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Information on EC 1.1.1.290 - 4-phosphoerythronate dehydrogenase
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EC Tree
1.1.1.290 4-phosphoerythronate dehydrogenaseIUBMB Comments
This enzyme catalyses a step in a bacterial pathway for the biosynthesis of pyridoxal 5'-phosphate. The enzyme contains a tightly-bound NAD(H) cofactor that is not re-oxidized by free NAD+. In order to re-oxidize the cofactor and restore enzyme activity, the enzyme catalyses the reduction of a 2-oxo acid (such as 2-oxoglutarate, oxaloacetate, or pyruvate) to the respective (R)-hydroxy acid . cf. EC 1.1.1.399, 2-oxoglutarate reductase.
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Word Map
- 1.1.1.290
-
2-hydroxyacid
- pyridoxine
-
salvage
- dehydrogenases
- aeruginosa
-
homodimeric
- pyridoxal
- 5'-phosphate
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
erythronate-4-phosphate dehydrogenase, 4-phosphoerythronate dehydrogenase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
erythronate-4-phosphate dehydrogenase
pdx gene product
PDXB
additional information
PdxB is a member of the D-isomer specific 2-hydroxyacid dehydrogenase superfamily
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-phospho-D-erythronate + NAD+ = (3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + NADH + H+
-
-
-
-
4-phospho-D-erythronate + NAD+ = (3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + NADH + H+
substrate recognition and catalytic mechanism, PdxB contains the conserved His254/Glu237/Arg208 triad
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SYSTEMATIC NAME
IUBMB Comments
4-phospho-D-erythronate:NAD+ 2-oxidoreductase
This enzyme catalyses a step in a bacterial pathway for the biosynthesis of pyridoxal 5'-phosphate. The enzyme contains a tightly-bound NAD(H) cofactor that is not re-oxidized by free NAD+. In order to re-oxidize the cofactor and restore enzyme activity, the enzyme catalyses the reduction of a 2-oxo acid (such as 2-oxoglutarate, oxaloacetate, or pyruvate) to the respective (R)-hydroxy acid [6]. cf. EC 1.1.1.399, 2-oxoglutarate reductase.
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CAS REGISTRY NUMBER
COMMENTARY
125858-75-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + NADH + H+
L-2-hydroxyglutarate + NAD+
-
stereospecific reaction
-
-
?
4-phospho-D-erythronate + NAD+
2-oxo-3-hydroxy-4-phospho-butanoate + NADH + H+
-
multiple turnovers requiring 2-oxo acids for re-oxidation of NADH bound to the enzyme PdxB a coupled assay with the enzymes SerC and PdxA following in the bioyntetic pathway, overview
-
-
?
erythronate-4-phosphate + NAD+
(3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + NADH
reaction in pathway leading from erythrose-4-phosphate and glutamate to nitrogen 1 and carbon 5,5', and 6 of the pyridoxine ring
-
-
?
erythronate-4-phosphate + NAD+
3-hydroxy-4-phospho-hydroxy-alpha-ketobutyrate + NADH
-
-
-
-
?
4-phospho-D-erythronate + NAD+
(3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + NADH
-
-
-
?
4-phospho-D-erythronate + NAD+
(3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + NADH
the enzyme is involved in biosynthesis of pyridoxal-5'-phosphate
-
-
?
4-phospho-D-erythronate + NAD+
2-oxo-3-hydroxy-4-phospho-butanoate + NADH
-
-
-
-
?
4-phospho-D-erythronate + NAD+
2-oxo-3-hydroxy-4-phospho-butanoate + NADH
-
-
-
-
?
4-phospho-D-erythronate + NAD+
3-hydroxy-2-oxo-4-(phosphonooxy)butanoate + NADH + H+
-
-
-
-
r
4-phospho-D-erythronate + NAD+
3-hydroxy-2-oxo-4-(phosphonooxy)butanoate + NADH + H+
-
-
-
-
r
additional information
?
-
pdxB is the first gene in the pdxB-hisT operon
-
-
?
additional information
?
-
the enzyme mediates a step in the biosynthesis of the coenzyme pyridoxal 5'-phosphate. Transcription of pdxB gene is positively growth rate regulated. PdxB-specific transcript remains unchanged during amino acid starvation in wild-type and relA mutant strains
-
-
?
additional information
?
-
-
2,6-dichloroindolphenol, N-nitrosodimethylamine, and methylene blue cannot be reduced in the presence of the enzyme and 4-phospho-D-erythronate
-
-
?
additional information
?
-
-
2-oxoglutarate, oxaloacetic acid, and pyruvate are equally good subtrates for the enzyme
-
-
?
additional information
?
-
-
2,6-dichloroindolphenol, N-nitrosodimethylamine, and methylene blue cannot be reduced in the presence of the enzyme and 4-phospho-D-erythronate
-
-
?
additional information
?
-
-
2-oxoglutarate, oxaloacetic acid, and pyruvate are equally good subtrates for the enzyme
-
-
?
additional information
?
-
active site and ligand binding structure, overview
-
-
?
additional information
?
-
-
active site and ligand binding structure, overview
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-phospho-D-erythronate + NAD+
(3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + NADH
the enzyme is involved in biosynthesis of pyridoxal-5'-phosphate
-
-
?
erythronate-4-phosphate + NAD+
(3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + NADH
reaction in pathway leading from erythrose-4-phosphate and glutamate to nitrogen 1 and carbon 5,5', and 6 of the pyridoxine ring
-
-
?
4-phospho-D-erythronate + NAD+
2-oxo-3-hydroxy-4-phospho-butanoate + NADH
-
-
-
-
?
4-phospho-D-erythronate + NAD+
2-oxo-3-hydroxy-4-phospho-butanoate + NADH
-
-
-
-
?
4-phospho-D-erythronate + NAD+
3-hydroxy-2-oxo-4-(phosphonooxy)butanoate + NADH + H+
-
-
-
-
r
4-phospho-D-erythronate + NAD+
3-hydroxy-2-oxo-4-(phosphonooxy)butanoate + NADH + H+
-
-
-
-
r
additional information
?
-
pdxB is the first gene in the pdxB-hisT operon
-
-
?
additional information
?
-
the enzyme mediates a step in the biosynthesis of the coenzyme pyridoxal 5'-phosphate. Transcription of pdxB gene is positively growth rate regulated. PdxB-specific transcript remains unchanged during amino acid starvation in wild-type and relA mutant strains
-
-
?
additional information
?
-
-
2,6-dichloroindolphenol, N-nitrosodimethylamine, and methylene blue cannot be reduced in the presence of the enzyme and 4-phospho-D-erythronate
-
-
?
additional information
?
-
-
2,6-dichloroindolphenol, N-nitrosodimethylamine, and methylene blue cannot be reduced in the presence of the enzyme and 4-phospho-D-erythronate
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
PdxB contains tightly bound NAD+ and/or NADH that cannot be removed by extensive dialysis
-
NAD+
NAD+ is bound to the C-terminal side of the beta-sheet of the nucleotide-binding domain in both subunits of PdxB, binding structure, overview
NADH
-
the enzyme contains a tightly bound NADH, the released cofactor is 10% NAD+ and 90% NADH
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-2-hydroxyglutarate
-
competitive versus 4-phospho-D-erythronate, noncompetitive versus 2-oxoglutarate
D-2-hydroxyglutaric acid
-
competitive inhibitor vs. 4-phospho-D-erythronate and a noncompetitive inhibitor vs. alpha-oxoglutarate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.093
2-oxoglutarate
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
0.086
oxaloacetic acid
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
0.128
pyruvate
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
0.0029
4-phospho-D-erythronate
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
2-oxoglutarate
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
1.1
oxaloacetic acid
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
1.3
pyruvate
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
1.4
4-phospho-D-erythronate
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11
2-oxoglutarate
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
13
oxaloacetic acid
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
9.9
pyruvate
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
6700
4-phospho-D-erythronate
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.017
D-2-hydroxyglutarate
-
pH 8.0, 22°C, recombinant enzyme, versus 2-oxoglutarate
0.03
D-2-hydroxyglutarate
-
pH 8.0, 22°C, recombinant enzyme, versus 4-phospho-D-erythronate
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.102
D-2-hydroxyglutaric acid
Escherichia coli
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
2
L-2-hydroxyglutaric acid
Escherichia coli
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
-
pyridoxal phosphate biosynthesis in Escherichia coli is quite different from the more widely used Pdx1/Pdx2-dependent pathway. Escherichia coli uses seven enzymes in a bifurcated pathway that converts pyruvate, glyceraldehyde-3-phosphate, and erythrose-4-phosphate to pyridoxal phosphate via the intermediates 1-deoxy-D-xylulose 5-phosphate and 1-amino-propan-2-one-3-phosphate. PdxB catalyzes the second step in the biosynthesis of pyridoxal phosphate by oxidizing 4-phospho-D-erythronate to 2-oxo-3-hydroxy-4-phospho-butanoate with concomitant reduction
metabolism
-
pyridoxal phosphate biosynthesis in Escherichia coli is quite different from the more widely used Pdx1/Pdx2-dependent pathway. Escherichia coli uses seven enzymes in a bifurcated pathway that converts pyruvate, glyceraldehyde-3-phosphate, and erythrose-4-phosphate to pyridoxal phosphate via the intermediates 1-deoxy-D-xylulose 5-phosphate and 1-amino-propan-2-one-3-phosphate. PdxB catalyzes the second step in the biosynthesis of pyridoxal phosphate by oxidizing 4-phospho-D-erythronate to 2-oxo-3-hydroxy-4-phospho-butanoate with concomitant reduction
-
physiological function
the pdxB gene, encoding erythronate-4-phosphate dehydrogenase, is required for de novo vitamin B6 biosynthesis. Mutation in pdxB causes growth deficiency of Photorhabdus luminescens in nutrient-poor medium, which is restored under nutrient-rich conditions or by supplementation with pyridoxal 5'-phosphate. Supplementation with pyridoxal, pyridoxine, and pyridoxamine also restores the growth of the pdxB mutant. Supplementation with pyridoxal 5'-phosphate restores the virulence-deficient phenotype against Caenorhabditis elegans
physiological function
Photorhabdus luminescens DSM 15139
-
the pdxB gene, encoding erythronate-4-phosphate dehydrogenase, is required for de novo vitamin B6 biosynthesis. Mutation in pdxB causes growth deficiency of Photorhabdus luminescens in nutrient-poor medium, which is restored under nutrient-rich conditions or by supplementation with pyridoxal 5'-phosphate. Supplementation with pyridoxal, pyridoxine, and pyridoxamine also restores the growth of the pdxB mutant. Supplementation with pyridoxal 5'-phosphate restores the virulence-deficient phenotype against Caenorhabditis elegans
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDXB_ACIAD
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
355
0
39464
Swiss-Prot
-
PDXB_ACIB3
Acinetobacter baumannii (strain AB307-0294)
355
0
39426
Swiss-Prot
-
PDXB_ACIB5
Acinetobacter baumannii (strain AB0057)
355
0
39426
Swiss-Prot
-
PDXB_ACIBC
Acinetobacter baumannii (strain ACICU)
355
0
39431
Swiss-Prot
-
PDXB_ACIBS
Acinetobacter baumannii (strain SDF)
355
0
39312
Swiss-Prot
-
PDXB_ACIBT
Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377)
355
0
39488
Swiss-Prot
-
PDXB_ACIBY
Acinetobacter baumannii (strain AYE)
355
0
39426
Swiss-Prot
-
PDXB_AERHH
Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049)
376
0
41143
Swiss-Prot
-
PDXB_RUTMC
Ruthia magnifica subsp. Calyptogena magnifica
345
0
38919
Swiss-Prot
-
PDXB_SACD2
Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024)
373
0
40728
Swiss-Prot
-
PDXB_SALAR
Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980)
378
0
41345
Swiss-Prot
-
PDXB_SALCH
Salmonella choleraesuis (strain SC-B67)
378
0
41298
Swiss-Prot
-
PDXB_SALDC
Salmonella dublin (strain CT_02021853)
378
0
41279
Swiss-Prot
-
PDXB_SALEP
Salmonella enteritidis PT4 (strain P125109)
378
0
41279
Swiss-Prot
-
PDXB_SALG2
Salmonella gallinarum (strain 287/91 / NCTC 13346)
378
0
41279
Swiss-Prot
-
PDXB_SALHS
Salmonella heidelberg (strain SL476)
378
0
41298
Swiss-Prot
-
PDXB_SALPA
Salmonella paratyphi A (strain ATCC 9150 / SARB42)
378
0
41384
Swiss-Prot
-
PDXB_SALPB
378
0
41298
Swiss-Prot
-
PDXB_SALPC
Salmonella paratyphi C (strain RKS4594)
378
0
41298
Swiss-Prot
-
PDXB_SALPK
Salmonella paratyphi A (strain AKU_12601)
378
0
41384
Swiss-Prot
-
PDXB_SALRD
Salinibacter ruber (strain DSM 13855 / M31)
392
0
41521
Swiss-Prot
-
PDXB_SALSV
Salmonella schwarzengrund (strain CVM19633)
378
0
41279
Swiss-Prot
-
PDXB_SALTY
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
378
0
41298
Swiss-Prot
-
PDXB_PSEA6
Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087)
374
0
41342
Swiss-Prot
-
PDXB_PSEA8
Pseudomonas aeruginosa (strain LESB58)
380
0
41086
Swiss-Prot
-
PDXB_PSEAB
Pseudomonas aeruginosa (strain UCBPP-PA14)
380
0
41039
Swiss-Prot
-
PDXB_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
380
0
41002
Swiss-Prot
-
PDXB_PSEE4
Pseudomonas entomophila (strain L48)
383
0
41798
Swiss-Prot
-
PDXB_PSEF5
Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)
380
0
41897
Swiss-Prot
-
PDXB_PSEFS
Pseudomonas fluorescens (strain SBW25)
380
0
41490
Swiss-Prot
-
PDXB_PSEP1
Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1)
380
0
41609
Swiss-Prot
-
PDXB_PSEPF
Pseudomonas fluorescens (strain Pf0-1)
380
0
41369
Swiss-Prot
-
PDXB_PSEPK
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
380
0
41614
Swiss-Prot
-
PDXB_PSESM
Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
380
0
41573
Swiss-Prot
-
PDXB_PSET1
Pseudoalteromonas translucida (strain TAC 125)
373
0
40787
Swiss-Prot
-
PDXB_PSEU2
Pseudomonas syringae pv. syringae (strain B728a)
380
0
41376
Swiss-Prot
-
PDXB_PSYA2
Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4)
377
0
41608
Swiss-Prot
-
PDXB_PSYCK
Psychrobacter cryohalolentis (strain ATCC BAA-1226 / DSM 17306 / VKM B-2378 / K5)
386
0
42643
Swiss-Prot
-
PDXB_SHIB3
Shigella boydii serotype 18 (strain CDC 3083-94 / BS512)
378
0
41306
Swiss-Prot
-
PDXB_SHIBS
Shigella boydii serotype 4 (strain Sb227)
378
0
41279
Swiss-Prot
-
PDXB_SHIDS
Shigella dysenteriae serotype 1 (strain Sd197)
378
0
41338
Swiss-Prot
-
PDXB_SHIF8
Shigella flexneri serotype 5b (strain 8401)
378
0
41337
Swiss-Prot
-
PDXB_SODGM
Sodalis glossinidius (strain morsitans)
377
0
40428
Swiss-Prot
-
PDXB_TERTT
Teredinibacter turnerae (strain ATCC 39867 / T7901)
370
0
39575
Swiss-Prot
-
PDXB_TOLAT
Tolumonas auensis (strain DSM 9187 / TA4)
373
0
41335
Swiss-Prot
-
PDXB_VESOH
Vesicomyosocius okutanii subsp. Calyptogena okutanii (strain HA)
345
0
39077
Swiss-Prot
-
PDXB_VIBCH
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
381
0
41865
Swiss-Prot
-
PDXB_VIBPA
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
377
0
41658
Swiss-Prot
-
PDXB_WIGBR
378
0
42967
Swiss-Prot
-
PDXB_YERE8
Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)
375
0
41323
Swiss-Prot
-
PDXB_YERP3
Yersinia pseudotuberculosis serotype O:1b (strain IP 31758)
375
0
41167
Swiss-Prot
-
PDXB_YERPA
Yersinia pestis bv. Antiqua (strain Antiqua)
375
0
41167
Swiss-Prot
-
PDXB_YERPB
Yersinia pseudotuberculosis serotype IB (strain PB1/+)
375
0
41167
Swiss-Prot
-
PDXB_ECO24
Escherichia coli O139:H28 (strain E24377A / ETEC)
378
0
41516
Swiss-Prot
-
PDXB_ECO27
Escherichia coli O127:H6 (strain E2348/69 / EPEC)
378
0
41337
Swiss-Prot
-
PDXB_ECO45
Escherichia coli O45:K1 (strain S88 / ExPEC)
378
0
41320
Swiss-Prot
-
PDXB_ECO55
Escherichia coli (strain 55989 / EAEC)
378
0
41334
Swiss-Prot
-
PDXB_ECO5E
Escherichia coli O157:H7 (strain EC4115 / EHEC)
378
0
41298
Swiss-Prot
-
PDXB_ECO7I
Escherichia coli O7:K1 (strain IAI39 / ExPEC)
378
0
41333
Swiss-Prot
-
PDXB_ECOBW
Escherichia coli (strain K12 / MC4100 / BW2952)
378
0
41368
Swiss-Prot
-
PDXB_ECODH
Escherichia coli (strain K12 / DH10B)
378
0
41368
Swiss-Prot
-
PDXB_ECOL5
Escherichia coli O6:K15:H31 (strain 536 / UPEC)
378
0
41319
Swiss-Prot
-
PDXB_ECOL6
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
378
0
41347
Swiss-Prot
-
PDXB_ECOLC
Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks)
378
0
41378
Swiss-Prot
-
PDXB_ECOLU
Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC)
378
0
41292
Swiss-Prot
-
PDXB_ECOSM
Escherichia coli (strain SMS-3-5 / SECEC)
378
0
41347
Swiss-Prot
-
PDXB_ECOUT
Escherichia coli (strain UTI89 / UPEC)
378
0
41320
Swiss-Prot
-
PDXB_EDWI9
Edwardsiella ictaluri (strain 93-146)
375
0
40521
Swiss-Prot
-
PDXB_ESCF3
Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73)
378
0
41404
Swiss-Prot
-
PDXB_HAHCH
Hahella chejuensis (strain KCTC 2396)
381
0
42089
Swiss-Prot
-
PDXB_HYDCU
Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2)
375
0
42174
Swiss-Prot
-
PDXB_IDILO
Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR)
381
0
42036
Swiss-Prot
-
PDXB_LEGPA
Legionella pneumophila (strain Paris)
350
0
38952
Swiss-Prot
-
PDXB_LEGPH
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
350
0
38952
Swiss-Prot
-
PDXB_LEGPL
Legionella pneumophila (strain Lens)
350
0
38943
Swiss-Prot
-
PDXB_MARN8
Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8)
384
0
42533
Swiss-Prot
-
PDXB_PECAS
Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672)
378
0
41282
Swiss-Prot
-
PDXB_PECCP
Pectobacterium carotovorum subsp. carotovorum (strain PC1)
378
0
41233
Swiss-Prot
-
PDXB_PHOLL
Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01)
375
0
41413
Swiss-Prot
-
PDXB_PHOPR
Photobacterium profundum (strain SS9)
391
0
42695
Swiss-Prot
-
PDXB_PORGI
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
369
0
40669
Swiss-Prot
-
PDXB_PSE14
Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
380
0
41174
Swiss-Prot
-
PDXB_ALCBS
Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2)
371
0
39938
Swiss-Prot
-
PDXB_ALIF1
Aliivibrio fischeri (strain ATCC 700601 / ES114)
376
0
41844
Swiss-Prot
-