ID NO:4) shown in FIG. 3D . The Ns at positions 180 and 184 are underlined but not bolded to represent some amino acid variation at those positions. At position 248, the presence of S instead of D is included in the conserved structure. The conserved amino acids are G at position 7, G at position 9, G at position 12, K at position 72, N at position 98, G at position 99, K at position 176, N at position 180, N at position 184, E at position 210, S at position 244, D or S at position 248, and E at position 256. One of skill in the art will be readily able to align a candidate sequence with SEQ ID NO:4, allowing for extensions, insertions and deletions such as in positions indicated in the structure diagram in FIG. 3A , such that the presence of the conserved amino acids of FIG. 3D can be determined. Any polypeptide having at least 10, at least 11, at least 12, or all 13 of these 13 conserved amino acids when compared to SEQ ID NO:4 and having 2-dehydropantoate reductase activity may be used in the present strains.
Nucleic acid molecules that may be used in the present strains include those encoding any protein having 2-dehydropantoate reductase activity, including for example: 1) those belonging to EC 1.1.1.169; 2) those with experimentally verified function and/or characterized structure (SEQ ID NOs: 9-17 and 4); 3) those having conserved structure of FIG. 3A , represented as a sequence in FIG. 3B (SEQ ID NO:19); 4) those having ten or more of the conserved amino acids highlighted in SEQ ID NO:4 in FIG. 3C ; 5) those with at least about 95% sequence identity to any of the 648 proteins listed in Appendix 1; and 6) those having ten or more of the conserved amino acids highlighted in SEQ ID NO:4 in FIG. 3D .
The following analysis of polypeptide sequences identified a structure that is common to aspartate 1-decarboxylases belonging to EC 4.1.1.11. A BLAST search was performed using the E. coli aspartate 1-decarboxylase (SEQ ID NO:7) against publicly available sequences, and protein sequence matches with an E-value of 0.00001 or smaller were extracted. Matched protein sequences in the range of 120-150 amino acids were retained. Sequence redundancy was reduced to 95% identity and 95% overlap. This filtering resulted in 493 sequences, which are listed in Appendix 2 by their accession numbers. A multiple sequence alignment was performed using Clustal W with the following parameters: Slow/Accurate Pairwise Parameters: Gap Opening=10, Gap Extend=0.1, Protein weight matrix Gonnet 250; Multiple Parameters: Gap Opening=10, Gap Extension=0.2, Protein Weight Matrix=Gonnet series. A sequence logo was generated by LOGO extraction using Weblogo, a publicly available web based application (Crooks et al (2004) Genome Research 14:1188-1190); Schneider and Stephens (1990) Nucleic Acids Res. 18:6097-6100). According to the provided information, each logo consists of stacks of symbols, one stack for each position in the sequence. The overall height of the stack indicates the sequence conservation at that position, while the height of symbols within the stack indicates the relative frequency of each amino or nucleic acid at that position. The percent frequency of each amino acid at each position was calculated for the set of 493 sequences.
From this analysis, the most highly conserved amino acid positions were identified as those having a single amino acid occurring in at least 99% of the 493 sequences analyzed, and were used to provide the conserved structure diagram shown in FIG. 2A . In this figure the conserved amino acids are indicated as K (lysine), H (histidine), Y (tyrosine), G (glycine), S (serine), R (arginine), T (threonine), N (asparagine), and I (isoleucine). The dashed lines represent positions in the multiple sequence alignment where insertions and deletions, including N-terminal and C-terminal extensions, occur in one or more of the aligned 493 aspartate 1-decarboxylase amino acid sequences belonging to EC 4.1.1.11. The conserved structure of FIG. 2A is represented as a sequence in FIG. 2B (SEQ ID NO:18). In this sequence the dashed positions are omitted, and notation of other conserved amino acids, which are not as highly conserved, is omitted.
The amino acids at the most highly conserved positions are highlighted in the E. coli aspartate 1-decarboxylase amino acid sequence (SEQ ID NO:7) in FIG. 2C and are K at position 9, H at position 11, Y at position 22, G at position 24, S at position 25, G at position 52, R at position 54, T at position 57, Y at position 58, N at position 72, G at position 73, and I at position 86. One of skill in the art will be readily able to align a candidate sequence with SEQ ID NO:7, allowing for extensions, insertions and deletions such as in positions indicated in the structure diagram of FIG. 2A , such that the presence of the conserved amino acids highlighted in FIG. 2C can be determined. Any polypeptide having at least 8, at least 9, at least 10, at least 11, or all 12 of these 12 conserved amino acids when compared to SEQ ID NO:7 and having aspartate 1-decarboxylase activity may be used in the present strains.
Of the 12 most highly conserved amino acid positions shown in FIG. 2B , five of these occurred in 100% of the 493 sequences aligned. These 100% conserved positions are K at position 9, Y at position 22, G at position 24, T at position 57, and Y at position 58. In one embodiment a polypeptide that may be used has all five of these 100% highly conserved amino acid positions when compared to the E. coli aspartate 1-decarboxylase amino acid sequence (SEQ ID NO:7).
Nucleic acid molecules that may be used in the present strains include those encoding any protein having aspartate 1-decarboxylase activity, including for example: 1) those belonging to EC 4.1.1.11; 2); 2) those with 95% sequence identity to the E. coli aspartate 1-decarboxylase (SEQ ID NO:7); 3) those having conserved structure of FIG. 2A , represented as a sequence in FIG. 2B (SEQ ID NO:18); 4) those having eight or more of the conserved amino acids highlighted in SEQ ID NO:7 in FIG. 2C ; 5) those having the five conserved amino acid positions K at position 9, Y at position 22, G at position 24, T at position 57, and Y at position 58, as compared to the E. coli aspartate 1-decarboxylase of SEQ ID NO:7; and 6) those with at least about 95% sequence identity to any of the 493 proteins listed in Appendix 2.
DNA sequences encoding polypeptides with 2-dehydropantoate reductase activity or aspartate 1-decarboxylase activity may also be identified using bioinformatics and/or experimental methods. Coding sequences can be found in databases including NCBI (ibid.) using gene name and/or enzyme name as is well know to one of skill in the art. Genes encoding 2-dehydropantoate reductase have multiple names, including for example panE or ApbA in E. coli , and PAN5 in Saccharomyces cerevisiae . In addition, nucleic acid sequences encoding these polypeptides can be readily found based on a known sequence using bioinformatics, including sequence analysis software such as BLAST sequence analysis using for example the E. coli sequences (2-dehydropantoate reductase: SEQ ID NO:3; aspartate 1-decarboxylase: SEQ ID NO:6). Experimental methods include those based on nucleic acid hybridization.
Nucleic acid molecules encoding 2-dehydropantoate reductase and aspartate 1-decarboxylase are found in numerous organisms including, for example, in some bacteria (excluding Zymomonas ), yeast, and plants. A coding region sequence from one of these sources, which is heterologous to Zymomonas , may be used directly or it may be optimized for expression in Zymomonas . For example, it may be codon optimized for optimal protein expression in Zymomonas , and/or introns may be removed if present in a eukaryotic coding region, both of which are well known to one skilled in the art.
Expression of Enzyme Activities
For expression, a nucleic acid molecule encoding a polypeptide having 2-dehydropantoate reductase activity and a nucleic acid molecule encoding aspartate 1-decarboxylase are each constructed in a chimeric gene with operably linked promoter and typically a termination sequence. Alternatively the coding regions are constructed as part of an operon that is operably linked to a promoter and a termination sequence. In an operon, typically a ribosome binding site is located upstream of the start codons for all open reading frames in the operon. Promoters that may be used in chimeric genes and operons are promoters that are expressed in Zymomonas cells such as the promoters of Z. mobilis glyceraldehyde-3-phosphate dehydrogenase gene (GAP promoter), Z. mobilis enolase gene (ENO promoter), and the Actinoplanes missouriensis xylose isomerase gene (GI promoter). Termination signals are also those that are expressed in the target cell.
Chimeric genes or an operon for 2-dehydropantoate reductase and aspartate 1-decarboxylase expression are typically constructed in or transferred to a vector for further manipulations. Vectors are well known in the art. Particularly useful for expression in Zymomonas are vectors that can replicate in both E. coli and Zymomonas , such as pZB188 which is described in U.S. Pat. No. 5,514,583. Vectors may include plasmids for autonomous replication in a cell, and plasmids for carrying constructs to be integrated into bacterial genomes. Plasmids for DNA integration may include transposons, regions of nucleic acid sequence homologous to the target bacterial genome, or other sequences supporting integration. An additional type of vector may be a transposome produced using, for example, a system that is commercially available from EPICENTRE®. It is well known how to choose an appropriate vector for the desired target host and the desired function.
Vectors carrying the desired coding regions are introduced into Zymomonas cells using known methods such as electroporation, freeze-thaw transformation, calcium-mediated transformation, or conjugation. The coding regions may be maintained on a plasmid in the cell, or integrated into the genome. Integration methods may be used that are well known in the art such as homologous recombination, transposon insertion, or transposome insertion. In homologous recombination, DNA sequences flanking a target integration site are placed bounding a spectinomycin-resistance gene, or other selectable marker, and the chimeric genes or operon for expression, leading to insertion of the selectable marker and the expression sequences into the target genomic site. In addition, the selectable marker may be bounded by site-specific recombination sites, so that after expression of the corresponding site-specific recombinase, the resistance gene is excised from the genome.
Transformed Zymomonas strains expressing 2-dehydropantoate reductase and aspartate 1-decarboxylase may be readily identified by their ability to grow in medium lacking PA. A wild type strain of Zymomonas mobilis engineered as described in examples herein was able to grow in minimal medium lacking PA as well as the wild type strain grew with supplementation of 2.5 mg/L PA (i.e. a saturating concentration of this vitamin). In a strain of Zymomonas mobilis previously engineered for expression of xylose utilization enzyme activities and adapted to growth on xylose (U.S. Pat. No. 7,629,156), and engineered for improved ethanol production through disruption of the endogenous glucose-fructose oxidoreductase (U.S. Pat. No. 7,741,119) gene, expressing 2-dehydropantoate reductase and aspartate 1-decarboxylase also conferred the ability to grow in minimal medium lacking PA. However supplementation with p-aminobenzoic acid (PABA) was required for growth of this strain due to disruption of the pabB gene encoding p-aminobenzoate synthase subunit I, which occurred in previous engineering steps.
Ethanol Production by Pantothenic Acid Producing Strain
The present engineered Zymomonas strain expressing 2-dehydropantoate reductase and aspartate 1-decarboxylase may be used as a biocatalyst in fermentation to produce ethanol. The Zymomonas strain is brought in contact with medium containing a carbon substrate. Typically one or more sugars provide the carbon substrate. In one embodiment the medium may be a minimal medium with no addition of a complex ingredient that contains PA such as yeast extract, or PA itself, such that the medium lacks PA. Alternatively, the medium may contain an amount of PA that is suboptimal for growth and/or production of Zymomonas strains not engineered for pantothenic acid production. In one embodiment a seed culture is grown in minimal medium lacking PA or in medium having a sub-optimal amount of PA. The seed culture is then used to inoculate a larger fermentation culture. The fermentation medium may lack PA or have a sub-optimal amount of PA. Alternatively, the fermentation medium may contain an adequate amount of PA for growth and/or production of Zymomonas strains not engineered for pantothenic acid production.
Seed culture medium and/or fermentation medium may contain biomass hydrolysate which provides mixed sugars as a carbon source, typically including glucose, xylose, and arabinose. It is desirable that the present engineered Zymomonas strain also expresses enzyme activities for utilization of xylose, or of xylose and arabinose. When the mixed sugars concentration is high such that growth is inhibited, the medium may include sorbitol, mannitol, or a mixture thereof as disclosed in U.S. Pat. No. 7,629,156. Galactitol or ribitol may replace or be combined with sorbitol or mannitol. The present Zymomonas strain grows in the medium where fermentation occurs and ethanol is produced. The fermentation is run without supplemented air, oxygen, or other gases (which may include conditions such as anaerobic, microaerobic, or microaerophilic fermentation), for at least about 24 hours, and may be run for 30 or more hours. The timing to reach maximal ethanol production is variable, depending on the fermentation conditions. Typically, if inhibitors are present in the medium, as may be present in hydrolysate medium, a longer fermentation period is required. The fermentations may be run at temperatures that are between about 30° C. and about 37° C., at a pH of about 4.5 to about 7.5.
The present Zymomonas strains may be grown in medium without PA supplementation in laboratory scale fermenters, and in scaled up fermentation where commercial quantities of ethanol are produced. Where commercial production of ethanol is desired, a variety of culture methodologies may be applied. For example, large-scale production from the present Zymomonas strains may be produced by both batch and continuous culture methodologies. A classical batch culturing method is a closed system where the composition of the medium is set at the beginning of the culture and not subjected to artificial alterations during the culturing process. Thus, at the beginning of the culturing process the medium is inoculated with the desired organism and growth or metabolic activity is permitted to occur adding nothing to the system. Typically, however, a “batch” culture is batch with respect to the addition of carbon source and attempts are often made at controlling factors such as pH and oxygen concentration.
A variation on the standard batch system is the Fed-Batch system. Fed-Batch culture processes are also suitable for growth of the present Zymomonas strains and comprise a typical batch system with the exception that the substrate is added in increments as the culture progresses. Batch and Fed-Batch culturing methods are common and well known in the art and examples may be found in Biotechnology: A Textbook of Industrial Microbiology, Crueger, Crueger, and Brock, Second Edition (1989) Sinauer Associates, Inc., Sunderland, Mass., or Deshpande, Mukund V., Appl. Biochem. Biotechnol., 36, 227, (1992), herein incorporated by reference.
Commercial production of ethanol may also be accomplished with a continuous culture. Continuous cultures are open systems where a culture medium is added continuously to a bioreactor and an equal amount of conditioned medium is removed simultaneously for processing. Continuous cultures generally maintain the cells at a constant high liquid phase density where cells are primarily in log phase growth.
Continuous or semi-continuous culture allows for the modulation of one factor or any number of factors that affect cell growth or end product concentration. For example, one method will maintain a limiting nutrient such as the carbon source or nitrogen level at a fixed rate and allow all other parameters to moderate. In other systems a number of factors affecting growth can be altered continuously while the cell concentration, measured by medium turbidity, is kept constant. Continuous systems strive to maintain steady state growth conditions and thus the cell loss due to medium being drawn off must be balanced against the cell growth rate in the culture. Methods of modulating nutrients and growth factors for continuous culture processes as well as techniques for maximizing the rate of product formation are well known in the art of industrial microbiology and a variety of methods are detailed by Brock, supra.
Ethanol may be produce in simultaneous saccharification and fermentation (SSF) where pretreated biomass is saccharified producing hydrolysate containing fermentable sugars concurrently with ethanol production by the present Zymomonas strain.
In one embodiment the present Zymomonas strain is grown in shake flasks in minimal medium lacking PA at about 30° C. to about 37° C. with shaking at about 150 rpm in orbital shakers and then transferred to a 10 L seed fermentor containing a similar medium. The seed culture is grown in the seed fermentor anaerobically until OD 600 is between 3 and 6, when it is transferred to the production fermentor where the fermentation parameters are optimized for ethanol production. Typical inoculum volumes transferred from the seed tank to the production tank range from about 2% to about 20% v/v. Typical fermentation medium contains biomass hydrolysate. A final concentration of about 5 mM sorbitol or mannitol is present in the medium. The fermentation is controlled at pH 5.0-6.0 using caustic solution (such as ammonium hydroxide, potassium hydroxide, or sodium hydroxide) and either sulfuric or phosphoric acid. The temperature of the fermentor is controlled at 30° C.-35° C. In order to minimize foaming, antifoam agents (any class—silicone based, organic based etc) are added to the vessel as needed. An antimicrobial, to which the present Zymomonas strain has tolerance, may be used optionally to minimize contamination.
Any set of conditions described above, and additionally variations in these conditions that are well known in the art, are suitable conditions for production of ethanol by a pantothenic acid producing Zymomonas strain.
EXAMPLES
The present invention is further defined in the following Examples. It should be understood that these Examples, while indicating preferred embodiments of the invention, are given by way of illustration only. From the above discussion and these Examples, one skilled in the art can ascertain the essential characteristics of this invention, and without departing from the spirit and scope thereof, can make various changes and modifications of the invention to adapt it to various uses and conditions.
General Methods
The meaning of abbreviations is as follows: “kb” means kilobase(s), “bp” means base pairs, “nts” means nucleotides, “hr” means hour(s), “min” means minute(s), “sec” means second(s), “d” means day(s), “L” means liter(s), “ml” means milliliter(s), “μL” means microliter(s), “μg” means microgram(s), “ng” means nanogram(s), “g” means gram(s), “mM” means millimolar, “μM” means micromolar, “nm” means nanometer(s), “μmol” means micromole(s), “pmol” means picomole(s), “OD” or “OD600” means optical density at 600 nm, “rpm” is revolutions per minute, “˜” means approximately.
Shake Flask Experiments with Minimal Media
Unless otherwise noted, all experiments described below were conducted in shake flasks (15-ml loosely-capped, conical shaped test tubes) using PA-depleted cells and a synthetic growth medium, MM-G5, that does not contain pantothenic acid. MM-G5 is a modified version of a minimal medium that is described in Goodman et al. ((1982) Applied and Environmental Microbiology 44:496-498). It contains 50 g/L glucose, 2 g/L KH 2 PO 4 , 1 g/L MgSO 4 (7H20) 2.5 g/L (NH 4 ) 2 SO 4 , 0.5 g/L NaCl, 50 mg/L CaCl 2 (2H 2 O), 1 mg/L Na 2 MoO 4 (2H 2 0), 5 mg/L FeSO 4 (7H 2 O), and 1 mg/L each of pyridoxine, nicotinic acid, biotin and thiamine; with the final pH brought to 5.9 with KOH, and the solution was filtered through a 0.2 μm membrane. It is also important to adjust the pH to ˜5.9 with KOH after dissolving the first five ingredients in close to the final volume of deionized water to avoid precipitation of the other components. To deplete intracellular and carryover PA, cells from agar plates or glycerol stocks were inoculated into MM-G5 medium to an OD of 0.1-0.3 and the cultures were incubated at 33° C. (˜150 rpm) until the cells stopped growing (˜14-20 hrs). However, depending on the history of the cells, the volume and density of the initial inoculum and the extent of growth that occurred during the incubation period, complete depletion of PA may require a second growth period in fresh MM-G5 medium and/or a longer incubation period. Unless stated otherwise, spectinomycin (200 μg/ml) was included in the growth media for all experiments that were performed with the plasmid-bearing strains ZW1/PanED#1 and 801/PanED#1.
Example 1
Construction of the Synthetic GipanEpanD Operon
To complete a putative pathway for pantothenic acid (PA) biosynthesis in Z. mobilis we designed a synthetic 1620 bp DNA fragment (SEQ ID NO:1) that codes for an artificial, chimeric E. coli panE and panD operon (referred to below as either the “GipanEpanD operon” or the “GI-PanED operon”). The 5′ end of the operon contains the A. missouriensis (ATCC 14538) GI promoter and there is a stretch of DNA at the 3′ end that corresponds to the small, stabilizing stem-loop sequence that immediately follows the xylose isomerase (xylA) stop codon in the E. coli XylA/B operon. The synthetic DNA fragment also has NcoI and SpeI sites at its 5′ end and NotI and EcoRI sites at its 3′ end that can be used for cloning purposes. With reference to the DNA sequence of SEQ ID NO:1, nts 23-209 (SEQ ID NO:2) correspond to the GI promoter; nts 210-1121 (SEQ ID NO:3) correspond to the E. coli panE open reading frame (Gen Bank accession number AAC73528) that codes for 2-dehydropantoate reductase; nts 1122-1139 (SEQ ID NO:5) correspond to a stretch of DNA that is upstream from the start codon for the Z. mobilis glyceraldehyde 3-phosphate dehydrogenase gene that includes the Shine-Delgarno sequence; nts 1140-1520 (SEQ ID NO:6) correspond to the E. coli panD open reading frame (Gen Bank accession no. AAC73242) that codes for aspartate 1-decarboxylase; and nts 1543-1577 (SEQ ID NO:8) correspond to the stabilizing xylA stem-loop structure described above. The GI-PanED operon DNA fragment was synthesized by Genescript (Piscataway, N.J.).
Example 2
Construction of the Shuttle Vector Used for GI-PanED Operon Expression in Z. mobilis , and Generation of PanED Strains
To introduce the GI-PanED operon into Z. mobilis , the synthetic DNA molecule described above was digested with NcoI and NotI, and the resulting fragment was ligated into the unique NcoI and NotI sites of the plasmid shuttle vector pZB188/aadA. As described in US 2009-0246876 A1, which is herein incorporated by reference, pZB188/aadA is vector pZB188 described in U.S. Pat. No. 5,514,583, which is herein incorporated by reference, which is able to replicate in Z. mobilis and E. coli since it has origins of replication for both bacterial species, with an added spectinomycin resistance DNA fragment. To generate non-methylated plasmid DNA for transformation of Z. mobilis , pZB188/aadA-GlpanEpanD was introduced into chemically competent E. coli SCS110 cells (Stratagene, San Diego, Calif.), and transformants were selected on LB medium that contained spectinomycin (100 μg/ml). Isolated non-methylated plasmid DNA was then electroporated into ZW1 (ATCC #31821) and ZW801-4. A detailed description of the construction of the xylose-utilizing recombinant strain, ZW801-4, starting from the wild type parent strain, ZW1, is provided in U.S. Pat. No. 7,741,084, which is herein incorporated by reference. Strain ZW801-4 was derived from strain ZW800, which was derived from strain ZW658, all as described in U.S. Pat. No. 7,741,084. ZW658 was constructed by integrating two operons, P gap xylAB and P gap taltkt, containing four xylose-utilizing genes encoding xylose isomerase (xylA), xylulokinase (xylB), transaldolase (tal), and transketolase (tkt), into the genome of ZW1 (rename of strain ZM4; ATCC #31821) via sequential transposition events to produce strain X13L3, which was renamed ZW641, and followed by adaptation on selective media containing xylose. ZW658 was deposited under the Budapest Treaty as ATCC #PTA-7858. In ZW658, the gene encoding glucose-fructose oxidoreductase was insertionally-inactivated using host-mediated, double-crossover, homologous recombination and spectinomycin resistance as a selectable marker to create strain ZW800. The spectinomycin resistance marker, which was bounded by loxP sites, was removed by site specific recombination using Cre recombinase to create strain ZW801-4. As disclosed in commonly owned and co-pending US Patent Application Publication #US 20090246846, which is herein incorporated by reference, ZW648 has much more xylose isomerase activity (about 4-fold higher) than ZW641 (represented by X13bC strain) due to a point mutation in the promoter (Pgap) that drives expression of the xylA coding region.
Transformants were selected on agar plates that contained mRM3-G5 media (50 g/L glucose, 10 g/L yeast extract (contains PA), 2 g/L KH 2 PO 4 , 1 g/L MgSO 4 ) and 200 μg/ml of spectinomycin. The resulting ZW1 and ZW801-4 strains that harbor the pZB188/aadA-GlpanEpanD shuttle vector were named ZW1/PanED #1 and 801/PanED #1, respectively. It should be noted that two primary transformants for each strain were evaluated in the shake flask experiments described below. Since both transformants behaved essentially the same in both cases, only the results that were obtained with ZW1/PanED#1 and 801/PanED#1 are presented below.
Example 3
Growth of ZW1 in MM-G5 Medium Requires PA Supplementation
The ZW1 strain from an mRM3-G5 plate that contained 50 g/L glucose, 10 g/L yeast extract, 2 g/L KH 2 PO4, 1 g/L MgSO 2 and 1.5% agar was inoculated into 20 ml of MM-G5 (described in General Methods) and the culture was incubated for ˜19 hours at 33° C. (150 rpm) to deplete carryover pantothenic acid. The OD600 increased from 0.178 to 0.408 during the incubation period. An aliquot of the PA-depleted cells was then diluted with fresh MM-G5 medium to an OD600 of 0.035, and 10-ml aliquots of the resulting culture were distributed to eight 15-ml conical test tubes that contained various amounts of pantothenic acid (0, 0.025, 0.063, 0.125, 0.25, 0.63, 2.5, or 5 mg/L, final concentrations). After this step the eight cultures were incubated at 33° C. at 150 rpm, and growth was monitored by following changes in optical density (OD) at 600 nm as a function of time. As shown in FIG. 4 , both the exponential growth rate and maximum cell density increased in a dose related manner with increasing concentrations of pantothenic acid until saturation was achieved and growth was no longer limited by this vitamin. It was clear from this experiment that a concentration of ˜2.5 mg/L PA or higher is able to support maximum growth of ZW1 in MM-G5 medium under the conditions employed. Growth was not observed unless the cells were supplemented with pantothenic acid.
Example 4
Effect of the Synthetic GI-PanED Operon in ZW1
Growth curves for ZW1 and ZW1/PanED #1 in the presence and absence of supplemented pantothenic acid were assayed. The protocol for this experiment was as follows. Two 10-ml MM-G5 cultures were started for each of strains ZW1 and ZW1/PanED #1. One was supplemented with PA (2.5 mg/L) while the other received an equivalent volume of sterile water. The initial ODs for all four cultures were ˜0.1. After a 15-hr incubation period at 33° C. (150 rpm), aliquots of these cultures were used to start new 10-ml cultures that contained the same growth media as the original cultures; the initial OD was ˜0.05 in all cases. The new cultures were incubated at 33° C. (150 rpm) and growth was monitored by OD600. The resulting exponential growth curves are shown in FIG. 5 .
Consistent with previous results, when ZW1 was depleted of pantothenic acid in MM-G5 medium and then transferred to fresh medium that had the same composition, it failed to grow ( FIG. 5A ). In contrast, when ZW1 was transferred to medium that contained 2.5 mg/L of pantothenic acid, the cells grew exponentially with a doubling time of about 2 hours to a final OD of ˜1.2 ( FIG. 5A ). Very different results were obtained with the ZW1 derivative that contains the synthetic GI-PanED operon. As shown in FIG. 5B , ZW1/PanED#1 (ZED#1) grew with the same kinetics in MM-G5 medium in the presence or absence of supplemented PA. Indeed, both growth curves for this strain were virtually identical to the growth curve for ZW1 when a saturating concentration of PA was present. These results clearly demonstrate that with introduction of panE and panD genes Zymomonas was able to synthesize PA, and PA was made in an amount sufficient to support the maximum growth rate in minimal medium lacking PA.
Example 5
Effect of the Synthetic GI-PanED Operon in ZW801-4
ZW801-4 has two vitamin requirements for growth in minimal medium. Growth experiments using ZW801-4 were carried out as described in General Methods and the resulting growth curves are shown in FIG. 6 . As seen in FIG. 6A , when ZW801-4 was depleted of pantothenic acid in MM-G5 and transferred to the same medium it failed to grow, similar to the results that were obtained with ZW1. However, very little growth was also observed when pantothenic acid (2.5 mg/L) was added to the growth medium during the second incubation period ( FIG. 6A ). There is a genetic basis for this observation that is related to strain construction. Like other ZW641 derivatives, ZW801-4 cannot synthesize p-aminobenzoic acid (PABA), which is a vitamin that is required for folic acid biosynthesis and hence is essential. As described in U.S. Pat. No. 7,741,084, the first step in the construction of ZW641 was the integration of a synthetic P gap taltkt operon (encoding E. coli transaldolase and transketolase under the control of the Z. mobilis P gap promoter) into the ZW1 chromosome. The operon was introduced by a transposon that randomly integrates into DNA, and the transposon insertion site for the strain that was selected for further metabolic engineering is in the open reading frame of the Z. mobilis pabB gene that codes for p-aminobenzoate synthase, subunit I, which is required for biosynthesis of PABA. The P gap taltkt transposon insert is located between nts 102021 and 102022 of GenBank accession number AE008692, as determined by whole genome DNA sequence analysis. Since the disrupted pabB gene does not appear to be functional, ZW641 and all strains that were derived from it require two vitamins for growth in minimal media, namely PA and PABA.
A titration experiment was conducted with ZW801-4 to determine the optimal concentration of PA for growth of in MM-G5 medium that contains a saturating concentration of PABA (15 mg/L; FIG. 6B ). Strain ZW801-4 cells were inoculated into 20 ml of MM-G5 medium and the culture was incubated for ˜19 hours at 33° C. (150 rpm) to deplete intracellular and carryover pantothenic acid. During the incubation period the OD increased from 0.143 to 0.364. The PA-depleted culture was then diluted with MM-G5 medium to an OD of ˜0.035 and PABA was added to a final concentration of 15 mg/L. Aliquots (10 ml) of the cell suspension were distributed to eight 15-ml conical tubes that contained various concentrations of PA (ranging from 0-5 mg/L), and the resulting cultures were incubated at 33° C. (150 rpm) to monitor growth. As shown in FIG. 6B , the optimal concentration of PA for growth of ZW801-4 in MM-G5 medium that contains a saturating concentration of PABA was ˜2.5 mg/L, similar to the requirement for ZW1 ( FIG. 4 ).
GI-PanED Operon in ZW801-4
Each of strains ZW801-4 and ZW801-4/PanED#1 was inoculated into 10 ml of MM-G5 and the cultures were incubated at 33° C. for 15 hrs to deplete pantothenic acid and partially deplete PABA; the initial OD was ˜0.1 in both cases. Following this step the cultures were diluted with the same growth medium to an OD of ˜0.04, and quadruplicate 10-ml aliquots of each cell suspension were distributed to eight 15-ml conical tubes. The tubes were then supplemented with PA, PABA both vitamins, or neither, and the resulting cultures were incubated at 33° C. to monitor growth at 600 nm. The final concentrations of PA and PABA when present were 2.5 mg/L and 15 mg/L, respectively, and the no vitamin control cultures received an equivalent volume of sterile water. The resulting growth curves are shown in FIG. 7 .
Consistent with previous results, ZW801-4 only grew when PA and PABA were both added to the growth medium ( FIG. 7A ). The small amount of growth that occurred in the culture that was only supplemented with PA is the result of carryover PABA, since there is always a small amount of residual PABA after the PA-depletion step during the first incubation period in MM-G5 medium (i.e. the cells use up all the PA before they run out of PABA). In contrast to the above results, the ZW801-4 strain that contained the synthetic GI-PanED operon only required PABA for growth ( FIG. 7B )) since it was able to synthesize pantothenic acid.
Note that the ZW801-4 culture that was supplemented with both vitamins grew slightly better in MM-G5 medium than the corresponding culture of ZW801-4/PanED#1 ( FIG. 7A versus 7 B). The most likely explanation for this result is “plasmid burden”, which is often observed with Z. mobilis and other bacterial strains (Kim et al, (2000) Applied and Environmental Microbiology 66:186-193 and references therein). This phenomenon, whereby energy that would otherwise be available for growth is diverted to plasmid replication and maintenance, would likely be far more pronounced in minimal medium compared to rich medium.
The key finding in this experiment is that ZW801-4/PanED#1 grew with the same kinetics and to the same cell density in the presence and absence of added pantothenic acid when the growth medium contained a saturating concentration of PABA. Taken together the above results clearly indicate that co-expression of the E. coli panE and panD coding regions in wild type and recombinant strains of Z. mobilis allowed growth under conditions where pantothenic acid was limiting.
APPENDIX 1
Polypeptides of 250-350 Amino Acids with E Value of 0.00001 or Smaller to SEQ ID NQ:4 with 95% Identity and 95% Overlap Redundancy Cut-offs


>gi|16128410|ref|NP — 414959.1| 2-dehydropantoate reductase, NADPH-specific [ Escherichia coli str. K-12 substr MG1655]
>gi|126031569|pdb|2OFP|A Chain A, Crystal Structure Of Escherichia Coli Ketopantoate Reductase In A Ternary Complex With Nadp+ And Pantoate
>gi|157146959|ref|YP — 001454278.1| 2-dehydropantoate 2-reductase [ Citrobacter koseri ATCC BAA-895]
>gi|168232408|ref|ZP — 02657466.1| 2-dehydropantoate 2-reductase [ Salmonella enterica subsp. enterica serovar Kentucky str. CDC 191]
>gi|283764244|ref|YP — 003364109.1| 2-dehydropantoate 2-reductase [ Citrobacter rodentium ICC168]
>gi|283834256|ref|ZP — 06353997.1| 2-dehydropantoate 2-reductase [ Citrobacter youngae ATCC 29220]
>gi|261341017|ref|ZP — 05968875.1| 2-dehydropantoate 2-reductase [ Enterobacter cancerogenus ATCC 35316]
>gi|296101546|ref|YP — 003611692.1| 2-dehydropantoate 2-reductase [ Enterobacter cloacae subsp. cloacae ATCC 13047]
>gi|146310553|ref|YP — 001175627.1| 2-dehydropantoate 2-reductase [ Enterobacter sp. 638]
>gi|206579053|ref|YP — 002240106.1| 2-dehydropantoate 2-reductase [ Klebsiella pneumoniae 342]
>gi|161615377|ref|YP — 001589342.1| hypothetical protein SPAB — 03148 [ Salmonella enterica subsp. enterica serovar Paratyphi B str. SPB7]
>gi|311280686|ref|YP — 003942917.1| 2-dehydropantoate 2-reductase [ Enterobacter cloacae SCF1]
>gi|493074|gb|AAA56681.1| ApbA protein [ Salmonella enterica subsp. enterica serovar Typhimurium]
>gi|260596793|ref|YP — 003209364.1| 2-dehydropantoate 2-reductase [ Cronobacter turicensis z3032]
>gi|156935026|ref|YP — 001438942.1| hypothetical protein ESA — 02877 [ Cronobacter sakazakii ATCC BAA-894]
>gi|188534647|ref|YP — 001908444.1| 2-dehydropantoate 2-reductase (KPA reductase) [ Erwinia tasmaniensis Et1/99]
>gi|157369326|ref|YP — 001477315.1| 2-dehydropantoate 2-reductase [ Serratia proteamaculans 568]
>gi|259909271|ref|YP — 002649627.1| 2-dehydropantoate 2-reductase (KPA reductase) [ Erwinia pyrifoliae Ep1/96]
>gi|317047160|ref|YP — 004114808.1| 2-dehydropantoate 2-reductase [ Pantoea sp. At-9b]
>gi|270263558|ref|ZP — 06191827.1| 2-dehydropantoate 2-reductase [ Serratia odorifera 4Rx13]
>gi|304395487|ref|ZP — 07377370.1| 2-dehydropantoate 2-reductase [ Pantoea sp. aB]
>gi|300715579|ref|YP — 003740382.1| 2-dehydropantoate 2-reductase (KPA reductase) [ Erwinia billingiae Eb661]
>gi|293392557|ref|ZP — 06636877.1| 2-dehydropantoate 2-reductase [ Serratia odorifera DSM 4582]
>gi|318604615|emb|CBY26113.1| 2-dehydropantoate 2-reductase [ Yersinia enterocolitica subsp. palearctica Y11]
>gi|238754221|ref|ZP — 04615578.1| 2-dehydropantoate 2-reductase [ Yersinia ruckeri ATCC 29473]
>gi|238783622|ref|ZP — 04627643.1| 2-dehydropantoate 2-reductase [ Yersinia bercovieri ATCC 43970]
>gi|238750992|ref|ZP — 04612488.1| 2-dehydropantoate 2-reductase [ Yersinia rohdei ATCC 43380]
>gi|238791418|ref|ZP — 04635056.1| 2-dehydropantoate 2-reductase [ Yersinia intermedia ATCC 29909]
>gi|22124921|ref|NP — 668344.1| 2-dehydropantoate 2-reductase [ Yersinia pestis KIM 10]
>gi|291616534|ref|YP — 003519276.1| PanE [ Pantoea ananatis LMG 20103]
>gi|227113453|ref|ZP — 03827109.1| 2-dehydropantoate 2-reductase [ Pectobacterium carotovorum subsp. brasiliensis PBR1692]
>gi|261822519|ref|YP — 003260625.1| 2-dehydropantoate 2-reductase [ Pectobacterium wasabiae WPP163]
>gi|238759275|ref|ZP — 04620442.1| 2-dehydropantoate 2-reductase [ Yersinia aldovae ATCC 35236]
>gi|271499585|ref|YP — 003332610.1| 2-dehydropantoate 2-reductase [ Dickeya dadantii Ech586]
>gi|322834061|ref|YP — 004214068.1| 2-dehydropantoate 2-reductase [ Rahnella sp. Y9602]
>gi|317492927|ref|ZP — 07951351.1| 2-dehydropantoate 2-reductase [ Enterobacteriaceae bacterium 9 — 2 — 54FAA]
>gi|307129910|ref|YP — 003881926.1| 2-dehydropantoate reductase, NADPH-specific [ Dickeya dadantii 3937]
>gi|251790660|ref|YP — 003005381.1| 2-dehydropantoate 2-reductase [ Dickeya zeae Ech1591]
>gi|242240305|ref|YP — 002988486.1| 2-dehydropantoate 2-reductase [ Dickeya dadantii Ech703]
>gi|269138340|ref|YP — 003295040.1| 2-dehydropantoate 2-reductase [ Edwardsiella tarda EIB202]
>gi|85058639|ref|YP — 454341.1| 2-dehydropantoate 2-reductase [ Sodalis glossinidius str. ‘morsitans’]
>gi|290474680|ref|YP — 003467560.1| 2-dehydropantoate reductase [ Xenorhabdus bovienii SS-2004]
>gi|294635317|ref|ZP — 06713814.1| 2-dehydropantoate 2-reductase [ Edwardsiella tarda ATCC 23685]
>gi|300722004|ref|YP — 003711284.1| 2-dehydropantoate reductase, NADPH-specific, alternative pyrimidine biosynthesis [ Xenorhabdus nematophila ATCC 19061]
>gi|253990908|ref|YP — 003042264.1| 2-dehydropantoate 2-reductase [ Photorhabdus asymbiotica subsp. asymbiotica ATCC 43949]
>gi|268592049|ref|ZP — 06126270.1| 2-dehydropantoate 2-reductase [ Providencia rettgeri DSM 1131]
>gi|261346377|ref|ZP — 05974021.1| 2-dehydropantoate 2-reductase [ Providencia rustigianii DSM 4541]
>gi|37527742|ref|NP — 931087.1| 2-dehydropantoate 2-reductase [ Photorhabdus luminescens subsp. laumondii TTO1]
>gi|226329087|ref|ZP — 03804605.1| hypothetical protein PROPEN — 02990 [ Proteus penneri ATCC 35198]
>gi|183601047|ref|ZP — 02962540.1| hypothetical protein PROSTU — 04668 [ Providencia stuartii ATCC 25827]
>gi|212709183|ref|ZP — 03317311.1| hypothetical protein PROVALCAL — 00216 [ Providencia alcalifaciens DSM 30120]
>gi|227358117|ref|ZP — 03842458.1| 2-dehydropantoate 2-reductase [ Proteus mirabilis ATCC 29906]
>gi|94677011|ref|YP — 588722.1| 2-dehydropantoate 2-reductase [ baumannia cicadellinicola str. Hc ( Homalodisca coagulata )]
>gi|32490895|ref|NP — 871149.1| hypothetical protein WGLp146 [ Wigglesworthia glossinidia endosymbiont of Glossina brevipalpis]
>gi|292493929|ref|YP — 003533073.1| 2-dehydropantoate 2-reductase [ Candidatus Riesia pediculicola USDA]
>gi|89073146|ref|ZP — 01159685.1| 2-dehydropantoate 2-reductase [ Photobacterium sp. SKA34]
>gi|90579842|ref|ZP — 01235650.1| 2-dehydropantoate 2-reductase [ Vibrio angustum S14]
>gi|90410911|ref|ZP — 01218925.1| 2-dehydropantoate 2-reductase [ Photobacterium profundum 3TCK]
>gi|54308007|ref|YP — 129027.1| 2-dehydropantoate 2-reductase [ Photobacterium profundum SS9]
>gi|323491692|ref|ZP — 08096870.1| 2-dehydropantoate 2-reductase [ Vibrio brasillensis LMG 20546]
>gi|148979964|ref|ZP — 01815804.1| 2-dehydropantoate 2-reductase [ Vibrionales bacterium SWAT-3]
>gi|153217426|ref|ZP — 01951177.1| 2-dehydropantoate 2-reductase [ Vibrio cholerae 1567]
>gi|91223419|ref|ZP — 01258684.1| 2-dehydropantoate 2-reductase [ Vibrio alginolyticus 12G01]
>gi|28899137|ref|NP — 798742.1| 2-dehydropantoate 2-reductase [ Vibrio parahaemolyticus RIMD 2210633]
>gi|229521149|ref|ZP — 04410569.1| 2-dehydropantoate 2-reductase [ Vibrio cholerae TM 11079-80]
>gi|153825996|ref|ZP — 01978663.1| 2-dehydropantoate 2-reductase [ Vibrio cholerae MZO-2]
>gi|229513947|ref|ZP — 04403409.1| 2-dehydropantoate 2-reductase [ Vibrio cholerae TMA 21]
>gi|261211422|ref|ZP — 05925710.1| 2-dehydropantoate 2-reductase [ Vibrio sp. RC341]
>gi|197335509|ref|YP — 002155481.1| 2-dehydropantoate 2-reductase [ Vibrio fischeri MJ11]
>gi|258620951|ref|ZP — 05715985.1| 2-dehydropantoate 2-reductase [ Vibrio mimicus VM573]
>gi|59711325|ref|YP — 204101.1| 2-dehydropantoate 2-reductase [ Vibrio fischeri ES114]
>gi|319999267|gb|AAO10217.2| 2-dehydropantoate 2-reductase [ Vibrio vulnificus]
>gi|258627307|ref|ZP — 05722091.1| 2-dehydropantoate 2-reductase [ Vibrio mimicus VM603]
>gi|84388932|ref|ZP — 00991140.1| 2-dehydropantoate 2-reductase [ Vibrio splendidus 12B01]
>gi|269103241|ref|ZP — 06155936.1| 2-dehydropantoate 2-reductase [ Photobacterium damselae subsp. damselae CIP 102761]
>gi|269960517|ref|ZP — 06174889.1| conserved hypothetical protein [ Vibrio harveyi 1DA3]
>gi|297580947|ref|ZP — 06942872.1| 2-dehydropantoate 2-reductase [ Vibrio cholerae RC385]
>gi|209694510|ref|YP — 002262438.1| 2-dehydropantoate 2-reductase [ Aliivibria salmonicida LFI1238]
>gi|163802380|ref|ZP — 02196274.1| 2-dehydropantoate 2-reductase [ Vibrio sp. AND4]
>gi|260773428|ref|ZP — 05882344.1| 2-dehydropantoate 2-reductase [ Vibrio metschnikovii CIP 69.14]
>gi|153833983|ref|ZP — 01986650.1| 2-dehydropantoate 2-reductase [ Vibrio harveyi HY01]
>gi|149189154|ref|ZP — 01867442.1| 2-dehydropantoate 2-reductase [ Vibrio shilonii AK1]
>gi|260775331|ref|ZP — 05884228.1| 2-dehydropantoate 2-reductase [ Vibrio coralliilyticus ATCC BAA-450]
>gi|261253775|ref|ZP — 05946348.1| 2-dehydropantoate 2-reductase [ Vibrio orientalis CIP 102891]
>gi|312884367|ref|ZP — 07744073.1| 2-dehydropantoate 2-reductase [ Vibrio caribbenthicus ATCC BAA-2122]
>gi|156975556|ref|YP — 001446463.1| 2-dehydropantoate 2-reductase [ Vibrio harveyi ATCC BAA-1116]
>gi|218708705|ref|YP — 002416326.1| 2-dehydropantoate 2-reductase [ Vibrio splendidus LGP32]
>gi|308125784|ref|ZP — 05777325.2| 2-dehydropantoate 2-reductase [ Vibrio parahaemolyticus K5030]
>gi|323497930|ref|ZP — 08102939.1| 2-dehydropantoate 2-reductase [ Vibrio sinaloensis DSM 21326]
>gi|315181023|gb|ADT87937.1| 2-dehydropantoate 2-reductase [ Vibrio furnissii NCTC 11218]
>gi|86145667|ref|ZP — 01063997.1| 2-dehydropantoate 2-reductase [ Vibrio sp. MED222]
>gi|237807568|ref|YP — 002892008.1| 2-dehydropantoate 2-reductase [ Tolumonas auensis DSM 9187]
>gi|254507837|ref|ZP — 05119967.1| 2-dehydropantoate 2-reductase [ Vibrio parahaemolyticus 16]
>gi|145300108|ref|YP — 001142949.1| 2-dehydropantoate 2-reductase [ Aeromonas salmonicida subsp. salmonicida A449]
>gi|117618856|ref|YP — 855669.1| 2-dehydropantoate 2-reductase [ Aeromonas hydrophila subsp. hydrophila ATCC 7966]
>gi|109897687|ref|YP — 660942.1| 2-dehydropantoate 2-reductase [ Pseudoalteromonas atlantica T6c]
>gi|167625112|ref|YP — 001675406.1| 2-dehydropantoate 2-reductase [ Shewanella halifaxensis HAW-EB4]
>gi|149911104|ref|ZP — 01899731.1| 2-dehydropantoate 2-reductase [ Moritella sp. PE36]
>gi|254480183|ref|ZP — 05093431.1| 2-dehydropantoate 2-reductase [marine gamma proteobacterium HTCC2148]
>gi|116052432|ref|YP — 792743.1| 2-dehydropantoate 2-reductase [ Pseudomonas aeruginosa UCBPP-PA14]
>gi|221134751|ref|ZP — 03561054.1| 2-dehydropantoate 2-reductase [ Glaciecola sp. HTCC2999]
>gi|157962933|ref|YP — 001502967.1| 2-dehydropantoate 2-reductase [ Shewanella pealeana ATCC 700345]
>gi|157376577|ref|YP — 001475177.1| 2-dehydropantoate 2-reductase [ Shewanella sediminis HAW-EB3]
>gi|294142129|ref|YP — 003558107.1| 2-dehydropantoate 2-reductase [ Shewanella violacea DSS12]
>gi|90409046|ref|ZP — 01217173.1| ketopantoate reductase [ Psychromonas sp. CNPT3]
>gi|120553890|ref|YP — 958241.1| 2-dehydropantoate 2-reductase [ Marinobacter aquaeolei VT8]
>gi|153002110|ref|YP — 001367791.1| 2-dehydropantoate 2-reductase [ Shewanella baltica OS185]
>gi|104783439|ref|YP — 609937.1| 2-dehydropantoate 2-reductase [ Pseudomonas entomophila L48]
>gi|163750766|ref|ZP — 02158001.1| 2-dehydropantoate 2-reductase [ Shewanella benthica KT99]
>gi|71278126|ref|YP — 267839.1| 2-dehydropantoate 2-reductase [ Colwellia psychrerythraea 34H]
>gi|152984521|ref|YP — 001350304.1| 2-dehydropantoate 2-reductase [ Pseudomonas aeruginosa PA7]
>gi|146291921|ref|YP — 001182345.1| 2-dehydropantoate 2-reductase [ Shewanella putrefaciens CN-32]
>gi|307304742|ref|ZP — 07584492.1| 2-dehydropantoate 2-reductase [ Shewanella baltica BA175]
>gi|196157569|ref|YP — 002127058.1| 2-dehydropantoate 2-reductase [ Alteromonas macleodii ‘Deep ecotype’]
>gi|146283482|ref|YP — 001173635.1| 2-dehydropantoate 2-reductase [ Pseudomonas stutzeri A1501]
>gi|226943468|ref|YP — 002798541.1| 2-dehydropantoate 2-reductase [ Azotobacter vinelandii DJ]
>gi|229592315|ref|YP — 002874434.1| 2-dehydropantoate 2-reductase [ Pseudomonas fluorescens SBW25]
>gi|126667530|ref|ZP — 01736500.1| 2-dehydropantoate 2-reductase [ Marinobacter sp. ELB17]
>gi|148549578|ref|YP — 001269680.1| 2-dehydropantoate 2-reductase [ Pseudomonas putida F1]
>gi|312962772|ref|ZP — 07777260.1| ketopantoate reductase ApbA [ Pseudomonas fluorescens WH6]
>gi|77460643|ref|YP — 350150.1| 2-dehydropantoate 2-reductase [ Pseudomonas fluorescens Pf0-1]
>gi|91792130|ref|YP — 561781.1| 2-dehydropantoate 2-reductase [ Shewanella denitrificans OS217]
>gi|167035489|ref|YP — 001670720.1| 2-dehydropantoate 2-reductase [ Pseudomonas putida GB-1]
>gi|89093977|ref|ZP — 01166922.1| 2-dehydropantoate 2-reductase [ Oceanospirillum sp. MED92]
>gi|324101840|gb|EGB99375.1| 2-dehydropantoate 2-reductase [ Pseudomonas sp. TJI-51]
>gi|83644750|ref|YP — 433185.1| 2-dehydropantoate 2-reductase [ Hahella chejuensis KCTC 2396]
>gi|146305972|ref|YP — 001186437.1| 2-dehydropantoate 2-reductase [ Pseudomonas mendocina ymp]
>gi|170727979|ref|YP — 001762005.1| 2-dehydropantoate 2-reductase [ Shewanella woodyi ATCC 51908]
>gi|170720144|ref|YP — 001747832.1| 2-dehydropantoate 2-reductase [ Pseudomonas putida W619]
>gi|113971493|ref|YP — 735286.1| 2-dehydropantoate 2-reductase [ Shewanella sp. MR-4]
>gi|119945922|ref|YP — 943602.1| 2-dehydropantoate 2-reductase [ Psychromonas ingrahamii 37]
>gi|288573554|ref|ZP — 06391911.1| 2-dehydropantoate 2-reductase [ Dethiosulfovibrio peptidovorans DSM 11002]
>gi|117919232|ref|YP — 868424.1| 2-dehydropantoate 2-reductase [ Shewanella sp. ANA-3]
>gi|311694203|gb|ADP97076.1| 2-dehydropantoate 2-reductase [marine bacterium HP15]
>gi|149378127|ref|ZP — 01895846.1| 2-dehydropantoate 2-reductase [ Marinobacter algicola DG893]
>gi|253576112|ref|ZP — 04853444.1| 2-dehydropantoate 2-reductase [ Paenibacillus sp. oral taxon 786 str. D14]
>gi|70732101|ref|YP — 261857.1| 2-dehydropantoate 2-reductase [ Pseudomonas fluorescens Pf-5]
>gi|304310467|ref|YP — 003810065.1| 2-dehydropantoate 2-reductase [ Ketopantoate reductase)/gamma proteobacterium HdN1]
>gi|212634008|ref|YP — 002310533.1| 2-dehydropantoate 2-reductase [ Shewanella piezotolerans WP3]
>gi|302189612|ref|ZP — 07266285.1| 2-dehydropantoate 2-reductase [ Pseudomonas syringae pv. syringae 642]
>gi|288931618|ref|YP — 003435678.1| 2-dehydropantoate 2-reductase [ Ferroglobus placidus DSM 10642]
>gi|127513823|ref|YP — 001095020.1| 2-dehydropantoate 2-reductase [ Shewanella loihica PV-4]
>gi|24375310|ref|NP — 719353.1| 2-dehydropantoate 2-reductase [ Shewanella oneidensis MR-1]
>gi|254515212|ref|ZP — 05127273.1| 2-dehydropantoate 2-reductase [gamma proteobacterium NOR5-3]
>gi|237799306|ref|ZP — 04587767.1| 2-dehydropantoate 2-reductase [ Pseudomonas syringae pv. oryzae str. 1 — 6]
>gi|294101101|ref|YP — 003552959.1| 2-dehydropantoate 2-reductase [ Aminobacterium colombiense DSM 12261]
>gi|119468495|ref|ZP — 01611586.1| putative 2-dehydropantoate reductase [ Alteromonadales bacterium TW-7]
>gi|312879258|ref|ZP — 07739058.1| 2-dehydropantoate 2-reductase [ Aminomonas paucivorans DSM 12260]
>gi|28871529|ref|NP — 794148.1| 2-dehydropantoate 2-reductase [ Pseudomonas syringae pv. tomato str. DC3000]
>gi|298488549|ref|ZP — 07006579.1| 2-dehydropantoate 2-reductase [ Pseudomonas savastanoi pv. savastanoi NCPPB 3335]
>gi|114561913|ref|YP — 749426.1| 2-dehydropantoate 2-reductase [ Shewanella frigidimarina NCIMB 400]
>gi|119477336|ref|ZP — 01617527.1| 2-dehydropantoate 2-reductase [marine gamma proteobacterium HTCC2143]
>gi|282165330|ref|YP — 003357715.1| 2-dehydropantoate 2-reductase [ Methanocella paludicola SANAE]
>gi|94502098|ref|ZP — 01308601.1| 2-dehydropantoate 2-reductase [ Oceanobacter sp. RED65]
>gi|269792076|ref|YP — 003316980.1| 2-dehydropantoate 2-reductase [ Thermanaerovibrio acidaminovorans DSM 6589]
>gi|322383702|ref|ZP — 08057453.1| 2-dehydropantoate 2-reductase-like protein [ Paenibacillus larvae subsp. larvae B-3650]
>gi|119775691|ref|YP — 928431.1| 2-dehydropantoate 2-reductase [ Shewanella amazonensis SB2B]
>gi|308048598|ref|YP — 003912164.1| 2-dehydropantoate 2-reductase [ Ferrimonas balearica DSM 9799]
>gi|85712652|ref|ZP — 01043698.1| 2-dehydropantoate 2-reductase [ Idiomarina baltica OS145]
>gi|229541211|ref|ZP — 04430271.1| 2-dehydropantoate 2-reductase [ Bacillus coagulans 36D1]
>gi|77361202|ref|YP — 340777.1| 2-dehydropantoate reductase [ Pseudoalteromonas haloplanktis TAC125]
>gi|11499285|ref|NP — 070523.1| 2-dehydropantoate 2-reductase [ Archaeoglobus fulgidus DSM 4304]
>gi|254427620|ref|ZP — 05041327.1| 2-dehydropantoate 2-reductase [ Alcanivorax sp. DG881]
>gi|317151157|ref|XP — 001824478.2| 2-dehydropantoate 2-reductase [ Aspergillus oryzae RIB40]
>gi|254281804|ref|ZP — 04956772.1| 2-dehydropantoate 2-reductase [gamma proteobacterium NOR51-B]
>gi|315125903|ref|YP — 004067906.1| 2-dehydropantoate reductase [ Pseudoalteromonas sp. SM9913]
>gi|300311176|ref|YP — 003775268.1| 2-dehydropantoate 2-reductase [ Herbaspirillum seropedicae SmR1]
>gi|251797891|ref|YP — 003012622.1| 2-dehydropantoate 2-reductase [ Paenibacillus sp. JDR-2]
>gi|307544890|ref|YP — 003897369.1| 2-dehydropantoate 2-reductase [ Halomonas elongata DSM 2581]
>gi|301064244|ref|ZP — 07204687.1| 2-dehydropantoate 2-reductase [delta proteobacterium NaphS2]
>gi|82523896|emb|CA|78619.1| ketopantoate reductase [uncultured delta proteobacterium]
>gi|315646013|ref|ZP — 07899134.1| 2-dehydropantoate 2-reductase [ Paenibacillus vortex V453]
>gi|229061526|ref|ZP — 04198870.1| 2-dehydropantoate 2-reductase [ Bacillus cereus AH603]
>gi|229162856|ref|ZP — 04290813.1| 2-dehydropantoate 2-reductase [ Bacillus cereus R309803]
>gi|228960138|ref|ZP — 04121802.1| 2-dehydropantoate 2-reductase [ Bacillus thuringiensis serovar pakistani str. T13001]
>gi|324327820|gb|ADY23080.1| 2-dehydropantoate 2-reductase [ Bacillus thuringiensis serovar finitimus YBT-020]
>gi|282857022|ref|ZP — 06266273.1| 2-dehydropantoate 2-reductase [ Pyramidobacter piscolens W5455]
>gi|56460968|ref|YP — 156249.1| 2-dehydropantoate 2-reductase [ Idiomarina loihiensis L2TR]
>gi|302342758|ref|YP — 003807287.1| 2-dehydropantoate 2-reductase [ Desulfarculus baarsii DSM 2075]
>gi|260655057|ref|ZP — 05860545.1| 2-dehydropantoate 2-reductase [ Jonquetella anthropi E3 — 33 E1]
>gi|297180479|gb|ADI16693.1| ketopantoate reductase [uncultured gamma proteobacterium HF0010 — 05D02]
>gi|229117417|ref|ZP — 04246793.1| 2-dehydropantoate 2-reductase [ Bacillus cereus Rock1-3]
>gi|294501030|ref|YP — 003564730.1| 2-dehydropantoate 2-reductase [ Bacillus megaterium QM B1551]
>gi|310643005|ref|YP — 003947763.1| 2-dehydropantoate 2-reductase [ Paenibacillus polymyxa SC2]
>gi|121704788|ref|XP — 001270657.1| 2-dehydropantoate 2-reductase, putative [ Aspergillus clavatus NRRL 1]
>gi|194015015|ref|ZP — 03053632.1| 2-dehydropantoate 2-reductase [ Bacillus pumilus ATCC 7061]
>gi|121534373|ref|ZP — 01666197.1| 2-dehydropantoate 2-reductase [ Thermosinus carboxydivorans Nor1]
>gi|300854950|ref|YP — 003779934.1| ketopantoate reductase PanE/ApbA [ Clostridium ljungdahlii DSM 13528]
>gi|228909746|ref|ZP — 04073569.1| 2-dehydropantoate 2-reductase [ Bacillus thuringiensis IBL 200]
>gi|153938200|ref|YP — 001390518.1| 2-dehydropantoate 2-reductase [ Clostridium botulinum F str. Langeland]
>gi|51243923|ref|YP — 063807.1| 2-dehydropantoate 2-reductase [ Desulfotalea psychrophila LSv54]
>gi|88858567|ref|ZP — 01133209.1| putative 2-dehydropantoate reductase [ Pseudoalteromonas tunicata D2]
>gi|241895418|ref|ZP — 04782714.1| 2-dehydropantoate 2-reductase [ Weissella paramesenteroides ATCC 33313]
>gi|229019124|ref|ZP — 04175958.1| 2-dehydropantoate 2-reductase [ Bacillus cereus AH1273]
>gi|313124944|ref|YP — 004035208.1| ketopantoate reductase [ Halogeometricum borinquense DSM 11551]
>gi|308069898|ref|YP — 003871503.1| 2-dehydropantoate 2-reductase [ Paenibacillus polymyxa E681]
>gi|134299186|ref|YP — 001112682.1| 2-dehydropantoate 2-reductase [ Desulfotomaculum reducens MI-1]
>gi|116750179|ref|YP — 846866.1| 2-dehydropantoate 2-reductase [ Syntrophobacter fumaroxidans MPOB]
>gi|242399000|ref|YP — 002994424.1| 2-dehydropantoate 2-reductase [ Thermococcus sibiricus MM 739]
>gi|190347904|gb|EDK40261.2| hypothetical proten PGUG — 04359 [ Pichia guilliermondii ATCC 6260]
>gi|301055411|ref|YP — 003793622.1| putative 2-dehydropantoate 2-reductase [ Bacillus anthracis CI]
>gi|300712827|ref|YP — 03738639.1| 2-dehydropantoate 2-reductase [ Halalkalicoccus jeotgali B3]
>gi|156052196|ref|XP — 001592059.1| hypothetical protein SS1G — 07507 [ Sclerotinia sclerotiorum 1980]
>gi|85704948|ref|ZP — 01036049.1| ketopantoate reductase ApbA [ Roseovarius sp. 217]
>gi|295399703|ref|ZP — 06809684.1| 2-dehydropantoate 2-reductase [ Geobacillus thermoglucosidasius C56-YS93]
>gi|254573604|ref|XP — 002493911.1| hypothetical protein [ Pichia pastoris GS115]
>gi|299132097|ref|ZP — 07025292.1| 2-dehydropantoate 2-reductase [ Afipia sp. 1NLS2]
>gi|307354061|ref|YP — 003895112.1| 2-dehydropantoate 2-reductase [ Methanoplanus petrolearius DSM 11571]
>gi|261405647|ref|YP — 003241888.1| 2-dehydropantoate 2-reductase [ Paenibacillus sp. Y412MC10]
>gi|289581665|ref|YP — 003480131.1| 2-dehydropantoate 2-reductase [ Natrialba magadii ATCC 43099]
>gi|212696972|ref|ZP — 03305100.1| hypothetical protein ANHYDRO — 01535 [ Anaerococcus hydrogenalis DSM 7454]
>gi|70730838|ref|YP — 260579.1| 2-dehydropantoate 2-reductase [ Pseudomonas fluorescens Pf-5]
>gi|225575149|ref|ZP — 03783759.1| hypothetical protein RUMHYD — 03238 [ Blautia hydrogenotrophica DSM 10507]
>gi|296504414|ref|YP — 003666114.1| 2-dehydropantoate 2-reductase [ Bacillus thuringiensis BMB171]
>gi|187780219|ref|ZP — 02996692.1| hypothetical protein CLOSPO — 03815 [ Clostridium sporogenes ATCC 15579]
>gi|56475560|ref|YP — 157149.1| ketopantoate reductase ApbA [ Aromatoleum aromaticum EbN1]
>gi|57641903|ref|YP — 184361.1| 2-dehydropantoate 2-reductase [ Thermococcus kodakarensis KOD1]
>gi|296242388|ref|YP — 003649875.1| 2-dehydropantoate 2-reductase [ Thermosphaera aggregans DSM 11486]
>gi|229031552|ref|ZP — 04187552.1| 2-dehydropantoate 2-reductase [ Bacillus cereus AH1271]
>gi|152996054|ref|YP — 001340889.1| 2-dehydropantoate 2-reductase [ Marinomonas sp. MWYL1]
>gi|88704128|ref|ZP — 01101843.1| Ketopantoate reductase ApbA/PanE [ Congregibacter litoralis KT71]
>gi|149181743|ref|ZP — 01860235.1| 2-dehydropantoate 2-reductase [ Bacillus sp. SG-1]
>gi|322371463|ref|ZP — 08046012.1| 2-dehydropantoate 2-reductase [ Haladaptatus paucihalophilus DX253]
>gi|110833490|ref|YP — 692349.1| 2-dehydropantoate 2-reductase [ Alcanivorax borkumensis SK2]
>gi|241663589|ref|YP — 002981949.1| 2-dehydropantoate 2-reductase [ Ralstonia pickettii 12D]
>gi|18977768|ref|NP — 579125.1| 2-dehydropantoate 2-reductase [ Pyrococcus furiosus DSM 3638]
>gi|110798963|ref|YP — 695239.1| 2-dehydropantoate 2-reductase [ Clostridium perfringens ATCC 13124]
>gi|169782143|ref|XP — 001825534.1| 2-dehydropantoate 2-reductase family protein [ Aspergillus oryzae RIB40]
>gi|157692185|ref|YP — 001486647.1| 2-dehydropantoate 2-reductase [ Bacillus pumilus SAFR-032]
>gi|15606805|ref|NP — 214186.1| hypothetical protein aq — 1727 [ Aquifex aeolicus VF5]
>gi|163782247|ref|ZP — 02177245.1| hypothetical protein HG1285 — 05655 [ Hydrogenivirga sp. 126-5-R1-1]
>gi|317129310|ref|YP — 004095592.1| 2-dehydropantoate 2 reductase [ Bacillus cellulosilyticus DSM 2522]
>gi|229174587|ref|ZP — 04302117.1| 2-dehydropantoate 2-reductase [ Bacillus cereus MM3]
>gi|229086485|ref|ZP — 04218657.1| 2-dehydropantoate 2-reductase [ Bacillus cereus Rock3-44]
>gi|167044940|gb|ABZ09606.1| putative Ketopantoate reductase PanE/ApbA [uncultured marine microorganism HF4000_APKG8D23]
>gi|15896190|ref|NP — 349539.1| ketopantoate reductase PanE/ApbA [ Clostridium acetobutylicum ATCC 824]
>gi|324103300|gb|EGC00636.1| 2-dehydropantoate 2-reductase [ Pseudomonas sp. TJI-51]
>gi|14520967|ref|NP — 126442.1| 2-dehydropantoate 2-reductase [ Pyrococcus abyssi GE 51]
>gi|222097366|ref|YP — 002531423.1| 2-dehydropantoate 2-reductase [ Bacillus cereus Q 1]
>gi|319649677|ref|ZP — 08003833.1| 2-dehydropantoate 2-reductase [ Bacillus sp. 2_A — 57_CT2]
>gi|258514829|ref|YP — 003191051.1| 2-dehydropantoate 2-reductase [ Desulfotomaculum acetoxidans DSM 771]
>gi|87121684|ref|ZP — 01077770.1| ketopantoate reductase [ Marinomonas sp. MED121]
>gi|145589722|ref|YP — 01156319.1| 2-dehydropantoate 2-reductase [ Polynucleobacter necessarius subsp. asymbioticus QLW-P1DMWA-1]
>gi|254173247|ref|ZP — 04879920.1| 2-dehydropantoate 2-reductase [ Thermococcus sp. AM4]
>gi|145592200|ref|YP — 001154202.1| 2-dehydropantoate 2-reductase [ Pyrobaculum arsenaticum DSM 13514]
>gi|91788789|ref|YP — 549741.1| 2-dehydropantoate 2-reductase [ Polaromonas sp. JS666]
>gi|257387161|ref|YP — 003176934.1| 2-dehydropantoate 2-reductase [ Halomicrobium mukohataei DSM 12286]
>gi|18314044|ref|NP — 560711.1| 2-dehydropantoate 2-reductase (ketopantoate reductase) [ Pyrobaculum aerophilum str. IM2]
>gi|319646112|ref|ZP — 08000342.1| YlbQ protein [ Bacillus sp. BT1B_CT2]
>gi|168232151|ref|ZP — 02657209.1| 2-dehydropantoate 2-reductase [ Salmonella enterica subsp. enterica serovar Kentucky str. CDC 191]
>gi|323488622|ref|ZP — 08093866.1| 2-dehydropantoate 2-reductase [ Planococcus donghaensis MPA1U2]
>gi|226313441|ref|YP — 002773335.1| 2-dehydropantoate 2-reductase [ Brevibacillus brevis NBRC 100599]
>gi|88799068|ref|ZP — 01114649.1| 2-dehydropantoate 2-reductase [ Reinekea sp. MED297]
>gi|242813341|ref|XP — 002486147.1| 2-dehydropantoate 2-reductase, putative [ Talaromyces stipitatus ATCC 10500]
>gi|225849819|ref|YP — 002730053.1| 2-dehydropantoate 2-reductase [ Persephonella marina EX-H1]
>gi|209664195|ref|YP — 002288052.1| 2-dehydropantoate 2-reductase [ Oligotropha carboxidovorans OM5]
>gi|188589152|ref|YP — 001920485.1| 2-dehydropantoate 2-reductase [ Clostridium botulinum E3 str. Alaska E43]
>gi|119505092|ref|ZP — 01627168.1| 2-dehydropantoate 2-reductase [marine gamma proteobacterium HTCC2080]
>gi|15789904|ref|NP — 279728.1| hypothetical protein VNG0730C [ Halobacterium sp. NRC-1]
>gi|300709487|ref|YP — 003735301.1| 2-dehydropantoate 2-reductase [ Halalkalicoccus jeotgali B3]
>gi|269124038|ref|YP — 003306615.1| 2-dehydropantoate 2-reductase [ Streptobacillus moniliformis DSM 12112]
>gi|212224616|ref|YP — 002307852.1| 2-dehydropantoate 2-reductase [ Thermococcus onnurineus NA1]
>gi|302335576|ref|YP — 003800783.1| 2-dehydropantoate 2-reductase [ Olsenella uli DSM 7084]
>gi|154150658|ref|YP — 001404276.1| 2-dehydropantoate 2-reductase [ Candidates Methanoregula boonei 6A8]
>gi|284166943|ref|YP — 003405222.1| 2-dehydropantoate 2-reductase [ Haloterrigena turkmenica DSM 5511]
>gi|172057979|ref|YP — 001814439.1| 2-dehydropantoate 2-reductase [ Exiguobacterium sibiricum 255-15]
>gi|313637013|gb|EFS02587.1| 2-dehydropantoate 2-reductase [ Listeria seeligeri FSL S4-171]
>gi|228998702|ref|ZP — 04158289.1| 2-dehydropantoate 2-reductase [ Bacillus mycoides Rock3-17]
>gi|152976282|ref|YP — 001375799.1| 2-dehydropantoate 2-reductase [ Bacillus cereus subsp. cytotoxis NVH 391-98]
>gi|92114269|ref|YP — 574197.1| 2-dehydropantoate 2-reductase [ Chromohalobacter salexigens DSM 3043]
>gi|240102379|ref|YP — 002958688.1| 2-dehydropantoate 2-reductase [ Thermococcus gammatolerans EJ3]
>gi|206889443|ref|YP — 002249396.1| 2-dehydropantoate 2-reductase [ Thermodesulfovibrio yellowstonii DSM 11347]
>gi|297583937|ref|YP — 003699717.1| 2-dehydropantoate 2-reductase [ Bacillus selenitireducens MLS10]
>gi|270290296|ref|ZP — 06196521.1| 2-dehydropantoate 2-reductase [ Pediococcus acidilactici 7 — 4]
>gi|147919508|ref|YP — 686752.1| putative 2-dehydropantoate 2-reductase [uncultured methanogenic archaeon RC-1]
>gi|313632475|gb|EFR99493.1| 2-dehydropantoate 2-reductase [ Listeria seeligeri FSL N1-067]
>gi|266623089|ref|ZP — 06116024.1| 2-dehydropantoate 2-reductase [ Clostridium hathewayi DSM 13479]
>gi|186470939|ref|YP — 001862257.1| 2-dehydropantoate 2-reductase [ Burkholderia phymatum STM815]
>gi|91975083|ref|YP — 567742.1| 2-dehydropantoate 2-reductase [ Rhodopseudomonas palustris BisB5]
>gi|168186958|ref|ZP — 02621593.1| 2-dehydropantoate 2-reductase [ Clostridium botulinum C str. Eklund]
>gi|171316249|ref|ZP — 02905471.1| 2-dehydropantoate 2-reductase [ Burkholderia ambifaria MEX-5]
>gi|118444120|ref|YP — 877052.1| 2-dehydropantoate 2-reductase [ Clostridium novyi NT]
>gi|304403996|ref|ZP — 07385658.1| 2-dehydropantoate 2-reductase [ Paenibacillus curdlanolyticus YK9]
>gi|14591192|ref|NP — 143268.1| 2-dehydropantoate 2-reductase [ Pyrococcus horikoshii OT3]
>gi|39937620|ref|NP — 949896.1| putative 2-dehydropantoate 2-reductase [ Rhodopseudomonas palustris CGA009]
>gi|257051985|ref|YP — 003129818.1| 2-dehydropantoate 2-reductase [ Halorhabdus utahensis DSM 12940]
>gi|297616632|ref|YP — 003701791.1| 2-dehydropantoate 2-reductase [ Syntrophothermus lipocalidus DSM 12680]
>gi|124485202|ref|YP — 001029818.1| hypothetical protein Mlab — 0375 [ Methanocorpusculum labreanum Z]
>gi|311029915|ref|ZP — 07708005.1| 2-dehydropantoate 2-reductase [ Bacillus sp. m3-13]
>gi|320355422|ref|YP — 004196761.1| 2-dehydropantoate 2-reductase [ Desulfobulbus propionicus DSM 2032]
>gi|255654270|ref|ZP — 05399679.1| putative ketopantoate reductase [ Clostridium difficile QCD-23m63]
>gi|86747344|ref|YP — 483840.1| 2-dehydropantoate 2-reductase [ Rhodopseudomonas palustris HaA2]
>gi|319796261|ref|YP — 004157901.1| 2-dehydropantoate 2-reductase [ Variovorax paradoxus EPS]
>gi|289435387|ref|YP — 003465259.1| 2-dehydropantoate 2-reductase [ Listeria seeligeri serovar 1/2b str. SLCC3954]
>gi|284161230|ref|YP — 003399853.1| 2-dehydropantoate 2-reductase [ Archaeoglobus profundus DSM 5631]
>gi|163792409|ref|ZP — 02186386.1| 2-dehydropantoate 2-reductase [alpha proteobacterium BAL199]
>gi|227535072|ref|ZP — 03965121.1| 2-dehydropantoate 2-reductase [ Lactobacillus paracasei subsp. paracasei ATCC 25302]
>gi|172065517|ref|YP — 001816229.1| 2-dehydropantoate 2-reductase [ Burkholderia ambifaria MC40-6]
>gi|56696485|ref|YP — 166842.1| 2-dehydropantoate 2-reductase [ Ruegeria pomeroyi DSS-3]
>gi|212639667|ref|YP — 002316187.1| 2-dehydropantoate 2-reductase [ Anoxybacillus flavithermus WK1]
>gi|73538792|ref|YP — 299159.1| ketopantoate reductase ApbA/PanE [ Ralstonia eutropha JMP134]
>gi|288818570|ref|YP — 003432918.1| 2-dehydropantoate 2-reductase [ Hydrogenobacter thermophilus TK-6]
>gi|160941380|ref|ZP — 02088717.1| hypothetical protein CLOBOL — 06273 [ Clostridium bolteae ATCC BAA-613]
>gi|167630796|ref|YP — 001681295.1| 2-dehydropantoate 2-reductase [ Heliobacterium modesticaldum Ice1]
>gi|89099594|ref|ZP — 01172469.1| 2-dehydropantoate 2-reductase [ Bacillus sp. NRRL B-14911]
>gi|227431961|ref|ZP — 03913981.1| possible 2-dehydropantoate 2-reductase [ Leuconostoc mesenteroides subsp. cremoris ATCC 19254]
>gi|299534661|ref|ZP — 07047993.1| putative 2-dehydropantoate 2-reductase [ Lysinibacillus fusiformis ZC1]
>gi|227552200|ref|ZP — 03982249.1| 2-dehydropantoate 2-reductase [ Enterococcus faecium TX1330]
>gi|289595871|ref|YP — 003482567.1| 2-dehydropantoate 2-reductase [ Aciduliprofundum boonei T469]
>gi|138894643|ref|YP — 001125096.1| 2-dehydropantoate 2-reductase [ Geobacillus thermodenitrificans NG80-2]
>gi|55379641|ref|YP — 137491.1| 2-dehydropantoate 2-reductase [ Haloarcula marismortui ATCC 43049]
>gi|294083831|ref|YP — 003550588.1| 2-dehydropantoate 2-reductase [ Candidatus Puniceispirillum marinum IMCC1322]
>gi|119898762|ref|YP — 933975.1| 2-dehydropantoate 2-reductase [ Azoarcus sp. BH72]
>gi|119872861|ref|YP — 930868.1| 2-dehydropantoate 2-reductase [ Pyrobaculum islandicum DSM 4184]
>gi|257456159|ref|ZP — 05621356.1| 2-dehydropantoate 2-reductase [ Treponema vincentii ATCC 35580]
>gi|257867166|ref|ZP — 05646819.1| ketopantoate reductase [ Enterococcus casseliflavus EC30]
>gi|126459006|ref|YP — 001055284.1| 2-dehydropantoate 2-reductase [ Pyrobaculum calidifontis JCM 11548]
>gi|239826511|ref|YP — 002949135.1| 2-dehydropantoate 2-reductase [ Geobacillus sp. WCH70]
>gi|91790339|ref|YP — 551291.1| 2-dehydropantoate 2-reductase [ Polaromonas sp. JS666]
>gi|256829670|ref|YP — 003158398.1| 2-dehydropantoate 2-reductase [ Desulfomicrobium baculatum DSM 4028]
>gi|315659442|ref|ZP — 07912305.1| 2-dehydropantoate 2-reductase [ Staphylococcus lugdunensis M23590]
>gi|150403611|ref|YP — 001330905.1| 2-dehydropantoate 2-reductase [ Methanococcus maripaludis C 7]
>gi|259047992|ref|ZP — 05738393.1| 2-dehydropantoate 2-reductase [ Granulicatella adiacens ATCC 49175]
>gi|24214890|ref|NP — 712371.1| 2-dehydropantoate 2-reductase [ Leptospira interrogans serovar Lai str. 56601]
>gi|319789510|ref|YP — 004151143.1| 2-dehydropantoate 2-reductase [ Thermovibrio ammonificans HB-1]
>gi|171320779|ref|ZP — 02909787.1| 2-dehydropantoate 2-reductase [ Burkholderia ambifaria MEX-5]
>gi|295705715|ref|YP — 003598790.1| 2-dehydropantoate 2-reductase [ Bacillus megaterium DSM 319]
>gi|256853805|ref|ZP — 05559170.1| 2-dehydropantoate 2-reductase [ Enterococcus faecalis T8]
>gi|186472751|ref|YP — 001860093.1| 2-dehydropantoate 2-reductase [ Burkholderia phymatum STM815]
>gi|164687814|ref|ZP — 02211842.1| hypothetical protein CLOBAR — 01458 [ Clostridium bartlettii DSM 16795]
>gi|315147351|gb|EFT91367.1| 2-dehydropantoate 2-reductase [ Enterococcus faecalis TX4244]
>gi|289450069|ref|YP — 003474740.1| putative 2-dehydropantoate 2-reductase [ Clostridiales genomosp. BVAB3 str. UPII9-5]
>gi|126178741|ref|YP — 001046706.1| 2-dehydropantoate 2-reductase [ Methanoculleus marisnigri JR1]
>gi|313622979|gb|EFR93276.1| 2-dehydropantoate 2-reductase [ Listeria innocua FSL J1-023]
>gi|197117182|ref|YP — 002137609.1| 2-dehydropantoate 2-reductase [ Geobacter bemidjiensis Bern]
>gi|257065623|ref|YP — 003151879.1| 2-dehydropantoate 2-reductase [ Anaerococcus prevotii DSM 20548]
>gi|221211405|ref|ZP — 03584384.1| 2-dehydropantoate 2-reductase [ Burkholderia multivorans CGD1]
>gi|121606900|ref|YP — 984229.1| 2-dehydropantoate 2-reductase [ Polaromonas naphthalenivorans CJ2]
>gi|229823430|ref|ZP — 04449499.1| hypothetical protein GCWU000282 — 00728 [ Catonella morbi ATCC 51271]
>gi|303256960|ref|ZP — 07342974.1| 2-dehydropantoate 2-reductase [ Burkholderiales bacterium 1 — 1 — 47]
>gi|159042347|ref|YP — 001541599.1| 2-dehydropantoate 2-reductase [ Caldivirga maquilingensis IC-167]
>gi|315155665|gb|EFT99681.1| 2-dehydropantoate 2-reductase [ Enterococcus faecalis TX0043]
>gi|317496587|ref|ZP — 07954935.1| 2-dehydropantoate 2-reductase [ Gemella moribillum M424]
>gi|323342656|ref|ZP — 08082888.1| 2-dehydropantoate 2-reductase [ Erysipelothrix rhusiopathiae ATCC 19414]
>gi|239817916|ref|YP — 002946826.1| 2-dehydropantoate 2-reductase [ Variovorax paradoxus S110]
>gi|254169372|ref|ZP — 04876201.1| 2-dehydropantoate 2-reductase [ Aciduliprofundum boonei T469]
>gi|307594721|ref|YP — 003901038.1| 2-dehydropantoate 2-reductase [ Vulcanisaeta distributa DSM 14429]
>gi|297530725|ref|YP — 003672000.1| 2-dehydropantoate 2-reductase [ Geobacillus sp. C56-T3]
>gi|300173017|ref|YP — 003772183.1| 2-dehydropantoate 2-reductase [ Leuconostoc gasicomitatum LMG 18811]
>gi|52549536|gb|AAU83385.1| hypothetical protein GZ27G5 — 16 [uncultured archaeon GZfos27G5]
>gi|119094200|gb|ABL61022.1| ketopantoate reductase [uncultured marine bacterium HF10 — 25F10]
>gi|162146807|ref|YP — 001601268.1| putative 2-dehydropantoate 2-reductase [ Gluconacetobacter diazotrophicus PAI 5]
>gi|256963612|ref|ZP — 05567763.1| ketopantoate reductase ApbA/PanE [ Enterococcus faecalis HIP11704]
>gi|313617966|gb|EFR90131.1| 2-dehydropantoate 2-reductase [ Listeria innocua FSL S4-378]
>gi|313679570|ref|YP — 004057309.1| 2-dehydropantoate 2-reductase [ Oceanithermus profundus DSM 14977]
>gi|313885617|ref|ZP — 07819367.1| 2-dehydropantoate 2-reductase[ (Eremococcus coleocola ACS-139-V-Col8]
>gi|163790016|ref|ZP — 02184451.1| 2-dehydropantoate 2-reductase [ Carnobacterium sp. AT7]
>gi|225870636|ref|YP — 002746583.1| ketopantoate reductase [ Streptococcus equi subsp. equi 4047]
>gi|320527125|ref|ZP — 08028312.1| 2-dehydropantoate 2-reductase [ Solobacterium moorei F0204]
>gi|316936042|ref|YP — 004111024.1| 2-dehydropantoate 2 reductase [ Rhodopseudomonas palustris DX-1]
>gi|209559212|ref|YP — 002285684.1| 2-dehydropantoate 2-reductase [ Streptococcus pyogenes NZ131]
>gi|315304102|ref|ZP — 07874502.1| 2-dehydropantoate 2-reductase [ Listeria ivanovii FSL F6-596]
>gi|323373091|gb|ADX45360.1| 2-dehydropantoate 2-reductase [ Acidovorax avenae subsp. avenae ATCC 19860]
>gi|169782199|ref|XP — 001825562.1| 2-dehydropantoate 2-reductase family protein [ Aspergillus oryzae RIB40]
>gi|188996324|ref|YP — 001930575.1| 2-dehydropantoate 2-reductase [ Sulfurihydrogenibrum sp. YO3AOP1]
>gi|206561131|ref|YP — 02231896.1| putative ketopantoate reductase [ Burkholderia cenocepacia J2315]
>gi|56807918|ref|ZP — 00365743.1| COG1893: Ketopantoate reductase [ Streptococcus pyogenes M49 591]
>gi|120610087|ref|YP — 969765.1| 2-dehydropantoate 2-reductase [ Acidovorax avenae subsp. citrulli AAC00-1]
>gi|52548816|gb|AAU82665.1| conserved hypothetical protein [uncultured archaeon GZfos19A5]
>gi|70725616|ref|YP — 252530.1| 2-dehydropantoate 2-reductase [ Staphylococcus haemolyticus JCSC1435]
>gi|292654245|ref|YP — 003534142.1| 2-dehydropantoate 2-reductase [ Haloferax volcanii DS2]
>gi|288931405|ref|YP — 003435465.1| 2-dehydropantoate 2-reductase [ Ferroglobus placidus DSM 10642]
>gi|150400258|ref|YP — 001324025.1| 2-dehydropantoate 2-reductase [ Methanococcus vannielii SB]
>gi|126466272|ref|YP — 001041381.1| 2-dehydropantoate 2-reductase [ Staphylothermus marinus F1]
>gi|221068483|ref|ZP — 03544588.1| 2-dehydropantoate 2-reductase [ Comamonas testosteroni KF-1]
>gi|299821547|ref|ZP — 07053435.1| possible 2-dehydropantoate 2-reductase [ Listeri grayi DSM 20601]
>gi|290508302|ref|ZP — 06547673.1| 2-dehydropantoate 2-reductase [ Klebsiella sp. 1 — 1 — 55]
>gi|297570429|ref|YP — 003691773.1| 2-dehydropantoate 2-reductase [ Desulfurivibrio alkaliphilus AHT2]
>gi|169827000|ref|YP — 001697158.1| putative 2-dehydropantoate 2-reductase [ Lysinibacillus sphaericus C3-41]
>gi|238503586|ref|XP — 002383026.1| 2-dehydropantoate 2-reductase family protein, putative [ Aspergillus flavus NRRL3357]
>gi|116873476|ref|YP — 850257.1| 2-dehydropantoate 2-reductase [ Listeria welshimeri serovar 6b str. SLCC5334]
>gi|242556790|pdb|3HWR|A Chain A, Crystal Structure Of PaneAPBA family ketopantoate reductase (Yp — 299159.1) From Ralstonia Eutropha Jmp134
>gi|302387383|ref|YP — 003823205.1| 2-dehydropantoate 2-reductase [ Clostridium saccharolyticum WM1]
>gi|307726219|ref|YP — 003909432.1| 2-dehydropantoate 2-reductase [ Burkholderia sp. CCGE1003]
>gi|257871049|ref|ZP — 05650702.1|ketopantoate reductase [ Enterococcus gallinarum EG2]
>gi|145254262|ref|XP — 001398576.1| 2-dehydropantoate 2-reductase family protein [ Aspergillus niger CBS 513.88]
>gi|227515951|ref|ZP — 03946000.1| 2-dehydropantoate 2-reductase [ Atopobium vaginae DSM 15829]
>gi|254247377|ref|ZP — 04940698.1|Ketopantoate reductase [ Burkholderia cenocepacia PC184]
>gi|297527045|ref|YP — 003669069.1| 2-dehydropantoate 2-reductase [ Staphylothermus hellenicus DSM 12710]
>gi|303233096|ref|ZP — 07319769.1| 2-dehydropantoate 2-reductase [ Atopobium vaginae PB189-T1-4]
>gi|253699477|ref|YP — 003020666.1| 2-dehydropantoate 2-reductase [ Geobacter sp. M21]
>gi|293401734|ref|ZP — 06645875.1| 2-dehydropantoate 2-reductase [ Erysipelotrichaceae bacterium 5 — 2 — 54FAA]
>gi|225849463|ref|YP — 002729628.1| 2-dehydropantoate 2-reductase [ Sulfurihydrogenibium azorense Az-Fu1]
>gi|227893553|ref|ZP — 04011358.1| 2-dehydropantoate 2-reductase [ Lactobacillus ultunensis DSM 16047]
>gi|85544557|pdb|2EW2|A Chain A, Crystal Structure Of The Putative 2-Dehydropantoate 2- Reductase From Enterococcus Faecalis
>gi|146318978|ref|YP — 001198690.1| 2-dehydropantoate 2-reductase [ Streptococcus suis 05ZYH33]
>gi|124266554|ref|YP — 001020558.1| 2-dehydropantoate 2-reductase [ Methylibium petroleiphilum PM1]
>gi|283768342|ref|ZP — 06341254.1| 2-dehydropantoate 2-reductase [ Bulleidia extructa W1219]
>gi|315223029|ref|ZP — 07864908.1| 2-dehydropantoate 2-reductase [ Streptococcus anginosus F0211]
>gi|207857980|ref|YP — 002244631.1| 2-dehydropantoate 2-reductase [ Salmonella enterica subsp. enterica serovar Enteritidis str. P125109]
>gi|134293442|ref|YP — 001117178.1| 2-dehydropantoate 2-reductase [ Burkholderia vietnamiensis G4]
>gi|52550479|gb|AAU84328.1| conserved hypothetical protein [uncultured archaeon GZfos9D1]
>gi|324965153|gb|ADY55932.1| 2-dehydropantoate 2-reductase [ Syntrophobotulus glycolicus DSM 8271]
>gi|296331086|ref|ZP — 06873560.1| 2-dehydropantoate 2-reductase [ Bacillus subtilis subsp. spizizenii ATCC 6633]
>gi|228474704|ref|ZP — 04059435.1| 2-dehydropantoate 2-reductase [ Staphylococcus hominis SK119]
>gi|119896483|ref|YP — 931696.1| 2-dehydropantoate 2-reductase [ Azoarcus sp. BH72]
>gi|297181166|gb|ADI17362.1| ketopantoate reductase [uncultured delta proteobacterium HF0070 — 30B07]
>gi|169333685|ref|ZP — 02860878.1| hypothetical protein ANASTE — 00069 [ Anaerofustis stercorihominis DSM 17244]
>gi|171184791|ref|YP — 001793710.1| 2-dehydropantoate 2-reductase [ Thermoproteus neutrophilus V24Sta]
>gi|116334695|ref|YP — 796222.1| 2-dehydropantoate 2-reductase [ Lactobacillus brevis ATCC 367]
>gi|45358235|ref|NP — 987792.1| binding-protein dependent transport system inner membrane protein [ Methanococcus maripaludis S2]
>gi|15673305|ref|NP — 267479.1| 2-dehydropantoate 2-reductase [ Lactococcus lactis subsp. lactis II 1403]
>gi|167569002|ref|ZP — 02361876.1| 2-dehydropantoate 2-reductase [ Burkholderia oklahomensis C6786]
>gi|222444726|ref|ZP — 03607241.1| hypothetical protein METSMIALI — 00339 [ Methanobrevibacter smithii DSM 2375]
>gi|148642093|ref|YP — 001272606.1| ketopantoate reductase. ApbA [ Methanobrevibacter smithii ATCC 35061]
>gi|56964133|ref|YP — 175864.1| 2-dehydropantoate 2-reductase [ Bacillus clausii KSM-K16]
>gi|76801123|ref|YP — 326131.1| 2-dehydropantoate 2-reductase [ Natronomonas pharaonis DSM 2160]
>gi|291563922|emb|CBL42738.1| ketopantoate reductase [butyrate-producing bacterium SS3/4]
>gi|126649737|ref|ZP — 01721973.1| 2-dehydropantoate 2-reductase [ Bacillus sp. B14905]
>gi|125623962|ref|YP — 001032445.1| 2-dehydropantoate 2-reductase [ Lactococcus lactis subsp. cremoris MG1363]
>gi|264677329|ref|YP — 003277235.1| 2-dehydropantoate 2-reductase [ Comamonas testosteroni CNB-2]
>gi|163793943|ref|ZP — 02187917.1| putative ketopantoate reductase [alpha proteobacterium BAL199]
>gi|229543594|ref|ZP — 04432654 1| 2-dehydropantoate 2-reductase [ Bacillus coagulans 36D1]
>gi|208435758|pdb|3EGO|A Chain A, Crystal Structure Of Probable 2-Dehydropantoate 2-Reductase Pane From Bacillus Subtillis
>gi|86143831|ref|ZP — 01062207.1| hypothetical protein MED217 — 01020 [ Leeuwenhoekiella blandensis MED217]
>gi|260946531|ref|XP — 002617563.1| hypothetical protein CLUG — 03007 [ Clavispora lusitaniae ATCC 42720]
>gi|15615142|ref|NP — 243445.1| 2-dehydropantoate 2-reductase [ Bacillus halodurans C-125]
>gi|239625263|ref|ZP — 04668294.1| 2-dehydropantoate 2-reductase [ Clostridiales bacterium 1 — 7 — 47_FAA]
>gi|315038258|ref|YP — 004031826.1| 2-dehydropantoate 2-reductase [ Lactobacillus amylovorus GRL 1112]
>gi|300310480|ref|YP — 003774572.1| 2-dehydropantoate 2-reductase [ Herbaspirillum seropedicae SmR1]
>gi|167893095|ref|ZP — 02480497.1| 2-dehydropantoate 2-reductase [ Burkholderia pseudomallei 7894]
>gi|89894746|ref|YP — 518233.1| hypothetical protein DSY2000 [ Desulfitobacterium hafniense Y51]
>gi|319762040|ref|YP — 004125977.1| 2-dehydropantoate 2-reductase [ Alicycliphilus denitrificans BC]
>gi|69250617|ref|ZP — 00605173.1| Ketopantoate reductase ApbA/PanE [ Enterococcus faecium DO]
>gi|288560576|ref|YP — 003424062.1| 2-dehydropantoate 2-reductase PanE [ Methanobrevibacter ruminantium M1]
>gi|70725181|ref|YP — 252095.1| 2-dehydropantoate 2-reductase [ Staphylococcus haemolyticus JCSC1435]
>gi|324098987|gb|EGB96980.1| 2-dehydropantoate 2-reductase [ Pseudomonas sp. TJI-51]
>gi|86608338|ref|YP — 477100.1| 2-dehydropantoate 2-reductase [ Synechococcus sp. JA-2-3B'a(2-13)]
>gi|67906799|gb|AAY82862.1| putative ketopantoate reductase [uncultured bacterium MedeBAC46A06]
>gi|310778974|ref|YP — 003967307.1| ketopantoate reductase [ Ilyobacter polytropus DSM 2926]
>gi|242372095|ref|ZP — 04817669.1| 2-dehydropantoate 2-reductase [ Staphylococcus epidermidis M23864:W1]
>gi|170749968|ref|YP — 001756228.1| 2-dehydropantoate 2-reductase [ Methylobacterium radiotolerans JCM 2831]
>gi|167588290|ref|ZP — 02380678.1| 2-dehydropantoate 2-reductase [ Burkholderia ubonensis Bu]
>gi|78067381|ref|YP — 370150.1| 2-dehydropantoate 2-reductase[ Burkholderia sp. 383]
>gi|124028371|ref|YP — 001013691.1| ketopantoate reductase [ Hyperthermus butylicus DSM 5456]
>gi|219848017|ref|YP — 002462450.1| 2-dehydropantoate 2-reductase [ Chloroflexus aggregans DSM 9485]
>gi|167580031|ref|ZP — 02372905.1| 2-dehydropantoate 2-reductase [ Burkholderia thailandensis TXDOH]
>gi|288553174|ref|YP — 003425109.1| 2-dehydropantoate 2-reductase [ Bacillus pseudofirmus OF4]
>gi|186470810|ref|YP — 001862128.1| 2-dehydropantoate 2-reductase [ Burkholderia phymatum STM815]
>gi|313890559|ref|ZP — 07824187.1| 2-dehydropantoate 2-reductase [ Streptococcus pseudoporcinus SPIN 20026]
>gi|310827874|ref|YP — 003960231.1| hypothetical protein ELI — 2285 [ Eubacterium limosum KIST612]
>gi|121595444|ref|YP — 987340.1| 2-dehydropantoate 2-reductase [ Acidovorax sp. JS42]
>gi|29375143|ref|NP — 814296.1| 2-dehydropantoate 2-reductase [ Enterococcus faecalis V583]
>gi|313899882|ref|ZP — 07833385.1| 2-dehydropantoate 2-reductase [ Clostridium sp. HGF2]
>gi|187920203|ref|YP — 001889234.1| 2-dehydropantoate 2-reductase [ Burkholderia phytofirmans PsJN]
>gi|27381507|ref|NP — 773036.1| 2-dehydropantoate 2-reductase [ Bradyrhizobium japonicum USDA 110]
>gi|300768503|ref|ZP — 07078402.1| 2-dehydropantoate 2-reductase [ Lactobacillus plantarum subsp. plantarum ATCC 14917]
>gi|197295211|ref|YP — 002153752.1| putative 2-dehydropantoate 2-reductase [ Burkholderia cenocepacia J2315]
>gi|225410102|ref|ZP — 03761291.1| hypothetical protein CLOSTASPAR — 05323 [ Clostridium asparagiforme DSM 15981]
>gi|222152909|ref|YP — 02562086.1| 2-dehydropantoate 2-reductase [ Streptococcus uberis 0140J]
>gi|300854058|ref|YP — 003779042.1| 2-dehydropantoate 2-reductase [ Clostridium ljungdahlii DSM 13528]
>gi|237653536|ref|YP — 002889650.1| 2-dehydropantoate 2-reductase [ Thauera sp. MZ1T]
>gi|259047521|ref|ZP — 05737922.1| 2-dehydropantoate 2-reductase [ Granulicatella adiacens ATCC 49175]
>gi|319957266|ref|YP — 004168529.1| 2-dehydropantoate 2-reductase [ Nitratifractor salsuginis DSM 16511]
>gi|320355269|ref|YP — 004196608.1| 2-dehydropantoate 2-reductase [ Desulfobulbus propionicus DSM 2032]
>gi|239636063|ref|ZP — 04677077.1| 2-dehydropantoate 2-reductase [ Staphylococcus warneri L37603]
>gi|320100944|ref|YP — 004176536.1| ketopantoate reductase [ Desulfurococcus mucosus DSM 2162]
>gi|169630635|ref|YP — 001704284.1| ketopantoate reductase ApbA/PanE [ Mycobacterium abscessus ATCC 19977]
>gi|81427656|ref|YP — 394653.1| 2-dehydropantoate 2-reductase [ Lactobacillus sakei subsp. sakei 23K]
>gi|241889407|ref|ZP — 04776708.1| 2-dehydropantoate 2-reductase [ Gemella haemolysans ATCC 10379]
>gi|251811868|ref|ZP — 04826341.1| 2-dehydropantoate 2-reductase [ Staphylococcus epidermidis BCM-HMP0060]
>gi|218883653|ref|YP — 002428035.1| 2-dehydropantoate 2-reductase [ Desulfurococcus kamchatkensis 1221n]
>gi|229918541|ref|YP — 002887187.1| 2-dehydropantoate 2-reductase [ Exiguobacterium sp. AT1b]
>gi|314939006|ref|ZP — 07846271.1| 2-dehydropantoate 2-reductase [ Enterococcus faecium TX0133a04]
>gi|69244336|ref|ZP — 00602804.1| Ketopantoate reductase ApbA/PanE [ Enterococcus faecium DO]
>gi|311068031|ref|YP — 003972954.1| 2-dehydropantoate2-reductase [ Bacillus atrophaeus 1942]
>gi|219847221|ref|YP — 002461654.1| 2-dehydropantoate 2-reductase [ Chloroflexus aggregans DSM 9485]
>gi|295699875|ref|YP — 003607768.1| 2-dehydropantoate 2-reductase [ Burkholderia sp. CCGE1002]
>gi|307730136|ref|YP — 003907360.1| 2-dehydropantoate 2-reductase [ Burkholderia sp. CCGE 1003]
>gi|261350733|ref|ZP — 05976150.1| 2-dehydropantoate 2-reductase [ Methanobrevibacter smithii DSM 2374]
>gi|84489765|ref|YP — 447997.1| putative 2-dehydropantoate 2-reductase [ Methanosphaera stadtmanae DSM 3091]
>gi|319893545|ref|YP — 004150420.1| 2-dehydropantoate 2-reductase [ Staphylococcus pseudintermedius HKU10-03]
>gi|197302450|ref|ZP — 03167505.1| hypothetical protein RUMLAC — 01178 [ Ruminococcus lactaris ATCC 29176]
>gi|258542366|ref|YP — 003187799.1| ketopantoate reductase ApbA/PanE [ Acetobacter pasteurianus IFO 3283-01]
>gi|172061542|ref|YP — 001809194.1| 2-dehydropantoate 2-reductase [ Burkholderia ambifaria MC40-6]
>gi|15894883|ref|NP — 348232.1| ketopantoate reductase [ Clostridium acetobutylicum ATCC 624]
>gi|299132927|ref|ZP — 07026122.1| 2-dehydropantoate 2-reductase [ Afipia sp. 1NLS2]
>gi|45657601|ref|YP — 001687.1| 2-dehydropantoate 2-reductase [ Leptospira interrogans serovar Copenhageni str. Fiocruz L1-130]
>gi|238024361|ref|YP — 002908593.1| 2-dehydropantoate 2-reductase [ Burkholderia glumae BGR1]
>gi|154685930|ref|YP — 001421091.1| 2-dehydropantoate 2-reductase [ Bacillus amyloliquefaciens FZB42]
>gi|126180322|ref|YP — 001048287.1| 2-dehydropantoate 2-reductase [ Methanoculleus marisnigri JR1]
>gi|161523150|ref|YP — 001586079.1| 2-dehydropantoate 2-reductase [ Burkholderia multivorans ATCC 17616]
>gi|323528188|ref|YP — 004230340.1| 2-dehydropantoate 2-reductase [ Burkholderia sp. CCGE1001]
>gi|254818916|ref|ZP — 05223917.1| 2-dehydropantoate 2-reductase [ Mycobacterium intracellulare ATCC 13950]
>gi|313498946|gb|ADR60312.1| 2-dehydropantoate 2-reductase [ Pseudomonas putida BIRD-1]
>gi|22537498|ref|NP — 688349.1| 2-dehydropantoate 2-reductase [ Streptococcus agalactiae 2603V/R]
>gi|123403597|ref|XP — 001302267.1| Ketopantoate reductase PanE/ApbA family protein [ Trichomonas vaginalis G3]
>gi|189348029|ref|YP — 001941225.1| 2-dehydropantoate 2-reductase [ Burkholderia multivorans ATCC 17616]
>gi|222150304|ref|YP — 002559457.1| 2-dehydropantoate 2-reductase homolog [ Macrococous caseolyticus JCSC5402]
>gi|90962337|ref|YP — 536253.1| 2-dehydropantoate 2-reductase [ Lactobacillus salivarius UCC118]
>gi|160900483|ref|YP — 001566065.1| 2-dehydropantoate 2-reductase [ Delftia acidovorans SPH-1]
>gi|297588109|ref|ZP — 06946753.1| 2-dehydropantoate 2-reductase [ Finegoldia magna ATCC 53516]
>gi|299533998|ref|ZP — 07047350.1| 2-dehydropantoate 2-reductase [ Comamonas testosteroni S44]
>gi|291547410|emb|CBL20518.1| 2-dehydropantoate 2-reductase [ Ruminococcus sp. SR1/5]
>gi|118592425|ref|ZP — 01549817.1| 2-dehydropantoate 2-reductase [ Stappia aggregata IAM 12614]
>gi|254826199|ref|ZP — 05231200.1| 2-dehydropantoate 2-reductase [ Listeria monocytogenes FSL J1-194]
>gi|116670444|ref|YP — 831377.1| 2-dehydropantoate 2-reductase [ Arthrobacter sp. FB24]
>gi|89897521|ref|YP — 521008.1| hypothetical protein DSY4775 [ Desulfitobacterium hafniense Y51]
>gi|293606857|ref|ZP — 06689205.1| 2-dehydropantoate 2-reductase [ Achromobacter piechaudii ATCC 43553]
>gi|126730558|ref|ZP — 01746368.1| 2-dehydropantoate 2-reductase [ Sagittula stellata E-37]
>gi|317133532|ref|YP — 004092846.1| 2-dehydropantoate 2-reductase [ Ethanoligenens harbinense YUAN-3]
>gi|167561774|ref|ZP — 02354690.1| 2-dehydropantoate 2-reductase [ Burkholderia oklahomensis EO147]
>gi|121604457|ref|YP — 981786.1| 2-dehydropantoate 2-reductase [ Polaromonas naphthalenivorans CJ2]
>gi|308173476|ref|YP — 003920181.1| 2-dehydropantoate 2-reductase [ Bacillus amyloliquefaciens DSM 7]
>gi|319939189|ref|ZP — 08013552.1| 2-dehydropantoate 2-reductase [ Streptococcus anginosus 1 — 2 — 62CV]
>gi|295136259|ref|YP — 003586935.1| ketopantoate reductase PanE/ApbA [ Zunongwangia profunda SM-A87]
>gi|94263023|ref|ZP — 01286842.1| 2-dehydropantoate 2-reductase [delta proteobacterium MLMS-1]
>gi|89896295|ref|YP — 519782.1| hypothetical protein DSY3549 [ Desulfitobacterium hafniense Y51]
>gi|314934501|ref|ZP — 07841860.1| 2-dehydropantoate 2-reductase [ Staphylococcus caprae C87]
>gi|167747028|ref|ZP — 02419155.1| hypothetical protein ANACAC — 01740 [ Anaerostipes caccae DSM 14662]
>gi|258425014|ref|ZP — 05687885.1| 2-dehydropantoate 2-reductase [ Staphylococcus aureus A9635]
>gi|225180981|ref|ZP — 03734429.1| 2-dehydropantoate 2-reductase [ Dethiobacter alkaliphilus AHT 1]
>gi|296111865|ref|YP — 003622247.1| 2-dehydropantoate 2-reductase [ Leuconostoc kimchii IMSNU 11154]
>gi|311319581|gb|EFQ87840.1| hypothetical protein PTT — 16492 [ Pyranophora teres f. teres 0-1]
>gi|225734175|pdb|3G17|A Chain A, Structure Of Putative 2-Dehydropantoate 2-Reductase From Staphylococcus Aureus
>gi|315283089|ref|ZP — 07871356.1| 2-dehydropantoate 2-reductase [ Listeria marthii FSL S4-120]
>gi|209543868|ref|YP — 002276097.1| 2-dehydropantoate 2-reductase [ Gluconacetobacter diazotrophicus PAI 5]
>gi|313113024|ref|ZP — 07798663.1| 2-denydropantoate 2-reductase [ Faecalibacterium cf. prausnitzii KLE1255]
>gi|291523448|emb|CBK81741.1| ketopantoate reductase [ Coprococcus catus GD/7]
>gi|260584453|ref|ZP — 05852200.1| 2-dehydropantoate 2-reductase [ Granulicatella elegans ATCC 700633]
>gi|261415325|ref|YP — 003249008.1| 2-dehydropantoate 2-reductase [ Fibrobacter succinogenos subsp. succinogenes S85]
>gi|45184780|ref|NP — 982498.1| AAL044Cp [ Ashbya gossypii ATCC 10895]
>gi|255034556|ref|YP — 003085177.1| Ketopantoate reductase ApbA/PanE domain proten [ Dyadobacter fermentans DSM 18053]
>gi|264680193|ref|YP — 003280103.1| 2-dehydropantoate 2-reductase [ Comamonas testosteroni CNB-2]
>gi|148658426|ref|YP — 001278631.1| 2-dehydropantoate 2-reductase [ Roseiflexus sp. RS-1]
>gi|242372246|ref|ZP — 04817820.1| 2-dehydropantoate 2-reductase [ Staphylococcus epidermidis M23864W1]
>gi|225070608|ref|ZP — 03779633.1| hypothetical protein CLOHYLEM — 06710 [ Clostridium hylemonae DSM 15053]
>gi|209520519|ref|ZP — 03269277.1| 2-dehydropantoate 2-reductase [ Burkholderia sp. H160]
>gi|217963807|ref|YP — 002349485.1| 2-dehydropantoate 2-reductase [ Listeria monocytogenes HCC23]
>gi|224477588|ref|YP — 002635194.1| putative 2-dehydropantoate 2-reductase [ Staphylococcus carnosus subsp. carnosus TM300]
>gi|118462253|ref|YP — 883754.1| 2-dehydropantoate 2-reductase [ Mycobacterium avium 104]
>gi|313672571|ref|YP — 004050682.1| 2-dehydropantoate 2-reductase [ Calditerrivibrio nitroreducens DSM 19672]
>gi|85714020|ref|ZP — 01045009.1| 2-dehydropantoate 2-reductase [ Nitrobacter sp. Nb-311A]
>gi|258593851|emb|CBE70192.1| putative 2-dehydropantoate 2-reductase (Ketopantoate reductase) (KPA reductase) (KPR) [ NC 10 bacterium ‘Dutch sediment’]
>gi|160896993|ref|YP — 001562575.1| 2-dehydropantoate 2-reductase [ Delftia acidovorans SPH-1]
>gi|91779353|ref|YP — 554561.1| ketopantoate reductase ApbA/PanE [ Burkholderia xenovorans LB400]
>gi|312795995|ref|YP — 004028917.1| Ketopantoate reductase PanE/ApbA family protein [ Burkholderia rhizoxinica HKI 454]
>gi|227544674|ref|ZP — 03974723.1| 2-dehydropantoate 2-reductase [ Lactobacillus reuteri CF48-3A]
>gi|134098436|ref|YP — 001104097.1| 2-dehydropantoate 2-reductase [ Saccharoporyspora erythraea NRRL 2338]
>gi|222478734|ref|YP — 002564971.1| 2-dehydropantoate 2-reductase [ Halorubrum lacusprofundi ATCC 49239]
>gi|301061481|ref|ZP — 07202245.1| 2-dehydropantoate 2-reductase [delta proteobacterium NaphS2]
>gi|300024342|ref|YP — 003756953.1| 2-dehydropantoate 2-reductase [ Hyphomicrobium denitrificans ATCC 51888]
>gi|254443388|ref|ZP — 05056864.1| 2-dehydropantoate 2-reductase [ Verrucomicrobiae bacterium DG1235]
>gi|254457455|ref|ZP — 05070883.1| 2-dehydropantoate 2-reductase [ Campylobacterales bacterium GD 1]
>gi|189192294|ref|XP — 001932486.1| 2-dehydropantoate 2-reductase [ Pyrenophora tritici-repentis Pt-1C-BFP]
>gi|114777349|ref|ZP — 01452346.1| putative 2-dehydropantoate 2-reductase [ Mariprofundus ferrooxydans PV-1]
>gi|108805776|ref|YP — 645713.1| 2-dehydropantoate 2-reductase [ Rubrobacter xylanophilus DSM 9941]
>gi|324027764|gb|ADY14523.1| 2-dehydropantoate 2-reductase [ Spirochaeta sp. Buddy]
>gi|227509602|ref|ZP — 03939651.1| 2-dehydropantoate 2-reductase [ Lactobacillus brevis subsp. gravesensis ATCC 27305]
>gi|256847249|ref|ZP — 05552695.1| 2-dehydropantoate 2-reductase [ Lactobacillus coleohominis 101-4-CHN]
>gi|218289275|ref|ZP — 03493510.1| 2-dehydropantoate 2-reductase [ Alicyclobacillus acidocaldarius LAA1]
>gi|68164573|gb|AAY87302.1| predicted ketopantoate reductase [uncultured bacterium BAC17H8]
>gi|150016117|ref|YP — 001308371.1| 2-dehydropantoate 2-reductase [ Clostridium beijerinckii NCIMB 8052]
>gi|291550661|emb|CBL26923.1| ketopantoate reductase [ Ruminococcus torques L2-14]
>gi|163848405|ref|YP — 001636449.1| 2-dehydropantoate 2-reductase [ Chloroflexus aurantiacus J-10-fl]
>gi|302337021|ref|YP — 003802227.1| 2-dehydropantoate 2-reductase [ Spirochaeta smaragdinae DSM 11293]
>gi|253995436|ref|YP — 003047500.1| 2-dehydropantoate 2-reductase [ Methylotenera mobilis JLW8]
>gi|209966707|ref|YP — 002299622.1| 2-dehydropantoate 2-reductase [ Rhodospirillum centenum SW]
>gi|309790241|ref|ZP — 07684811.1| hypothetical protein OSCT — 0762 [ Oscillochloris trichoides DG6]
>gi|159491174|ref|XP — 001703548.1| ketopantoate reductase [ Chlamydomonas reinhardtii]
>gi|288556204|ref|YP — 003428139.1| 2-dehydropantoate 2-reductase [ Bacillus pseudofirmus OF4]
>gi|119960789|ref|YP — 946726.1| 2-dehydropantoate 2-reductase [ Arthrobacter aurescens TC1]
>gi|221209631|ref|ZP — 03582612.1| 2-dehydropantoate 2-reductase [ Burkholderia multivorans CGD1]
>gi|149927298|ref|ZP — 01915554.1| 2-dehydropantoate 2-reductase [ Limnobacter sp. MED105]
>gi|255017282|ref|ZP — 05289408.1| 2-dehydropantoate 2-reductase [ Listeria monocytogenes FSL F2-515]
>gi|295700080|ref|YP — 003607973.1| 2-dehydropantoate 2-reductase [ Burkholderia sp. CCGE1002]
>gi|209518576|ref|ZP — 03267396.1| 2-dehydropantoate 2-reductase [ Burkholderia sp. H160]
>gi|323528526|ref|YP — 004230678.1| 2-dehydropantoate 2-reductase [ Burkholderia sp. CCGE1001]
>gi|312130704|ref|YP — 003998044.1| ketopantoate reductase apba/pano domain protein [ Leadbetterella byssophila DSM 17132]
>gi|33592466|ref|NP — 880110.1| putative ketopantoate reductase [ Bordetella pertussis Tohama 1]
>gi|156740709|ref|YP — 001430838.1| 2-dehydropantoate 2-reductase [ Roseiflexus castenholzii DSM 13941]
>gi|183980885|ref|YP — 001849176.1| ketopantoate reductase, ApoA [ Mycobacterium marinum M]
>gi|315225886|ref|ZP — 07867674.1| 2-dehydropantoate 2-reductase [ Parascardovia denticolens DSM 10105]
>gi|170692978|ref|ZP — 02884139.1| 2-dehydropantoate 2-reductase [ Burkholderia graminis C4D1M]
>gi|184155218|ref|YP — 001843558.1| 2-dehydropantoate 2-reductase [ Lactobacillus fermentum IFO 3956]
>gi|229824124|ref|ZP — 04450193.1| hypothetical protein GCWU000282 — 01428 [ Catonella morbi ATCC 51271]
>gi|254557206|ref|YP — 003063623.1| 2-dehydropantoate 2-reductase [ Lactobacillus plantarum JDM1]
>gi|88812802|ref|ZP — 01128047.1| 2-dehydropantoate 2-reductase [ Nitrococcus mobilis Nb- 231]
>gi|297625706|ref|YP — 003687469.1| Putative 2-dehydropantoate 2-reductase (Ketopantoate reductase) (KPA reductase) (KPR) [ Propionibacterium freudenreichii subsp. shermanii CIRM-BIA1]
>gi|163848886|ref|YP — 001636930.1| 2-dehydropantoate 2-reductase [ Chloroflexus aurantiacus J-10-fl]
>gi|239817446|ref|YP — 002946356.1| 2-dehydropantoate 2-reductase [ Vartovorax paradoxus S110]
>gi|324314617|gb|ADY25732.1| 2-dehydropantoate 2-reductase [ Deinococcus proteolyticus MRP]
>gi|314934649|ref|ZP — 07842008.1| 2-dehydropantoate 2-reductase [ Staphylococcus caprae C87]
>gi|308270715|emb|CBX27325.1| hypothetical protein N47_H21470 [uncultured Desulfobacterium sp.]
>gi|228475460|ref|ZP — 04060178.1| 2-dehydropantoate 2-reductase [ Staphylococcus hominis SK119]
>gi|167618101|ref|ZP — 02386732.1| 2-dehydropantoate 2-reductase [ Burkholderia thailandensis Bt4]
>gi|197122126|ref|YP — 002134077.1| 2-dehydropantoate 2-reductase [ Anaeromyxobacter sp. K]
>gi|92115818|ref|YP — 575547.1| 2-dehydropantoate 2-reductase [ Nitrobacter hamburgensis X14]
>gi|107025901|ref|YP — 623412.1| 2-dehydropantoate 2-reductase [ Burkholderia cenocepacia AU 1054]
>gi|167747378|ref|ZP — 02419505.1| hypothetical protein ANACAC — 02097 [ Anaerostipes caccae DSM 14662]
>gi|149188756|ref|ZP — 01867047.1| 2-dehydropantoate 2-reductase [ Vibrio shilonii AK1]
>gi|239628405|ref|ZP — 04671436.1| ketopantoate reductase PanE/ApbA [ Clostridiales bacterium 1 — 7 — 47_FAA]
>gi|315659888|ref|ZP — 07912747.1| 2-dehydropantoate 2-reductase [ Staphylococcus lugdunensis M23590]
>gi|257454611|ref|ZP — 05619867.1| 2-dehydropantoate 2-reductase [ Enhydrobacter aerosaccus SK60]
>gi|160940948|ref|ZP — 02088288.1| hypothetical protein CLOBOL — 05840 [ Clostridium bolteae ATCC BAA-613]
>gi|167588280|ref|ZP — 02380668.1| 2-dehydropantoate 2-reductase [ Burkholderia ubonensis Bu]
>gi|159125630|gb|EDP50747.1| 2-dehydropantoate 2-reductase [ Aspergillus fumigatus A1163]
>gi|87199694|ref|YP — 496951.1| 2-dehydropantoate 2-reductase [ Novosphingobium aromaticivorans DSM 12444]
>gi|307727196|ref|YP — 003910409.1| 2-dehydropantoate 2-reductase [ Burkholderia sp. CCGE1003]
>gi|149375503|ref|ZP — 01893273.1| 2-dehydropantoate 2-reductase [ Marinobacter algicola DG893]
>gi|284992269|ref|YP — 003410823.1| 2-dehydropantoate 2-reductase [ Geodermatophilus obscurus DSM 43160]
>gi|319795820|ref|YP — 004157460.1| 2-dehydropantoate 2-reductase [ Variovorax paradoxus EPS]
>gi|311696931|gb|ADP99804.1| ketopantoate reductase ApbA/PanE [marine bacterium HP15]
>gi|220916894|ref|YP — 002492198.1| 2-dehydropantoate 2-reductase [ Anaeromyxobacter dehalogenans 2CP-1]
>gi|29832362|ref|NP — 826996.1| oxidoreductase [ Streptomyces avermitilis MA-4680]
>gi|291246372|ref|YP — 003505758.1| putative 2-dehydropantoate 2-reductase PanE [ Staphylococcus simulans bv. staphylolyticus]
>gi|73661462|ref|YP — 300243.1| 2-dehydropantoate 2-reductase [ Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305]
>gi|266619728|ref|ZP — 06112663.1| 2-dehydropantoate 2-reductase [ Clostridium hathewayi DSM 13479]
>gi|319891385|ref|YP — 004148260.1| 2-dehydropantoate 2-reductase [ Staphylococcus pseudintermedius HKU 10-03]
>gi|258512824|ref|YP — 003186258.1| 2-dehydropantoate 2-reductase [ Alicyclobacillus acidocaldarius subsp. acidocaldarius DSM 446]
>gi|296440847|ref|ZP — 06882926.1| 2-dehydropantoate 2-reductase [ Clostridium lentocellum DSM 5427]
>gi|254254805|ref|ZP — 04948122.1| Ketopantoate reductase [ Burkholderia dolosa AUO158]
>gi|222053269|ref|YP — 002535631.1| 2-dehydropantoate 2-reductase [ Geobacter sp. FRC-32]
>gi|89097458|ref|ZP — 01170347.1| 2-dehydropantoate 2-reductase [ Bacillus sp. NRRL B-14911]
>gi|298506713|gb|ADI85436.1| 2-dehydropantoate 2-reductase [ Geobacter sulfurreducens KN400]
>gi|187919138|ref|YP — 001888169.1| 2-dehydropantoate 2-reductase [ Burkholderia phytofirmans PsJN]
>gi|291246359|ref|YP — 003505745.1| putative 2-dehydropantoate 2-reductase PanE [ Staphylococcus simulans bv. staphylolyticus]
>gi|260438889|ref|ZP — 05792705.1| 2-dehydropantoate 2-reductase [ Butyrivibrio crossotus DSM 2876]
>gi|148654505|ref|YP — 001274710.1| 2-dehydropantoate 2-reductase [ Roseiflexus sp. RS-1]
>gi|162146827|ref|YP — 001601288.1| 2-dehydropantoate 2-reductase [ Gluconacetobacter diazotrophicus PAI 5]
>gi|186473315|ref|YP — 001860657.1| 2-dehydropantoate 2-reductase [ Burkholderia phymatum STM815]
>gi|209885679|ref|YP — 002289536.1| 2-dehydropantoate 2-reductase [ Oligotropha carboxidovorans OM5]
>gi|90421544|ref|YP — 529914.1| 2-dehydropantoate 2-reductase [ Rhodopseudomonas palustris BisB18]
>gi|172063745|ref|YP — 001811396.1| 2-dehydropantoate 2-reductase [ Burkholderia ambifaria MC40-6]
>gi|254555474|ref|YP — 003061891.1| 2-dehydropantoate 2-reductase [ Lactobacillus plantarum JDM1]
>gi|253701459|ref|YP — 003022648.1| 2-dehydropantoate 2-reductase [ Geobacter sp. M21]
>gi|108760447|ref|YP — 631324.1| 2-dehydropantoate 2-reductase [ Myxococcus xanthus DK 1622]
>gi|148271549|ref|YP — 001221110.1| 2-dehydropantoate 2-reductase [ Clavibacter michiganensis subsp. michiganensis NCPPB 382]
>gi|86158581|ref|YP — 465366.1| 2-dehydropantoate 2-reductase [ Anaeromyxobacter dehalogenans 2CP-C]
>gi|307823565|ref|ZP — 07653794.1| 2-dehydropantoate 2-reductase [ Methylobacter tundripaludum SV96]
>gi|169629992|ref|YP — 001703641.1| 2-dehydropantoate 2-reductase [ Mycobacterium abscessus ATCC 19977]
>gi|114561980|ref|YP — 749493.1| 2-dehydropantoate 2-reductase [ Shewanella frigidimarina NCIMB 400]
>gi|119508832|ref|ZP — 01627984.1| 2-dehydropantoate 2-reductase [ Nodularia spumigena CCY9414]
>gi|86740566|ref|YP — 480966.1| 2-dehydropantoate 2-reductase [ Frankia sp. Ccl3]
>gi|169594880|ref|XP — 001790864.1| hypothetical protein SNOG — 00170 [ Phaeosphaeria nodorum SN15]
>gi|27379715|ref|NP — 771244.1| 2-dehydropantoate 2-reductase [ Bradyrhizobium japonicum USDA 110]
>gi|284164004|ref|YP — 003402283.1| 2-dehydropantoate 2-reductase [ Haloterrigena turkmenica DSM 5511]
>gi|241661691|ref|YP — 002980051.1| 2-dehydropantoate 2-reductase [ Ralstonia pickerttii 12D]


APPENDIX 2
Polypeptides of 120-150 Amino Acids with E Value of 0.00001 or Smaller to SEQ ID NO:7 with 95% Identity and 95% Overlap Redundancy Cut-offs


>gi|15799815|ref|NP — 285827.1| aspartate alpha-decarboxylase [ Escherichia coli 0157:H7 EDL933]
>gi|39654551|pdb|1PT0|A Chain A, Unprocessed Pyruvoyl Dependent Aspartate Decarboxylase With An Alanine Insertion At Position 26
>gi|283783924|ref|YP — 003363789.1| aspartate L-decarboxylase [ Citrobacter rodentium ICC168]
>gi|290512515|ref|ZP — 06551881.1| aspartate 1-decarboxylase [ Klebsiella sp. 1 — 1 — 55]
>gi|261338866|ref|ZP — 05966724.1| hypothetical protein ENTCAN — 05063 [ Enterobacter cancerogenus ATCC 35316]
>gi|156935344|ref|YP — 001439260.1| aspartate alpha-decarboxylase [ Cronobacter sakazakii ATCC BAA-894]
>gi|283477352|emb|CAY73268.1| panD [ Erwinia pyrifoliae DSM 12163]
>gi|322834360|ref|YP — 004214387.1| aspartate 1-decarboxylase [ Rahnella sp. Y9602]
>gi|291616317|ref|YP — 003519059.1| PanD [ Pantoea ananatis LMG 20103]
>gi|317493244|ref|ZP — 07951666.1| aspartate 1-decarboxylase [ Enterobacteriaceae bacterium 9 — 2 — 54FAA]
>gi|317046954|ref|YP — 004114602.1| aspartate 1-decarboxylase [ Pantoea sp. At-9b]
>gi|251788657|ref|YP — 003003378.1| aspartate alpha-decarboxylase [ Dickeya zeae Ech1591]
>gi|261820473|ref|YP — 003258579.1| aspartate 1-decarboxylase [ Pectobacterium wasabiae WPP163]
>gi|293394524|ref|ZP — 06638820.1| aspartate 1-decarboxylase [ Serratia odorifera DSM 4582]
>gi|292489262|ref|YP — 003532149.1| aspartate 1-decarboxylase [ Erwinia amylovora CFBP1430]
>gi|300715369|ref|YP — 003740172.1| Aspartate 1-decarboxylase [ Erwinia billingiae Eb661]
>gi|197284104|ref|YP — 002149976.1| aspartate alpha-decarboxylase [ Proteus mirabilis HI4320]
>gi|238918726|ref|YP — 002932240.1| aspartate alpha-decarboxylase [ Edwardsiella ictaluri 93-146]
>gi|85058464|ref|YP — 454166.1| aspartate alpha-decarboxylase [ Sodalis glossinidius str. ‘morsitans’]
>gi|294635062|ref|ZP — 06713578.1| aspartate 1-decarboxylase [ Edwardsiella tarda ATCC 23685]
>gi|320539340|ref|ZP — 08039009.1| aspartate 1-decarboxylase [ Serratia symbiotica str. Tucson]
>gi|37524865|ref|NP — 928209.1| aspartate alpha-decarboxylase [ Photorhabdus luminescens subsp. laumondii TTO1]
>gi|290476655|ref|YP — 003469560.1| aspartate 1-decarboxylase [ Xenorhabdus bovienii SS-2004]
>gi|183600092|ref|ZP — 02961585.1| hypothetical protein PROSTU — 03624 [ Providencia stuartii ATCC 25827]
>gi|291326707|ref|ZP — 06125512.2| hypothetical protein PROVRETT — 07565 [ Providencia rettgeri DSM 1131]
>gi|212711314|ref|ZP — 03319442.1| hypothetical protein PROVALCAL — 02386 [ Providencia alcalifaciens DSM 30120]
>gi|149910516|ref|ZP — 01899156.1| aspartate 1-decarboxylase precursor [ Moritella sp. PE36]
>gi|148653905|ref|YP — 001280998.1| aspartate alpha-decarboxylase [ Psychrobacter sp. PRwf-1]
>gi|308050924|ref|YP — 003914490.1| L-aspartate 1-decarboxylase [ Ferrimonas balearica DSM 9799]
>gi|90406866|ref|ZP — 01215058.1| aspartate 1-decarboxylase precursor [ Psychromonas sp. CNPT3]
>gi|71064749|ref|YP — 263476.1| aspartate alpha-decarboxylase [ Psychrobacter arcticus 273-4]
>gi|237809047|ref|YP — 002893487.1| aspartate 1-decarboxylase [ Tolumonas auensis DSM 9187]
>gi|291613420|ref|YP — 003523577.1| aspartate 1-decarboxylase [ Sideroxydans lithotrophicus ES-1]
>gi|257455800|ref|ZP — 05621026.1| aspartate 1-decarboxylase [ Enhydrobacter aerosaccus SK60]
>gi|119944351|ref|YP — 942031.1| aspartate 1-decarboxylase [ Psychromonas ingrahamii 37]
>gi|297539336|ref|YP — 003675105.1| aspartate 1-decarboxylase [ Methylotenera sp. 301]
>gi|257094027|ref|YP — 003167668.1| aspartate alpha-decarboxylase [ Candidatus Accumulibacter phosphatis clade IIA str. UW-1]
>gi|253997254|ref|YP — 003049318.1| aspartate 1-decarboxylase [ Methylotenera mobilis JLW8]
>gi|121603845|ref|YP — 981174.1| aspartate alpha-decarboxylase [ Polaromonas naphthalenivorans CJ2]
>gi|220934056|ref|YP — 002512955.1| Aspartate 1-decarboxylase [ Thioalkalivibrio sp. HL-EbGR7]
>gi|91786803|ref|YP — 547755.1| aspartate alpha-decarboxylase [ Polaromonas sp. JS666]
>gi|253999879|ref|YP — 003051942.1| aspartate 1-decarboxylase [ Methylovorus sp. SIP3-4]
>gi|167835820|ref|ZP — 02462703.1| aspartate alpha-decarboxylase [ Burkholderia thailandensis MSMB43]
>gi|71908800|ref|YP — 286387.1| aspartate alpha-decarboxylase [ Dechloromonas aromatica RCB]
>gi|323525130|ref|YP — 004227283.1| aspartate 1-decarboxylase [ Burkholderia sp. CCGE1001]
>gi|53803579|ref|YP — 114732.1| aspartate alpha-decarboxylase [ Methylococcus capsulatus str. Bath]
>gi|302879352|ref|YP — 003847916.1| aspartate 1-decarboxylase [ Gallionella capsiferriformans ES-2]
>gi|89901803|ref|YP — 524274.1| aspartate alpha-decarboxylase [ Rhodoferax ferrireducens T118]
>gi|239820653|ref|YP — 002947838.1| aspartate 1-decarboxylase [ Variovorax paradoxus S110]
>gi|34497092|ref|NP — 901307.1| aspartate alpha-decarboxylase [ Chromobacterium violaceum ATCC 12472]
>gi|167585777|ref|ZP — 02378165.1| aspartate alpha-decarboxylase [ Burkholderia ubonensis Bu]
>gi|239815072|ref|YP — 002943982.1| aspartate 1-decarboxylase [ Variovorax paradoxus S110]
>gi|91774949|ref|YP — 544705.1| aspartate alpha-decarboxylase [ Methylobacillus flagellatus KT]
>gi|254447307|ref|ZP — 05060774.1| aspartate 1-decarboxylase [gamma proteobacterium HTCC5015]
>gi|186476949|ref|YP — 001858419.1| aspartate alpha-decarboxylase [ Burkholderia phymatum STM815]
>gi|74318073|ref|YP — 315813.1| aspartate alpha-decarboxylase [ Thiobacillus denitrificans ATCC 25259]
>gi|254429606|ref|ZP — 05043313.1| aspartate 1-decarboxylase [ Alcanivorax sp. DG881]
>gi|78067243|ref|YP — 370012.1| aspartate alpha-decarboxylase [ Burkholderia sp. 383]
>gi|169796983|ref|YP — 001714776.1| aspartate alpha-decarboxylase [ Acinetobacter baumannii AYE]
>gi|307546720|ref|YP — 003899199.1| aspartate 1-decarboxylase [ Halomonas elongata DSM 2581]
>gi|224825655|ref|ZP — 03698759.1| aspartate 1-decarboxylase [ Lutiella nitroferrum 2002]
>gi|262369399|ref|ZP — 06062727.1| aspartate 1-decarboxylase [ Acinetobacter johnsonii SH046]
>gi|262376653|ref|ZP — 06069881.1| aspartate 1-decarboxylase [ Acinetobacter lwoffii SH145]
>gi|241766440|ref|ZP — 04764313.1| aspartate 1-decarboxylase [ Acidovorax delafieldii 2AN]
>gi|161524030|ref|YP — 001579042.1| aspartate alpha-decarboxylase [ Burkholderia multivorans ATCC 17616]
>gi|288942456|ref|YP — 003444696.1| aspartate 1-decarboxylase [ Allochromatium vinosum DSM 180]
>gi|299137499|ref|ZP — 07030680.1| aspartate 1-decarboxylase [ Acidobacterium sp. MP5ACTX8]
>gi|238028348|ref|YP — 002912579.1| hypothetical protein bglu — 1g28090 [ Burkholderia glumae BGR1]
>gi|71901432|ref|ZP — 00683522.1| Aspartate decarboxylase [ Xylella fastidiosa Ann-1]
>gi|71276366|ref|ZP — 00652643.1| Aspartate decarboxylase [ Xylella fastidiosa Dixon]
>gi|94500961|ref|ZP — 01307486.1| aspartate 1-decarboxylase precursor [ Oceanobacter sp. RED65]
>gi|149927699|ref|ZP — 01915951.1| aspartate alpha-decarboxylase [ Limnobacter sp. MED 105]
>gi|90020709|ref|YP — 526536.1| aspartate 1-decarboxylase [ Saccharophagus degradans 2-40]
>gi|254491956|ref|ZP — 05105134.1| aspartate 1-decarboxylase [ Methylophaga thiooxidans DMS010]
>gi|92115182|ref|YP — 575110.1| aspartate alpha-decarboxylase [ Chromohalobacter salexigens DSM 3043]
>gi|78485863|ref|YP — 391788.1| aspartate alpha-decarboxylase [ Thiomicrospira crunogena XCL-2]
>gi|307826254|ref|ZP — 07656463.1| aspartate 1-decarboxylase [ Methylobacter tundripaludum SV96]
>gi|89093284|ref|ZP — 01166234.1| aspartate 1-decarboxylase [ Oceanospirillum sp. MED92]
>gi|146283618|ref|YP — 001173771.1| aspartate alpha-decarboxylase [ Pseudomonas stutzeri A1501]
>gi|264679999|ref|YP — 003279908.1| aspartate 1-decarboxylase [ Comamonas testosteroni CNB-2]
>gi|116052878|ref|YP — 793195.1| aspartate alpha-decarboxylase [ Pseudomonas aeruginosa UCBPP-PA14]
>gi|160897278|ref|YP — 001562860.1| aspartate alpha-decarboxylase [ Delftia acidovorans SPH-1]
>gi|121997470|ref|YP — 001002257.1| aspartate 1-decarboxylase [ Halorhodospira halophila SL1]
>gi|38372456|sp|Q848I5.1| PAND_PSEFL RecName: Full=Aspartate 1-decarboxylase;
>gi|21231219|ref|NP — 637136.1| aspartate alpha-decarboxylase [ Xanthomonas campestris pv. campestris str. ATCC 33913]
>gi|319949737|ref|ZP — 08023765.1| aspartate alpha-decarboxylase [ Dietzia cinnamea P 4]
>gi|226940325|ref|YP — 002795399.1| PanD [ Laribacter hongkongensis HLHK9]
>gi|88800686|ref|ZP — 01116245.1| aspartate 1-decarboxylase precursor [ Reinekea sp. MED297]
>gi|194365298|ref|YP — 002027908.1| aspartate alpha-decarboxylase [ Stenotrophomonas maltophilia R551-3]
>gi|254469038|ref|ZP — 05082444.1| aspartate 1-decarboxylase [beta proteobacterium KB13]
>gi|188576407|ref|YP — 001913336.1| aspartate alpha-decarboxylase [ Xanthomonas oryzae pv. oryzae PXO99A]
>gi|171059338|ref|YP — 001791687.1| aspartate 1-decarboxylase [ Leptothrix cholodnii SP-6]
>gi|121595787|ref|YP — 987683.1| aspartate alpha-decarboxylase [ Acidovorax sp. JS42]
>gi|289209202|ref|YP — 003461268.1| aspartate 1-decarboxylase [ Thioalkalivibrio sp. K90mix]
>gi|213965138|ref|ZP — 03393336.1| aspartate 1-decarboxylase [ Corynebacterium amycolatum SK46]
>gi|91787463|ref|YP — 548415.1| aspartate alpha-decarboxylase [ Polaromonas sp. JS666]
>gi|254784766|ref|YP — 003072194.1| aspartate 1-decarboxylase [ Teredinibacter turnerae T7901]
>gi|187478858|ref|YP — 786882.1| aspartate 1-decarboxylase [ Bordetella avium 197N]
>gi|114776473|ref|ZP — 01451518.1| aspartate 1-decarboxylase precursor [ Mariprofundus ferrooxydans PV-1]
>gi|226946298|ref|YP — 002801371.1| aspartate alpha-decarboxylase [ Azotobacter vinelandii DJ]
>gi|118594493|ref|ZP — 01551840.1| aspartate 1-decarboxylase precursor [ Methylophilales bacterium HTCC2181]
>gi|87118637|ref|ZP — 01074536.1| putative aspartate 1- decarboxylase [ Marinomonas sp. MED121]
>gi|285017994|ref|YP — 003375705.1| aspartate 1-decarboxylase precursor (aspartate alpha-decarboxylase) protein [ Xanthomonas albilineans GPE PC73]
>gi|83859460|ref|ZP — 00952981.1| aspartate 1-decarboxylase [ Oceanicaulis alexandrii HTCC2633]
>gi|319786659|ref|YP — 004146134.1| aspartate 1-decarboxylase [ Pseudoxanthomonas suwonensis 11-1]
>gi|152995292|ref|YP — 001340127.1| aspartate 1-decarboxylase [ Marinomonas sp. MWYL1]
>gi|194290690|ref|YP — 002006597.1| aspartate alpha-decarboxylase [ Cupriavidus taiwanensis LMG 19424]
>gi|162449208|ref|YP — 001611575.1| hypothetical protein sce0938 [ Sorangium cellulosum ‘So ce 56’]
>gi|153003251|ref|YP — 001377576.1| aspartate 1-decarboxylase [ Anaeromyxobacter sp. Fw109-5]
>gi|293604513|ref|ZP — 06686918.1| aspartate 1-decarboxylase [ Achromobacter piechaudii ATCC 43553]
>gi|289704810|ref|ZP — 06501229.1| aspartate 1-decarboxylase [ Micrococcus luteus SK58]
>gi|237749062|ref|ZP — 04579542.1| aspartate 1-decarboxylase [ Oxalobacter formigenes OXCC13]
>gi|255020069|ref|ZP — 05292141.1| Aspartate 1-decarboxylase [ Acidithiobacillus caldus ATCC51756]
>gi|119962044|ref|YP — 949406.1| aspartate 1-decarboxylase [ Arthrobacter aurescens TC1]
>gi|15805744|ref|NP — 294441.1| aspartate alpha-decarboxylase [ Deinococcus radiodurans R1]
>gi|197124548|ref|YP — 002136499.1| aspartate 1-decarboxylase [ Anaeromyxobacter sp. K]
>gi|300310032|ref|YP — 003774124.1| aspartate 1-decarboxylase precursor protein [ Herbaspirillum seropedicae SmR1]
>gi|77164404|ref|YP — 342929.1| aspartate alpha-decarboxylase [ Nitrosococcus oceani ATCC 19707]
>gi|158706108|sp|Q1IYG7.2|PAND_DEIGD RecName: Full=Aspartate 1-decarboxylase;
>gi|183985072|ref|YP — 001853363.1| aspartate 1-decarboxylase precursor PanD [ Mycobacterium marinum M]
>gi|291287339|ref|YP — 003504155.1| aspartate 1-decarboxylase [ Denitrovibrio acetiphilus DSM 12809]
>gi|302870300|ref|YP — 003838937.1| aspartate 1-decarboxylase [ Micromonospora aurantiaca ATCC 27029]
>gi|296040174|ref|ZP — 06832727.1| aspartate 1-decarboxylase [ Rhodococcus equi ATCC 33707]
>gi|153870646|ref|ZP — 02000002.1| Aspartate decarboxylase [ Beggiatoa sp. PS]
>gi|148271711|ref|YP — 001221272.1| aspartate alpha-decarboxylase [ Clavibacter michiganensis subsp. michiganensis NCPPB 382]
>gi|300690455|ref|YP — 003751450.1| aspartate 1-decarboxylase [ Ralstonia solanacearum PSI07]
>gi|292491194|ref|YP — 003526633.1| aspartate 1-decarboxylase [ Nitrosococcus halophilus Nc4]
>gi|300703064|ref|YP — 003744666.1| aspartate 1-decarboxylase [ Ralstonia solanacearum CFBP2957]
>gi|187930038|ref|YP — 001900525.1| aspartate alpha-decarboxylase [ Ralstonia pickettii 12J]
>gi|41406555|ref|NP — 959391.1| aspartate alpha-decarboxylase [ Mycobacterium avium subsp. paratuberculosis K-10]
>gi|169627646|ref|YP — 001701295.1| aspartate 1-decarboxylase precursor [ Mycobacterium abscessus ATCC 19977]
>gi|192360161|ref|YP — 001983429.1| aspartate 1-decarboxylase [ Cellvibrio japonicus Ueda107]
>gi|320094682|ref|ZP — 08026439.1| aspartate 1-decarboxylase [ Actinomyces sp. oral taxon 178 str. F0338]
>gi|283778561|ref|YP — 003369316.1| aspartate 1-decarboxylase [ Pirellula staleyi DSM 6068]
>gi|256789458|ref|ZP — 05527889.1| aspartate alpha-decarboxylase [ Streptomyces lividans TK24]
>gi|291297625|ref|YP — 003508903.1| aspartate 1-decarboxylase [ Stackebrandtia nassauensis DSM 44728]
>gi|55980575|ref|YP — 143872.1| aspartate alpha-decarboxylase [ Thermus thermophilus HB8]
>gi|120406311|ref|YP — 956140.1| aspartate alpha-decarboxylase [ Mycobacterium vanbaalenii PYR-1]
>gi|119475802|ref|ZP — 01616154.1| aspartate 1-decarboxylase precursor [marine gamma proteobacterium HTCC2143]
>gi|114319727|ref|YP — 741410.1| aspartate alpha-decarboxylase [ Alkalilimnicola ehrlichii MLHE-1]
>gi|90416572|ref|ZP — 01224503.1| aspartate 1-decarboxylase precursor [marine gamma proteobacterium HTCC2207]
>gi|184200024|ref|YP — 001854231.1| aspartate 1-decarboxylase precursor [ Kocuria rhizophila DC2201]
>gi|72162261|ref|YP — 289918.1| aspartate alpha-decarboxylase [ Thermobifida fusca YX]
>gi|154507911|ref|ZP — 02043553.1| hypothetical protein ACTODO — 00396 [ Actinomyces odontolyticus ATCC 17982]
>gi|319442411|ref|ZP — 07991567.1| aspartate alpha-decarboxylase [ Corynebacterium variabile DSM 44702]
>gi|225028053|ref|ZP — 03717245.1| hypothetical protein EUBHAL — 02322 [ Eubacterium hallii DSM 3353]
>gi|271970326|ref|YP — 003344522.1| aspartate 1-decarboxylase [ Streptosporangium roseum DSM 43021]
>gi|296138304|ref|YP — 003645547.1| aspartate 1-decarboxylase [ Tsukamurella paurometabola DSM 20162]
>gi|226304123|ref|YP — 002764081.1| aspartate 1-decarboxylase [ Rhodococcus erythropolis PR4]
>gi|145588837|ref|YP — 001155434.1| aspartate alpha-decarboxylase [ Polynucleobacter necessarius subsp. asymbioticus QLW-P1DMWA-1]
>gi|108801724|ref|YP — 641921.1| aspartate alpha-decarboxylase [ Mycobacterium sp. MCS]
>gi|323489711|ref|ZP — 08094938.1| aspartate 1-decarboxylase [ Planococcus donghaensis MPA1U2]
>gi|320450484|ref|YP — 004202580.1| aspartate 1-decarboxylase [ Thermus scotoductus SA-01]
>gi|240172844|ref|ZP — 04751503.1| aspartate alpha-decarboxylase [ Mycobacterium kansasii ATCC 12478]
>gi|148264137|ref|YP — 001230843.1| aspartate alpha-decarboxylase [ Geobacter uraniireducens Rf4]
>gi|302562209|ref|ZP — 07314551.1| aspartate 1-decarboxylase [ Streptomyces griseoflavus Tu4000]
>gi|197119382|ref|YP — 002139809.1| aspartate alpha-decarboxylase [ Geobacter bemidjiensis Bem]
>gi|15610737|ref|NP — 218118.1| aspartate alpha-decarboxylase [ Mycobacterium tuberculosis H37Rv]
>gi|159040208|ref|YP — 001539461.1| aspartate alpha-decarboxylase [ Salinispora arenicola CNS-205]
>gi|237746908|ref|ZP — 04577388.1| aspartate-1-decarboxylase [ Oxalobacter formigenes HOxBLS]
>gi|52080749|ref|YP — 079540.1| aspartate alpha-decarboxylase [ Bacillus licheniformis ATCC 14580]
>gi|296113074|ref|YP — 003627012.1| aspartate 1-decarboxylase [ Moraxella catarrhalis RH4]
>gi|111021388|ref|YP — 704360.1| aspartate alpha-decarboxylase [ Rhodococcus jostii RHA1]
>gi|298368957|ref|ZP — 06980275.1| aspartate 1-decarboxylase [ Neisseria sp. oral taxon 014 str. F0314]
>gi|315446243|ref|YP — 004079122.1| L-aspartate 1-decarboxylase [ Mycobacterium sp. Spyr1]
>gi|297190372|ref|ZP — 06907770.1| aspartate 1-decarboxylase [ Streptomyces pristinaespiralis ATCC 25486]
>gi|315924106|ref|ZP — 07920332.1| aspartate 1-decarboxylase [ Pseudoramibacter alactolyticus ATCC 23263]
>gi|15677149|ref|NP — 274302.1| aspartate alpha-decarboxylase [ Neisseria meningitidis MC58]
>gi|239980059|ref|ZP — 04702583.1| aspartate alpha-decarboxylase [ Streptomyces albus J1074]
>gi|15827028|ref|NP — 301291.1| aspartate alpha-decarboxylase [ Mycobacterium leprae TN]
>gi|116672429|ref|YP — 833362.1| aspartate alpha-decarboxylase [ Arthrobacter sp. FB24]
>gi|229918730|ref|YP — 002887376.1| aspartate 1-decarboxylase [ Exiguobacterium sp. AT 1b]
>gi|238020351|ref|ZP — 04600777.1| hypothetical protein GCWU000324 — 00231 [ Kingella oralis ATCC 51147]
>gi|163840966|ref|YP — 001625371.1| aspartate alpha-decarboxylase [ Renibacterium salmoninarum ATCC 33209]
>gi|68535357|ref|YP — 250062.1| aspartate alpha-decarboxylase [ Corynebacterium jeikeium K411]
>gi|117927421|ref|YP — 871972.1| L-aspartate 1-decarboxylase [ Acidothermus cellulolyticus 11B]
>gi|124268753|ref|YP — 001022757.1| aspartate alpha-decarboxylase [ Methylibium petroleiphilum PM1]
>gi|220914411|ref|YP — 002489720.1| aspartate 1-decarboxylase [ Arthrobacter chlorophenolicus A6]
>gi|108758834|ref|YP — 634947.1| aspartate 1-decarboxylase [ Myxococcus xanthus DK 1622]
>gi|269218264|ref|ZP — 06162118.1| aspartate 1-decarboxylase [ Actinomyces sp. oral taxon 848 str. F0332]
>gi|311743353|ref|ZP — 07717160.1| aspartate 1-decarboxylase [ Aeromicrobium marinum DSM 15272]
>gi|145596791|ref|YP — 001161088.1| aspartate alpha-decarboxylase [ Salinispora tropica CNB-440]
>gi|198284767|ref|YP — 002221088.1| aspartate 1-decarboxylase [ Acidithiobacillus ferrooxidans ATCC 53993]
>gi|308178526|ref|YP — 003917932.1| aspartate 1-decarboxylase [ Arthrobacter arilaitensis Re117]
>gi|255065696|ref|ZP — 05317551.1| aspartate 1-decarboxylase [ Neisseria sicca ATCC 29256]
>gi|88810485|ref|ZP — 01125742.1| aspartate 1-decarboxylase precursor [ Nitrococcus mobilis Nb-231]
>gi|158706097|sp|A1SDW8.2|PAND_NOCSJ RecName: Full=Aspartate 1-decarboxylase;
>gi|172041372|ref|YP — 001801086.1| aspartate alpha-decarboxylase [ Corynebacterium urealyticum DSM 7109]
>gi|291297729|ref|YP — 003509007.1| aspartate 1-decarboxylase [ Stackebrandtia nassauensis DSM 44728]
>gi|294675086|ref|YP — 003575702.1| aspartate 1-decarboxylase [ Prevotella ruminicola 23]
>gi|291519794|emb|CBK75015.1| L-aspartate 1-decarboxylase [ Butyrivibrio fibrisolvens 16/4]
>gi|78042854|ref|YP — 361172.1| aspartate alpha-decarboxylase [ Carboxydothermus hydrogenoformans Z-2901]
>gi|54022371|ref|YP — 116613.1| aspartate alpha-decarboxylase [ Nocardia farcinica IFM 10152]
>gi|153815600|ref|ZP — 01968268.1| hypothetical protein RUMTOR — 01836 [ Ruminococcus torques ATCC 27756]
>gi|119952798|ref|YP — 950285.1| aspartate 1-decarboxylase [ Arthrobacter aurescens TC1]
>gi|118581933|ref|YP — 903183.1| aspartate alpha-decarboxylase [ Pelobacter propionicus DSM 2379]
>gi|308174032|ref|YP — 003920737.1| aspartate 1-decarboxylase [ Bacillus amyloliquefaciens DSM 7]
>gi|227498405|ref|ZP — 03928551.1| aspartate alpha-decarboxylase [ Acidaminococcus sp. D21]
>gi|261880070|ref|ZP — 06006497.1| aspartate 1-decarboxylase [ Prevotella bergensis DSM 17361]
>gi|284989228|ref|YP — 003407782.1| aspartate 1-decarboxylase [ Geodermatophilus obscurus DSM 43160]
>gi|89099887|ref|ZP — 01172759.1| aspartate 1-decarboxylase precursor [ Bacillus sp. NRRL B-14911]
>gi|296271376|ref|YP — 003654008.1| aspartate 1-decarboxylase [ Thermobispora bispora DSM 43833]
>gi|168698967|ref|ZP — 02731244.1| hypothetical protein GobsU — 05571 [ Gemmata obscuriglobus UQM 2246]
>gi|220929206|ref|YP — 002506115.1| aspartate 1-decarboxylase [ Clostridium cellulolyticum H10]
>gi|84495005|ref|ZP — 00994124.1| aspartate 1-decarboxylase precursor [ Janibacter sp. HTCC2649]
>gi|291547262|emb|CBL20370.1| L-aspartate 1-decarboxylase [ Ruminococcus sp. SR1/5]
>gi|298246275|ref|ZP — 06970081.1| aspartate 1-decarboxylase [ Ktedonobacter racemifer DSM 44963]
>gi|150017466|ref|YP — 001309720.1| aspartate alpha-decarboxylase [ Clostridium beijerinckii NCIMB 8052]
>gi|300934633|ref|ZP — 07149889.1| aspartate alpha-decarboxylase [ orynebacterium resistens DSM 45100]
>gi|269124634|ref|YP — 003298004.1| aspartate 1-decarboxylase [ Thermomonospora curvata DSM 43183]
>gi|269128681|ref|YP — 003302051.1| aspartate 1-decarboxylase [ Thermomonospora curvata DSM 43183]
>gi|307244703|ref|ZP — 07526806.1| aspartate 1-decarboxylase [ Peptostreptococcus stomatis DSM 17678]
>gi|282862735|ref|ZP — 06271796.1| aspartate 1-decarboxylase [ Streptomyces sp. ACTE]
>gi|227494386|ref|ZP — 03924702.1| aspartate 1-decarboxylase [ Actinomyces coleocanis DSM 15436]
>gi|268316317|ref|YP — 003290036.1| aspartate 1-decarboxylase [ Rhodothermus marinus DSM 4252]
>gi|226312091|ref|YP — 002771985.1| aspartate 1-decarboxylase precursor [ Brevibacillus brevis NBRC 100599]
>gi|308069472|ref|YP — 003871077.1| Aspartate 1-decarboxylase precursor (Aspartate alpha-decarboxylase) [ Paenibacillus polymyxa E681]
>gi|121535059|ref|ZP — 01666876.1| aspartate 1-decarboxylase [ Thermosinus carboxydivorans Nor1]
>gi|29376392|ref|NP — 815546.1| aspartate alpha-decarboxylase [ Enterococcus faecalis V583]
>gi|172057787|ref|YP — 001814247.1| aspartate 1-decarboxylase [ Exiguobacterium sibiricum 255-15]
>gi|289522732|ref|ZP — 06439586.1| aspartate 1-decarboxylase [ Anaerobaculum hydrogeniformans ATCC BAA-1850]
>gi|315605842|ref|ZP — 07880874.1| aspartate 1-decarboxylase [ Actinomyces sp. oral taxon 180 str. F0310]
>gi|255994546|ref|ZP — 05427681.1| aspartate 1-decarboxylase [ Eubacterium saphenum ATCC 49989]
>gi|251796457|ref|YP — 003011188.1| aspartate 1-decarboxylase [ Paenibacillus sp. JDR-2]
>gi|54295766|ref|YP — 128181.1| aspartate alpha-decarboxylase [ Legionella pneumophila str. Lens]
>gi|258654511|ref|YP — 003203667.1| aspartate 1-decarboxylase [ Nakamurella multipartita DSM 44233]
>gi|311068755|ref|YP — 003973678.1| aspartate alpha-decarboxylase [ Bacillus atrophaeus 1942]
>gi|229544027|ref|ZP — 04433086.1| aspartate 1-decarboxylase [ Bacillus coagulans 36D1]
>gi|257068435|ref|YP — 003154690.1| L-aspartate 1-decarboxylase [ Brachybacterium faecium DSM 4810]
>gi|256753469|ref|ZP — 05494262.1| aspartate 1-decarboxylase [ Clostridium papyrosolvens DSM 2782]
>gi|324980408|gb|EGC16074.1| aspartate 1-decarboxylase [ Kingella denitrificans ATCC 33394]
>gi|225075174|ref|ZP — 03718373.1| hypothetical protein NEIFLAOT — 00174 [ Neisseria flavescens NRL30031/H210]
>gi|258510312|ref|YP — 003183746.1| aspartate 1-decarboxylase [ Alicyclobacillus acidocaldarius subsp. acidocaldarius DSM 446]
>gi|309813243|ref|ZP — 07706964.1| aspartate 1-decarboxylase [ Dermacoccus sp. Ellin185]
>gi|77919424|ref|YP — 357239.1| aspartate alpha-decarboxylase [ Pelobacter carbinolicus DSM 2380]
>gi|124009556|ref|ZP — 01694230.1| aspartate 1-decarboxylase [ Microscilla marina ATCC 23134]
>gi|320007101|gb|ADW01951.1| aspartate 1-decarboxylase [ Streptomyces flavogriseus ATCC 33331]
>gi|299538597|ref|ZP — 07051880.1| aspartate 1-decarboxylase precursor [ Lysinibacillus fusiformis ZC1]
>gi|225017697|ref|ZP — 03706889.1| hypothetical protein CLOSTMETH — 01626 [ Clostridium methylpentosum DSM 5476]
>gi|256397482|ref|YP — 003119046.1| aspartate 1-decarboxylase [ Catenulispora acidiphila DSM 44928]
>gi|320006702|gb|ADW01552.1| aspartate 1-decarboxylase [ Streptomyces flavogriseus ATCC 33331]
>gi|323471151|gb|ADX74836.1| L-aspartate 1-decarboxylase [ Arthrobacter phenanthrenivorans Sphe3]
>gi|25026691|ref|NP — 736745.1| aspartate alpha-decarboxylase [ Corynebacterium efficiens YS-314]
>gi|16079298|ref|NP — 390122.1| aspartate alpha-decarboxylase [ Bacillus subtilis subsp. subtilis str. 168]
>gi|319790447|ref|YP — 004152080.1| aspartate 1-decarboxylase [ Thermovibrio ammonificans HB-1]
>gi|251779952|ref|ZP — 04822872.1| aspartate 1-decarboxylase [ Clostridium botulinum E1 str. ‘BoNT E Beluga’]
>gi|167462328|ref|ZP — 02327417.1| aspartate alpha-decarboxylase [ Paenibacillus larvae subsp. larvae BRL-230010]
>gi|225025397|ref|ZP — 03714589.1| hypothetical protein EIKCOROL — 02295 [ Eikenella corrodens ATCC 23834]
>gi|291279242|ref|YP — 003496077.1| aspartate 1 -decarboxylase [ Deferribacter desulfuricans SSM1]
>gi|311896800|dbj|BAJ29208.1| putative L-aspartate 1-decarboxylase [ Kitasatospora setae KM-6054]
>gi|169827548|ref|YP — 001697706.1| aspartate 1-decarboxylase [ Lysinibacillus sphaericus C3-41]
>gi|299134421|ref|ZP — 07027614.1| aspartate 1-decarboxylase [ Afipia sp. 1NLS2]
>gi|242372243|ref|ZP — 04817817.1| aspartate alpha-decarboxylase [ Staphylococcus epidermidis M23864:W1]
>gi|226325379|ref|ZP — 03800897.1| hypothetical protein COPCOM — 03181 [ Coprococcus comes ATCC 27758]
>gi|284029184|ref|YP — 003379115.1| aspartate 1-decarboxylase [ Kribbella flavida DSM 17836]
>gi|319651315|ref|ZP — 08005445.1| aspartate 1-decarboxylase [ Bacillus sp. 2_A — 57_CT2]
>gi|254496676|ref|ZP — 05109539.1| aspartate alpha-decarboxylase [ Legionella drancourtii LLAP12]
>gi|256833308|ref|YP — 003162035.1| aspartate 1-decarboxylase [ Jonesia denitrificans DSM 20603]
>gi|261417985|ref|YP — 003251667.1| aspartate 1-decarboxylase [ Geobacillus sp. Y412MC61]
>gi|302876569|ref|YP — 0038452021| aspartate 1-decarboxylase [ Clostridium cellulovorans 743B]
>gi|212638969|ref|YP — 002315489.1| aspartate alpha-decarboxylase [ Anoxybacillus flavithermus WK1]
>gi|15896169|ref|NP — 349518.1| aspartate alpha-decarboxylase [ Clostridium acetobutylicum ATCC 824]
>gi|304406905|ref|ZP — 07388559.1| aspartate 1-decarboxylase [ Paenibacillus curdlanolyticus YK9]
>gi|317128616|ref|YP — 004094898.1| aspartate 1-decarboxylase [ Bacillus cellulosilyticus DSM 2522]
>gi|149183103|ref|ZP — 01861554.1| aspartate 1-decarboxylase precursor [ Bacillus sp. SG-1]
>gi|169335507|ref|ZP — 02862700.1| hypothetical protein ANASTE — 01921 [ Anaerofustis stercorihominis DSM 17244]
>gi|197303353|ref|ZP — 03168393.1| hypothetical protein RUMLAC — 02076 [ Ruminococcus lactaris ATCC 29176]
>gi|268608082|ref|ZP — 06141811.1| aspartate alpha-decarboxylase [ Ruminococcus flavefaciens FD-1]
>gi|294789798|ref|ZP — 06755027.1| aspartate 1-decarboxylase [ Simonsiella muelleri ATCC 29453]
>gi|49484793|ref|YP — 042017.1| aspartate alpha-decarboxylase [ Staphylococcus aureus subsp. aureus MRSA252]
>gi|28377460|ref|NP — 784352.1| aspartate alpha-decarboxylase [ Lactobacillus plantarum WCFS1]
>gi|182418494|ref|ZP — 02949787.1| aspartate 1-decarboxylase [ Clostridium butyricum 5521]
>gi|302553297|ref|ZP — 07305639.1| aspartate 1-decarboxylase [ Streptomyces viridochromogenes DSM 40736]
>gi|159896918|ref|YP — 001543165.1| aspartate 1-decarboxylase [ Herpetosiphon aurantiacus ATCC 23779]
>gi|114570673|ref|YP — 757353.1| aspartate alpha-decarboxylase [ Maricaulis maris MCS10]
>gi|239827468|ref|YP — 002950092.1| aspartate 1-decarboxylase [ Geobacillus sp. WCH70]
>gi|323465432|gb|ADX77585.1| aspartate 1-decarboxylase [ Staphylococcus pseudintermedius ED99]
>gi|182434568|ref|YP — 001822287.1| aspartate alpha-decarboxylase [ Streptomyces griseus subsp. griseus NBRC 13350]
>gi|149178749|ref|ZP — 01857332.1| aspartate 1-decarboxylase [ Planctomyces maris DSM 8797]
>gi|297616344|ref|YP — 003701503.1| aspartate 1-decarboxylase [ Syntrophothermus lipocalidus DSM 12680]
>gi|83816527|ref|YP — 445536.1| aspartate 1-decarboxylase [ Salinibacter ruber DSM 13855]
>gi|288556128|ref|YP — 003428063.1| aspartate alpha-decarboxylase [ Bacillus pseudofirmus OF4]
>gi|239635857|ref|ZP — 04676881.1| aspartate 1-decarboxylase [ Staphylococcus warneri L37603]
>gi|302342373|ref|YP — 003806902.1| aspartate 1-decarboxylase [ Desulfarculus baarsii DSM 2075]
>gi|146297697|ref|YP — 001181468.1| aspartate 1-decarboxylase [ Caldicellulosiruptor saccharolyticus DSM 8903]
>gi|147676557|ref|YP — 001210772.1| aspartate alpha-decarboxylase [ Pelotomaculum thermopropionicum SI]
>gi|138895755|ref|YP — 001126208.1| aspartate alpha-decarboxylase [ Geobacillus thermodenitrificans NG80-2]
>gi|193215499|ref|YP — 001996698.1| aspartate alpha-decarboxylase [ Chloroherpeton thalassium ATCC 35110]
>gi|270158276|ref|ZP — 06186933.1| aspartate 1-decarboxylase [ Legionella longbeachae D-4968]
>gi|154483470|ref|ZP — 02025918.1| hypothetical protein EUBVEN — 01174 [ Eubacterium ventriosum ATCC 27560]
>gi|19551386|ref|NP — 599388.1| aspartate alpha-decarboxylase [ Corynebacterium glutamicum ATCC 13032]
>gi|269956437|ref|YP — 003326226.1| aspartate 1-decarboxylase [ Xylanimonas cellulosilytica DSM 15894]
>gi|154491071|ref|ZP — 02031012.1| hypothetical protein PARMER — 00990 [ Parabacteroides merdae ATCC 43184]
>gi|164511440|emb|CAN89641.1| putative aspartate-1-decarboxylase precursor [ Streptomyces collinus]
>gi|284044344|ref|YP — 003394684.1| aspartate 1-decarboxylase [ Conexibacter woesei DSM 14684]
>gi|300786909|ref|YP — 003767200.1| aspartate 1-decarboxylase [ Amycolatopsis mediterranei U32]
>gi|118443940|ref|YP — 877157.1| aspartate alpha-decarboxylase [ Clostridium novyi NT]
>gi|294671143|ref|ZP — 06735998.1| hypothetical protein NEIELOOT — 02851 [ Neisseria elongata subsp. glycolytica ATCC 29315]
>gi|317499217|ref|ZP — 07957492.1| aspartate decarboxylase [ Lachnospiraceae bacterium 5 — 1 — 63FAA]
>gi|300087723|ref|YP — 003758245.1| aspartate 1-decarboxylase [ Dehalogenimonas lykanthroporepellens BL-DC-9]
>gi|312792944|ref|YP — 004025867.1| aspartate 1-decarboxylase [ Caldicellulosiruptor kristjanssonii 177R1B]
>gi|253577525|ref|ZP — 04854838.1| aspartate 1-decarboxylase [ Paenibacillus sp. oral taxon 786 str. D14]
>gi|304364119|ref|ZP — 07361364.1| aspartate 1-decarboxylase [ Actinomyces viscosus C505]
>gi|70725184|ref|YP — 252098.1| aspartate alpha-decarboxylase [ Staphylococcus haemolyticus JCSC1435]
>gi|238924848|ref|YP — 002938364.1| aspartate 1-decarboxylase [ Eubacterium rectale ATCC 33656]
>gi|167748367|ref|ZP — 02420494.1| hypothetical protein ANACAC — 03111 [ Anaerostipes caccae DSM 14662]
>gi|294498158|ref|YP — 003561858.1| aspartate 1-decarboxylase [ Bacillus megaterium QM B1551]
>gi|229172278|ref|ZP — 04299842.1| Aspartate 1-decarboxylase alpha chain [ Bacillus cereus MM3]
>gi|89892958|ref|YP — 516445.1| aspartate alpha-decarboxylase [ Desulfitobacterium hafniense Y51]
>gi|158312064|ref|YP — 001504572.1| aspartate alpha-decarboxylase [ Frankia sp. EAN1 pec]
>gi|303257894|ref|ZP — 07343903.1| aspartate 1-decarboxylase [ Burkholderiales bacterium 1 — 1 — 47]
>gi|296131758|ref|YP — 003639005.1| aspartate 1-decarboxylase [ Thermincola sp. JR]
>gi|288817983|ref|YP — 003432330.1| aspartate 1-decarboxylase [ Hydrogenobacter thermophilus TK-6]
>gi|291246356|ref|YP — 003505742.1| putative aspartate alpha-decarboxylase PanD [ Staphylococcus simulans bv. staphylolyticus]
>gi|188996356|ref|YP — 001930607.1| aspartate 1-decarboxylase [ Sulfurihydrogenibium sp. YO3AOP1]
>gi|160894028|ref|ZP — 02074807.1| hypothetical protein CLOL250 — 01583 [ Clostridium sp. L2-50]
>gi|228475771|ref|ZP — 04060489.1| aspartate 1-decarboxylase [ Staphylococcus hominis SK119]
>gi|56963830|ref|YP — 175561.1| aspartate alpha-decarboxylase [ Bacillus clausii KSM-K16]
>gi|82548277|gb|ABB82968.1| putative aspartate decarboxylase [uncultured organism HF70 — 19B12]
>gi|148244908|ref|YP — 001219602.1| aspartate alpha-decarboxylase [ Candidatus Vesicomyosocius okutanii HA]
>gi|153855966|ref|ZP — 01996907.1| hypothetical protein DORLON — 02932 [ Dorea longicatena DSM 13814]
>gi|226947534|ref|YP — 002802625.1| aspartate 1-decarboxylase [ Clostridium botulinum A2 str. Kyoto]
>gi|297568701|ref|YP — 003690045.1| aspartate 1-decarboxylase [ Desulfurivibrio alkaliphilus AHT2]
>gi|289548459|ref|YP — 003473447.1| aspartate 1-decarboxylase [ Thermocrinis albus DSM 14484]
>gi|225180974|ref|ZP — 03734422.1| aspartate 1-decarboxylase [ Dethiobacter alkaliphilus AHT 1]
>gi|117165150|emb|CAJ88706.1| putative L-aspartate-alpha-decarboxylase [ Streptomyces ambofaciens ATCC 23877]
>gi|317123772|ref|YP — 004097884.1| L-aspartate 1-decarboxylase [ Intrasporangium calvum DSM 43043]
>gi|294055934|ref|YP — 003549592.1| aspartate 1-decarboxylase [ Coraliomargarita akajimensis DSM 45221]
>gi|15614252|ref|NP — 242555.1| aspartate alpha-decarboxylase [ Bacillus halodurans C-125]
>gi|297560480|ref|YP — 003679454.1| aspartate 1-decarboxylase [ Nocardiopsis dassonvillei subsp. dassonvillei DSM 43111]
>gi|295094090|emb|CBK83181.1| L-aspartate 1-decarboxylase [ Coprococcus sp. ART55/1]
>gi|312197107|ref|YP — 004017168.1| aspartate 1-decarboxylase [ Frankia sp. Eul1c]
>gi|302038222|ref|YP — 003798544.1| aspartate 1-decarboxylase [ Candidatus Nitrospira defluvii]
>gi|294640899|ref|ZP — 06718851.1| aspartate 1-decarboxylase [ Ruminococcus albus 8]
>gi|227548075|ref|ZP — 03978124.1| aspartate alpha-decarboxylase [ Corynebacterium lipophiloflavum DSM 44291]
>gi|314934646|ref|ZP — 07842005.1| aspartate 1-decarboxylase [ Staphylococcus caprae C87]
>gi|258405137|ref|YP — 003197879.1| aspartate 1-decarboxylase [ Desulfohalobium retbaense DSM 5692]
>gi|302538161|ref|ZP — 07290503.1| aspartate 1-decarboxylase [ Streptomyces sp. C]
>gi|87308237|ref|ZP — 01090378.1| aspartate 1-decarboxylase precursor [ Blastopirellula marina DSM 3645]
>gi|269797992|ref|YP — 003311892.1| aspartate 1-decarboxylase [ Veillonella parvula DSM 2008]
>gi|21673091|ref|NP — 661156.1| aspartate alpha-decarboxylase [ Chlorobium tepidum TLS]
>gi|225851045|ref|YP — 002731279.1| aspartate alpha-decarboxylase [ Persephonella marina EX-H1]
>gi|119356218|ref|YP — 910862.1| aspartate alpha-decarboxylase [ Chlorobium phaeobacteroides DSM 266]
>gi|323141842|ref|ZP — 08076706.1| aspartate 1-decarboxylase [ Phascolarctobacterium sp. YIT 12067]
>gi|15605956|ref|NP — 213333.1| aspartate alpha-decarboxylase [ Aquifex aeolicus VF5]
>gi|317052380|ref|YP — 004113496.1| aspartate 1-decarboxylase [ Desulfurispirillum indicum S5]
>gi|163782147|ref|ZP — 02177146.1| aspartate 1-decarboxylase precursor [ Hydrogenivirga sp. 128-5-R1-1]
>gi|125973417|ref|YP — 001037327.1| aspartate alpha-decarboxylase [ Clostridium thermocellum ATCC 27405]
>gi|315647107|ref|ZP — 07900220.1| aspartate 1-decarboxylase [ Paenibacillus vortex V453]
>gi|152993855|ref|YP — 001359576.1| aspartate decarboxylase [ Sulfurovum sp. NBC37-1]
>gi|16803939|ref|NP — 465424.1| aspartate alpha-decarboxylase [ Listeria monocytogenes EGD-e]
>gi|29833787|ref|NP — 828421.1| aspartate alpha-decarboxylase [ Streptomyces avermitilis MA-4680]
>gi|167629397|ref|YP — 001679896.1| aspartate 1-decarboxylase [ Heliobacterium modesticaldum Ice1]
>gi|157692740|ref|YP — 001487202.1| aspartate alpha-decarboxylase [ Bacillus pumilus SAFR-032]
>gi|258513596|ref|YP — 003189818.1| aspartate 1-decarboxylase [ Desulfotomaculum acetoxidans DSM 771]
>gi|320105461|ref|YP — 004181051.1| aspartate 1-decarboxylase [ Terriglobus saanensis SP1PR4]
>gi|238019295|ref|ZP — 04599721.1| hypothetical protein VEIDISOL — 01159 [ Veillonella dispar ATCC 17748]
>gi|261406085|ref|YP — 003242326.1| aspartate 1-decarboxylase [ Paenibacillus sp. Y412MC10]
>gi|323703659|ref|ZP — 08115301.1| aspartate 1-decarboxylase [ Desulfotomaculum nigrificans DSM 574]
>gi|254389556|ref|ZP — 05004782.1| aspartate 1-decarboxylase [ Streptomyces clavuligerus ATCC 27064]
>gi|163813891|ref|ZP — 02205285.1| hypothetical protein COPEUT — 00044 [ Coprococcus eutactus ATCC 27759]
>gi|118473676|ref|YP — 884441.1| aspartate alpha-decarboxylase [ Mycobacterium smegmatis str. MC2 155]
>gi|242243653|ref|ZP — 04798097.1| aspartate alpha-decarboxylase [ Staphylococcus epidermidis W23144]
>gi|295840549|ref|ZP — 06827482.1| aspartate 1-decarboxylase [ Streptomyces sp. SPB74]
>gi|229084647|ref|ZP — 04216915.1| Aspartate 1-decarboxylase alpha chain [ Bacillus cereus Rock3-44]
>gi|193213421|ref|YP — 001999374.1| aspartate alpha-decarboxylase [ Chlorobaculum parvum NCIB 8327]
>gi|78189411|ref|YP — 379749.1| aspartate alpha-decarboxylase [ Chlorobium chlorochromatii CaD3]
>gi|262203861|ref|YP — 003275069.1| aspartate 1-decarboxylase [ Gordonia bronchialis DSM 43247]
>gi|57237347|ref|YP — 178360.1| aspartate alpha-decarboxylase [ Campylobacter jejuni RM1221]
>gi|110597596|ref|ZP — 01385881.1| aspartate 1-decarboxylase [ Chlorobium ferrooxidans DSM 13031]
>gi|224477558|ref|YP — 002635164.1| putative aspartate 1-decarboxylase [ Staphylococcus carnosus subsp. carnosus TM300]
>gi|311900398|dbj|BAJ32806.1| putative L-aspartate 1-decarboxylase [ Kitasatospora setae KM-6054]
>gi|228472221|ref|ZP — 04056987.1| aspartate 1-decarboxylase [ Capnocytophaga gingivalis ATCC 33624]
>gi|212696954|ref|ZP — 03305082.1| hypothetical protein ANHYDRO — 01517 [ Anaerococcus hydrogenalis DSM 7454]
>gi|152975064|ref|YP — 001374581.1| aspartate alpha-decarboxylase [ Bacillus cereus subsp. cytotoxis NVH 391-98]
>gi|311030322|ref|ZP — 07708412.1| aspartate alpha-decarboxylase [ Bacillus sp. m3-13]
>gi|23099218|ref|NP — 692684.1| aspartate alpha-decarboxylase [ Oceanobacillus iheyensis HTE831]
>gi|183983171|ref|YP — 001851462.1| aspartate 1-decarboxylase precursor PanD — 2 [ Mycobacterium marinum M]
>gi|306820308|ref|ZP — 07453947.1| aspartate 1-decarboxylase [ Eubacterium yurii subsp. margaretiae ATCC 43715]
>gi|312621811|ref|YP — 004023424.1| aspartate 1-decarboxylase [ Caldicellulosiruptor kronotskyensis 2002]
>gi|239927316|ref|ZP — 04684269.1| aspartate alpha-decarboxylase [ Streptomyces ghanaensis ATCC 14672]
>gi|295696300|ref|YP — 003589538.1| aspartate 1-decarboxylase [ Bacillus tusciae DSM 2912]
>gi|303238877|ref|ZP — 07325408.1| aspartate 1-decarboxylase [ Acetivibrio cellulolyticus CD2]
>gi|289435249|ref|YP — 003465121.1| hypothetical protein Ise — 1886 [ Listeria seeligeri serovar 1/2b str. SLCC3954]
>gi|302555661|ref|ZP — 07308003.1| aspartate 1-decarboxylase [ Streptomyces viridochromogenes DSM 40736]
>gi|297584390|ref|YP — 003700170.1| aspartate 1-decarboxylase [ Bacillus selenitireducens MLS10]
>gi|291532722|emb|CBL05835.1| L-aspartate 1-decarboxylase [ Megamonas hypermegale ART12/1]
>gi|167041215|gb|ABZ05972.1| putative aspartate decarboxylase [uncultured marine microorganism HF4000 — 001N02]
>gi|168181292|ref|ZP — 02615956.1| aspartate 1-decarboxylase [ Clostridium botulinum Bf]
>gi|134298040|ref|YP — 001111536.1| aspartate 1-decarboxylase [ Desulfotomaculum reducens MI-1]
>gi|124514996|gb|EAY56507.1| Aspartate 1-decarboxylase [ Leptospirillum rubarum]
>gi|195953149|ref|YP — 002121439.1| aspartate 1-decarboxylase [ Hydrogenobaculum sp. Y04AAS1]
>gi|229102244|ref|ZP — 04232953.1| Aspartate 1-decarboxylase alpha chain [ Bacillus cereus Rock3-28]
>gi|319955894|ref|YP — 004167157.1| l-aspartate 1-decarboxylase [ Nitratifractor salsuginis DSM 16511]
>gi|227819486|ref|YP — 002823457.1| aspartate alpha-decarboxylase [ Sinorhizobium fredii NGR234]
>gi|134299644|ref|YP — 001113140.1| aspartate 1-decarboxylase [ Desulfotomaculum reducens MI-1]
>gi|78187623|ref|YP — 375666.1| aspartate alpha-decarboxylase [ Chlorobium luteolum DSM 273]
>gi|294632508|ref|ZP — 06711068.1| aspartate 1-decarboxylase [ Streptomyces sp. e14]
>gi|218246666|ref|YP — 002372037.1| aspartate 1-decarboxylase [ Cyanothece sp. PCC 8801]
>gi|153954248|ref|YP — 001395013.1| aspartate alpha-decarboxylase [ Clostridium kluyveri DSM 555]
>gi|240145726|ref|ZP — 04744327.1| aspartate 1-decarboxylase [ Roseburia intestinalis L1-82]
>gi|187777515|ref|ZP — 02993988.1| hypothetical protein CLOSPO — 01106 [ Clostridium sporogenes ATCC 15579]
>gi|189345854|ref|YP — 001942383.1| aspartate 1-decarboxylase [ Chlorobium limicola DSM 245]
>gi|225849174|ref|YP — 002729338.1| aspartate alpha-decarboxylase [ Sulfurihydrogenibium azorense Az-Fu1]
>gi|42524914|ref|NP — 970294.1| aspartate alpha-decarboxylase [ Bdellovibrio bacteriovorus HD100]
>gi|296124338|ref|YP — 003632116.1| aspartate 1-decarboxylase [ Planctomyces limnophilus DSM 3776]
>gi|260592486|ref|ZP — 05857944.1| aspartate 1-decarboxylase [ Prevotella veroralis F0319]
>gi|224373697|ref|YP — 002608069.1| aspartate alpha-decarboxylase [ Nautilia profundicola AmH]
>gi|290955740|ref|YP — 003486922.1| L-aspartate-alpha-decarboxylase [ Streptomyces scabiei 87.22]
>gi|169830320|ref|YP — 001716302.1| aspartate 1-decarboxylase [ Candidatus Desulforudis audaxviator MP104C]
>gi|154246282|ref|YP — 001417240.1| aspartate alpha-decarboxylase [ Xanthobacter autotrophics Py2]
>gi|194335559|ref|YP — 002017353.1| aspartate 1-decarboxylase [ Pelodictyon phaeoclathratiforme BU-1]
>gi|315187531|gb|EFU21287.1| L-aspartate 1-decarboxylase [ Spirochaeta thermophila DSM 6578]
>gi|145220354|ref|YP — 001131063.1| aspartate alpha-decarboxylase [ Prosthecochloris vibrioformis DSM 265]
>gi|206890877|ref|YP — 002249664.1| aspartate 1-decarboxylase [ Thermodesulfovibrio yellowstonii DSM 11347]
>gi|315303837|ref|ZP — 07874325.1| aspartate 1-decarboxylase [ Listeria ivanovii FSL F6-596]
>gi|257065635|ref|YP — 003151891.1| aspartate 1-decarboxylase [ Anaerococcus prevotii DSM 20548]
>gi|299821666|ref|ZP — 07053554.1| aspartate 1-decarboxylase [ Listeria grayi DSM 20601]
>gi|254458768|ref|ZP — 05072192.1| aspartate 1-decarboxylase [ Campylobacterales bacterium GD 1]
>gi|209526587|ref|ZP — 03275112.1| aspartate 1-decarboxylase [ Arthrospira maxima CS-328]
>gi|242310629|ref|ZP — 04809784.1| aspartate 1-decarboxylase [ Helicobacter pullorum MIT 98-5489]
>gi|260888452|ref|ZP — 05899715.1| aspartate 1-decarboxylase [ Selenomonas sputigena ATCC 35185]
>gi|116747816|ref|YP — 844503.1| aspartate 1-decarboxylase [ Syntrophobacter fumaroxidans MPOB]
>gi|149195160|ref|ZP — 01872251.1| aspartate alpha-decarboxylase [ Caminibacter mediatlanticus TB-2]
>gi|237750942|ref|ZP — 04581422.1| aspartate alpha-decarboxylase [ Helicobacter bilis ATCC 43879]
>gi|189499388|ref|YP — 001958858.1| aspartate alpha-decarboxylase [ Chlorobium phaeobacteroides BS1]
>gi|313142475|ref|ZP — 07804668.1| aspartate 1-decarboxylase [ Helicobacter canadensis MIT 98-5491]
>gi|78776535|ref|YP — 392850.1| aspartate alpha-decarboxylase [ Sulfurimonas denitrificans DSM 1251]
>gi|312879261|ref|ZP — 07739061.1| L-aspartate 1-decarboxylase [ Aminomonas paucivorans DSM 12260]
>gi|313683409|ref|YP — 004061147.1| l-aspartate 1-decarboxylase [ Sulfuricurvum kujiense DSM 16994]
>gi|290968108|ref|ZP — 06559653.1| aspartate 1-decarboxylase [ Megasphaera genomosp. type — 1 str. 28L]
>gi|94269421|ref|ZP — 01291457.1| Aspartate 1-decarboxylase [delta proteobacterium MLMS-1]
>gi|34557994|ref|NP — 907809.1| aspartate alpha-decarboxylase [ Wolinella succinogenes DSM 1740]
>gi|83589014|ref|YP — 429023.1| aspartate alpha-decarboxylase [ Moorella thermoacetica ATCC 39073]
>gi|288904380|ref|YP — 003429601.1| aspartate 1-decarboxylase [ Streptococcus gallolyticus UCN34]
>gi|256546079|ref|ZP — 05473432.1| aspartate 1-decarboxylase [ Anaerococcus vaginalis ATCC 51170]
>gi|84687580|ref|ZP — 01015455.1| aspartate 1-decarboxylase precursor [ Maritimibacter alkaliphilus HTCC2654]
>gi|319440712|ref|ZP — 07989868.1| aspartate alpha-decarboxylase [ Corynebacterium variabile DSM 44702]
>gi|152990004|ref|YP — 001355726.1| aspartate alpha-decarboxylase [ Nitratiruptor sp. SB155-2]
>gi|196229549|ref|ZP — 03128414.1| aspartate 1-decarboxylase [ Chthoniobacter flavus Ellin428]
>gi|310778937|ref|YP — 003967270.1| L-aspartate 1-decarboxylase [ Ilyobacter polytropus DSM 2926]
>gi|194333223|ref|YP — 002015083.1| aspartate alpha-decarboxylase [ Prosthecochloris aestuarii DSM 271]
>gi|307720220|ref|YP — 003891360.1| L-aspartate 1-decarboxylase [ Sulfurimonas autotrophica DSM 16294]
>gi|317057177|ref|YP — 004105644.1| aspartate 1-decarboxylase [ Ruminococcus albus 7]
>gi|281358405|ref|ZP — 06244887.1| aspartate 1-decarboxylase [ Victivallis vadensis ATCC BAA-548]
>gi|13474851|ref|NP — 106421.1| aspartate alpha-decarboxylase [ Mesorhizobium loti MAFF303099]
>gi|270308113|ref|YP — 003330171.1| aspartate 1-decarboxylase [ Dehalococcoides sp. VS]
>gi|324963812|gb|ADY54591.1| L-aspartate 1-decarboxylase [ Syntrophobotulus glycolicus DSM 8271]
>gi|13488064|ref|NP — 085658.1| aspartate alpha-decarboxylase [ Mesorhizobium loti MAFF303099]
>gi|315638262|ref|ZP — 07893443.1| aspartate 1-decarboxylase [ Campylobacter upsaliensis JV21]
>gi|171778858|ref|ZP — 02919920.1| hypothetical protein STRINF — 00779 [ Streptococcus infantarius subsp. infantarius ATCC BAA-102]
>gi|17231061|ref|NP — 487609.1| aspartate alpha-decarboxylase [ Nostoc sp. PCC 7120]
>gi|317121598|ref|YP — 004101601.1| L-aspartate 1-decarboxylase [ Thermaerobacter marianensis DSM 12885]
>gi|225163545|ref|ZP — 03725856.1| Aspartate 1-decarboxylase [ Opitutaceae bacterium TAV2]
>gi|224437987|ref|ZP — 03658926.1| aspartate alpha-decarboxylase [ Helicobacter cinaedi CCUG 18818]
>gi|237752532|ref|ZP — 04583012.1| aspartate alpha-decarboxylase [ Helicobacter winghamensis ATCC BAA-430]
>gi|157736689|ref|YP — 001489372.1| aspartate alpha-decarboxylase [ Arcobacter butzleri RM4018]
>gi|317152682|ref|YP — 004120730.1| aspartate 1-decarboxylase [ Desulfovibrio aespoeensis Aspo-2]
>gi|298491519|ref|YP — 003721696.1| aspartate 1-decarboxylase [ ‘Nostoc azollae’ 0708]
>gi|268680556|ref|YP — 003304987.1| aspartate 1-decarboxylase [ Sulfurospirillum deleyianum DSM 6946]
>gi|269792079|ref|YP — 003316983.1| aspartate 1-decarboxylase [ Thermanaerovibrio acidaminovorans DSM 6589]
>gi|158335510|ref|YP — 001516682.1| aspartate alpha-decarboxylase [ Acaryochloris marina MBIC11017]
>gi|91204562|emb|CAJ70790.1| strongly similar to aspartate 1-decarboxylase precursor (aspartate alpha-decarboxylase) [ Candidatus Kuenenia stuttgartiensis]
>gi|288573810|ref|ZP — 06392167.1| aspartate 1-decarboxylase [ Dethiosulfovibrio peptidovorans DSM 11002]
>gi|289432636|ref|YP — 003462509.1| aspartate 1-decarboxylase [ Dehalococcoides sp. GT]
>gi|182677509|ref|YP — 001831655.1| aspartate alpha-decarboxylase [ Beijerinckia indica subsp. indica ATCC 9039]
>gi|229004643|ref|ZP — 04162381.1| aspartate alpha-decarboxylase [ Bacillus mycoides Rock1-4]
>gi|119512431|ref|ZP — 01631513.1| aspartate 1-decarboxylase precursor [ Nodularia spumigena CCY9414]
>gi|269839249|ref|YP — 003323941.1| aspartate 1-decarboxylase [ Thermobaculum terrenum ATCC BAA-798]
>gi|186682855|ref|YP — 001866051.1| aspartate alpha-decarboxylase [ Nostoc punctiforme PCC 73102]
>gi|258511926|ref|YP — 003185360.1| aspartate 1-decarboxylase [ Alicyclobacillus acidocaldarius subsp. acidocaldarius DSM 446]
>gi|218288596|ref|ZP — 03492873.1| aspartate 1-decarboxylase [ Alicyclobacillus acidocaldarius LAA1]
>gi|282896795|ref|ZP — 06304801.1| Aspartate decarboxylase [ Raphidiopsis brookii D9]
>gi|206896045|ref|YP — 002246959.1| aspartate 1-decarboxylase [ Coprothermobacter proteolyticus DSM 5265]
>gi|320012833|gb|ADW07683.1| aspartate 1-decarboxylase [ Streptomyces flavogriseus ATCC 33331]
>gi|323700614|ref|ZP — 08112526.1| aspartate 1-decarboxylase [ Desulfovibrio sp. ND132]
>gi|37523797|ref|NP — 927174.1| aspartate alpha-decarboxylase [ Gloeobacter violaceus PCC 7421]
>gi|296272234|ref|YP — 003654865.1| aspartate 1-decarboxylase [ Arcobacter nitrofigilis DSM 7299]
>gi|119872877|ref|YP — 930884.1| aspartate 1-decarboxylase [ Pyrobaculum islandicum DSM 4184]
>gi|226312675|ref|YP — 002772569.1| aspartate 1-decarboxylase precursor [ Brevibacillus brevis NBRC 100599]
>gi|282900379|ref|ZP — 06308329.1| Aspartate decarboxylase [ Cylindrospermopsis raciborskii CS-505]
>gi|307151736|ref|YP — 003887120.1| aspartate 1-decarboxylase [ Cyanothece sp. PCC 7822]
>gi|222100611|ref|YP — 002535179.1| Aspartate 1-decarboxylase precursor [ Thermotoga neapolitana DSM 4359]
>gi|320102432|ref|YP — 004178023.1| L-aspartate 1-decarboxylase [ Isosphaera pallida ATCC 43644]
>gi|322378504|ref|ZP — 08052954.1| Aspartate 1-decarboxylase precursor [ Helicobacter suis HS1]
>gi|217076689|ref|YP — 002334405.1| aspartate alpha-decarboxylase [ Thermosipho africanus TCF52B]
>gi|315497331|ref|YP — 004086135.1| aspartate 1-decarboxylase [ Asticcacaulis excentricus CB 48]
>gi|166366461|ref|YP — 001658734.1| aspartate alpha-decarboxylase [ Microcystis aeruginosa NIES-843]
>gi|220904255|ref|YP — 002479567.1| Aspartate 1-decarboxylase [ Desulfovibrio desulfuricans subsp. desulfuricans str. ATCC 27774]
>gi|57339838|gb|AAW49906.1| hypothetical protein FTT1391 [synthetic construct]
>gi|16331671|ref|NP — 442399.1| aspartate alpha-decarboxylase [ Synechocystis sp. PCC 6803]
>gi|303327013|ref|ZP — 07357455.1| aspartate 1-decarboxylase [ Desulfovibrio sp. 3 — 1_syn3]
>gi|67460926|sp|Q7VJB2.2|PAND_HELHP RecName: Full=Aspartate 1-decarboxylase;