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Information on EC 1.1.1.37 - malate dehydrogenase and Organism(s) Escherichia coli and UniProt Accession P61889

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EC Tree
     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.37 malate dehydrogenase
IUBMB Comments
There are several forms of malate dehydrogenases that differ by their use of substrate and cofactors. This NAD+-dependent enzyme forms oxaloacetate and unlike EC 1.1.1.38, malate dehydrogenase (oxaloacetate-decarboxylating), is unable to convert it to pyruvate. Also oxidizes some other 2-hydroxydicarboxylic acids. cf. EC 1.1.1.82, malate dehydrogenase (NADP+); EC 1.1.1.299, malate dehydrogenase [NAD(P)+]; and EC 1.1.5.4, malate dehydrogenase (quinone).
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This record set is specific for:
Escherichia coli
UNIPROT: P61889
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
malate dehydrogenase, mdh, mitochondrial malate dehydrogenase, malic dehydrogenase, cytosolic malate dehydrogenase, maldh, nad-dependent malate dehydrogenase, mitochondrial mdh, s-mdh, l-malate dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malate dehydrogenase
-
(R)-2-hydroxyacid dehydrogenase
-
-
-
-
L-malate dehydrogenase
-
-
-
-
L-malate:NAD oxidoreductase
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malate (NAD) dehydrogenase
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-
-
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malate dehydrogenase (NAD)
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-
-
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malic acid dehydrogenase
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-
-
-
malic dehydrogenase
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-
-
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mbNAD-MDH
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-
-
-
mNAD-MDH
-
-
-
-
NAD+-dependent malate dehydrogenase
-
-
NAD-dependent malate dehydrogenase
-
-
-
-
NAD-dependent malic dehydrogenase
-
-
-
-
NAD-L-malate dehydrogenase
-
-
-
-
NAD-linked malate dehydrogenase
-
-
-
-
NAD-malate dehydrogenase
-
-
-
-
NAD-malic dehydrogenase
-
-
-
-
NAD-specific malate dehydrogenase
-
-
-
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VEG69
-
-
-
-
Vegetative protein 69
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
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reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
(S)-malate:NAD+ oxidoreductase
There are several forms of malate dehydrogenases that differ by their use of substrate and cofactors. This NAD+-dependent enzyme forms oxaloacetate and unlike EC 1.1.1.38, malate dehydrogenase (oxaloacetate-decarboxylating), is unable to convert it to pyruvate. Also oxidizes some other 2-hydroxydicarboxylic acids. cf. EC 1.1.1.82, malate dehydrogenase (NADP+); EC 1.1.1.299, malate dehydrogenase [NAD(P)+]; and EC 1.1.5.4, malate dehydrogenase (quinone).
CAS REGISTRY NUMBER
COMMENTARY hide
9001-64-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-malate + NAD+
oxaloacetate + NADH + H+
show the reaction diagram
malate + NAD+
oxaloacetate + NADH + H+
show the reaction diagram
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
show the reaction diagram
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
show the reaction diagram
-
-
-
-
r
citrate + NAD+
? + NADH
show the reaction diagram
-
-
-
-
?
malate + NAD+
oxaloacetate + NADH + H+
show the reaction diagram
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
show the reaction diagram
-
-
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-malate + NAD+
oxaloacetate + NADH + H+
show the reaction diagram
malate + NAD+
oxaloacetate + NADH + H+
show the reaction diagram
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
show the reaction diagram
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
show the reaction diagram
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
show the reaction diagram
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
-
the ribose from NAD+ interacts with residues Gly10, Gly11, Ile12, Gly78, Val79, Asn119, Tyr33, Asp34, Ala77, Ile97, Leu101, Ser76, Ile117, Val146, and Met227
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
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MDH activity is strongly inhibited by excess of oxaloacetate and NADH
oxaloacetate
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MDH activity is strongly inhibited by excess of oxaloacetate and NADH
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.6 - 6.8
L-malate
0.26 - 0.5
NAD+
0.052 - 0.087
NADH
0.04 - 3
oxaloacetate
0.00012
(S)-malate
-
pH and temperature not specified in the publication
0.00087
NAD+
-
pH and temperature not specified in the publication
0.023 - 0.056
oxaloacetate
additional information
additional information
-
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.77 - 931
oxaloacetate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
mutant N122C-L305C
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
2-dimensional electrophoresis, recombinant enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
increased enzyme content in cells grown on acid media
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32200
2 * 32200, calculated from amino acid sequence
64400
calculated from amino acid sequence
33500
-
4 * 33500
56000
-
gel filtration
60000
60000 - 67000
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sedimentation equilibrium centrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 32200, calculated from amino acid sequence
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method, using 100 mM N-(2-acetamido)-iminodiacetic acid pH 6.5, 0.2 M sodium acetate, 30% (w/v) PEG MME 5000, 5% (v/v) glycerol
crystal structure determination and analysis
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F144I
site-directed mutagenesis, inactive mutant
G210A
site-directed mutagenesis, the mutant shows 30% reduced activity compared to the wild-type enzyme
G210A/V214I
site-directed mutagenesis, the double mutant shows a 2.2fold increase in lacatate dehydrogenase activity compared to the wild-type enzyme
I12V/R81Q/M85E/G210A/V214I
construction of a pentamutant by site-directed mutagenesis, whose substrate specificity is switched from malate dehydrogenase to that of lactate dehydrogenase, EC 1.1.1.27, the mutant shows highly reduced activity compared to the wild-type enzyme, overview
N122D
site-directed mutagenesis, inactive mutant
R81Q
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
V214I
site-directed mutagenesis, the mutant's activity is not affected
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Source 30Q column chromatography and Superdex 75 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Escherichia coli malate dehydrogenase gene cloned into expression vector pASK40 by PCR
expressed in Escherichia coli BL21 (DE3) cells
gene mdh, expression of the enzyme in strain BL21(DE3) as soluble protein
gene mdh, expression of wild-type and mutant enzymes in strains DH10B and W945T1-2
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme expression is downregulated by the aerobic respiration control protein (ArcA), particularly under anaerobic conditions
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Banaszak, L.J.; Bradshaw, R.A.
Malate dehydrogenases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
11
369-396
1975
Geobacillus stearothermophilus, Bacillus subtilis, Bos taurus, Drosophila virilis, Escherichia coli, Equus sp., Gallus sp., Ovis aries, Neurospora crassa, Phycomyces blakesleeanus, Rattus norvegicus, Salmo sp., Sus scrofa, Thunnus albacares
-
Manually annotated by BRENDA team
You, K.S.; Kaplan, N.O.
Purification and properties of malate dehydrogenase from Pseudomonas testosteroni
J. Bacteriol.
123
704-716
1975
Geobacillus stearothermophilus, Bacillus subtilis, Bos taurus, Delftia acidovorans, Comamonas testosteroni, Escherichia coli, Equus sp., Solanum tuberosum, Sus scrofa, Triticum aestivum
Manually annotated by BRENDA team
Mevarech, M.; Eisenberg, H.; Neumann, E.
Malate dehydrogenase isolated from extremely halophilic bacteria of the dead sea. 1. Purification and molecular characterization
Biochemistry
16
3781-3785
1977
Bacillus subtilis, Bos taurus, Comamonas testosteroni, Escherichia coli, Halobacterium salinarum, Sus scrofa, Thermus aquaticus
Manually annotated by BRENDA team
Tyagi, A.K.; Siddiqui, F.A.; Venkitasubramanian, T.A.
Studies on the purification and characterization of malate dehydrogenase from Mycobacterium phlei
Biochim. Biophys. Acta
485
255-267
1977
Bacillus subtilis, Bos taurus, Escherichia coli, Homo sapiens, Mycobacterium tuberculosis, Mycobacterium kansasii, Mycolicibacterium phlei, Mycobacterium scrofulaceum, Neurospora crassa, no activity in Mycobacterium fortuitum, no activity in Mycobacterium smegmatis, no activity in Mycobacterium smegmatis 607
Manually annotated by BRENDA team
Sprott, G.D.; McKellar, R.C.; Shaw, K.M.; Giroux, J.; Martin, W.G.
Properties of malate dehydrogenase isolated from Methanospirillum hungatii
Can. J. Microbiol.
25
192-200
1978
Saccharomyces cerevisiae, Escherichia coli, Methanothermobacter thermautotrophicus, Methanospirillum hungatei, Sus scrofa
Manually annotated by BRENDA team
Iijima, S.; Saiki, T.; Beppu, T.
Physicochemical and catalytic properties of thermostable malate dehydrogenase from an extreme thermophile Thermus flavus AT-62
Biochim. Biophys. Acta
613
1-9
1980
Geobacillus stearothermophilus, Bacillus subtilis, Comamonas testosteroni, Escherichia coli, Thermus thermophilus, Sus scrofa, Thermus thermophilus AT-62
Manually annotated by BRENDA team
Sundaram, T.K.; Wright, I.P.; Wilkinson, A.E.
Malate dehydrogenase from thermophilic and mesophilic bacteria. Molecular size, subunit structure, amino acid composition, immunochemical homology, and catalytic activity
Biochemistry
19
2017-2022
1980
Geobacillus stearothermophilus, [Bacillus] caldotenax, Bacillus subtilis, Bacillus sp. (in: Bacteria), Escherichia coli, Neurospora crassa, Vogesella indigofera, Sus scrofa, Laceyella sacchari, Thermobifida fusca, Thermus aquaticus, Thermus aquaticus YT-1, Thermobifida fusca NCIB 11185, Laceyella sacchari NCIB 10486
Manually annotated by BRENDA team
Storer, A.C.; Sprott, G.D.; Martin, W.G.
Kinetic and physical properties of the L-malate-NAD+ oxidoreductase from Methanospirillum hungatii and comparison with the enzyme from other sources
Biochem. J.
193
235-244
1981
Bacillus subtilis, Bos taurus, Saccharomyces cerevisiae, Comamonas testosteroni, Escherichia coli, Equus sp., Thermus thermophilus, Gallus sp., Halobacterium salinarum, Methanospirillum hungatei, Mycobacterium sp., Mycolicibacterium phlei, Neurospora crassa, Rattus norvegicus, Salmo sp., Sus scrofa, Thermus aquaticus, Thunnus albacares, Methanospirillum hungatei GPI
Manually annotated by BRENDA team
Smith, K.; Sundaram, T.K.; Kernick, M.; Wilkinson, A.E.
Purification of bacterial malate dehydrogenases by selective elution from a triazinyl dye affinity column
Biochim. Biophys. Acta
708
17-25
1982
[Bacillus] caldotenax, Bacillus subtilis, Bacillus sp. (in: Bacteria), Comamonas testosteroni, Escherichia coli, Thermus aquaticus, Thermus aquaticus B
-
Manually annotated by BRENDA team
Waters, J.K.; Karr, D.B.; Emerich, D.W.
Malate dehydrogenase from Rhizobium japonicum 3I1b-143 bacteroids and Glycine max root-nodule mitochondria
Biochemistry
24
6479-6486
1985
Geobacillus stearothermophilus, Bacillus subtilis, Bradyrhizobium japonicum, Chromobacterium violaceum, Escherichia coli, Euglena gracilis, Glycine max, Phaseolus vulgaris, Pisum sativum, Zea mays
-
Manually annotated by BRENDA team
Hartl, T.; Grossebueter, W.; Goerisch, H.; Stezowski, J.J.
Crystalline NAD/NADP-dependent malate dehydrogenase; the enzyme from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius
Biol. Chem. Hoppe-Seyler
368
259-267
1987
Escherichia coli, Thermus thermophilus, Methanothermobacter thermautotrophicus, Methanospirillum hungatei, Sulfolobus acidocaldarius, Sus scrofa, Laceyella sacchari, Thermoplasma acidophilum, Thermus aquaticus
Manually annotated by BRENDA team
Tayeh, M.A.; Madigan, M.T.
Malate dehydrogenase in phototrophic purple bacteria: Purification, molecular weight, and quaternary structure
J. Bacteriol.
169
4196-4202
1987
Geobacillus stearothermophilus, [Bacillus] caldolyticus, Priestia megaterium, Bacillus subtilis, Bacillus sp. (in: Bacteria), Bos taurus, Brevibacterium sp., Corynebacterium sp., Escherichia coli, Halobacterium salinarum, Methanospirillum hungatei, no activity in Chromatium sp., Rhodobacter capsulatus, Rhodocyclus purpureus, Rhodomicrobium vannielii, Rhodopseudomonas palustris, Rhodospirillum rubrum, Sulfolobus acidocaldarius, Sus scrofa, Laceyella sacchari, Thermoplasma acidophilum, Rhodobacter capsulatus B100, Rhodocyclus purpureus 6770, Rhodospirillum rubrum 1.1.1, Rhodobacter capsulatus 37b4, Rhodomicrobium vannielii EY33
Manually annotated by BRENDA team
Tayeh, M.A.; Madigan, M.T.
Malate dehydrogenases in phototrophic purple bacteria. Thermal stability, amino acid composition and immunological properties
Biochem. J.
252
595-600
1988
Geobacillus stearothermophilus, Priestia megaterium, Bacillus subtilis, Saccharomyces cerevisiae, Escherichia coli, Methanospirillum hungatei, Rhodobacter capsulatus, Rhodocyclus purpureus, Rhodomicrobium vannielii, Rhodospirillum rubrum, Sulfolobus acidocaldarius, Sus scrofa, Thermoplasma acidophilum, Rhodobacter capsulatus B100, Rhodocyclus purpureus 6770, Rhodospirillum rubrum 1.1.1, Rhodomicrobium vannielii EY33
Manually annotated by BRENDA team
Hall, M.D.; Banaszak, L.J.
Crystal structure of a ternary complex of Escherichia coli malate dehydrogenase citrate and NAD at 1.9 A resolution
J. Mol. Biol.
232
213-222
1993
Escherichia coli
Manually annotated by BRENDA team
Muslin, E.H.; Dong, L.; Stevens, F.J.; Donnelly, M.; Schiffer, M.; Anderson, L.E.
Engineering a domain-locking disulfide into a bacterial malate dehydrogenase produces a redox-sensitive enzyme
Biophys. J.
68
2218-2223
1995
Synechocystis sp., Pisum sativum, Spinacia oleracea, Sus scrofa, Zea mays, Escherichia coli (P61889), Escherichia coli, Synechocystis sp. 6803 CF
Manually annotated by BRENDA team
Van Kuijk, B.L.M.; Stams, A.J.M.
Purification and characterization of malate dehydrogenase from the syntrophic propionate-oxidizing bacterium strain MPOB
FEMS Microbiol. Lett.
144
141-144
1996
Geobacillus stearothermophilus, Bacillus subtilis, Syntrophobacter fumaroxidans, Chlorobaculum tepidum, Prosthecochloris vibrioformis, Citrullus lanatus, Escherichia coli, Thermus thermophilus, Heliomicrobium gestii, Methanothermus fervidus, Mus musculus, Phenylobacterium immobile, Planomonospora venezuelensis, Streptomyces atratus, Streptosporangium roseum, Syntrophobacter fumaroxidans MPOB
Manually annotated by BRENDA team
Musrati, R.A.; Kollarova, M.; Mernik, N.; Mikulasova, D.
Malate dehydrogenase: Distribution, function and properties
Gen. Physiol. Biophys.
17
193-210
1998
Saccharomyces cerevisiae, Citrullus lanatus, Escherichia coli, Eucalyptus globulus, Euglena gracilis, Thermus thermophilus, Haloarcula marismortui, Methanothermus fervidus, Mus musculus, Nitzschia alba, Rattus norvegicus, Kitasatospora aureofaciens, Sulfolobus acidocaldarius, Sus scrofa, Zea mays
Manually annotated by BRENDA team
Kim, S.Y.; Hwang, K.Y.; Kim, S.H.; Sung, H.C.; Han, Y.S.; Cho, Y.
Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum
J. Biol. Chem.
274
11761-11767
1999
Escherichia coli, Thermus thermophilus, Sus scrofa, Aquaspirillum arcticum (Q9ZF99), Aquaspirillum arcticum
Manually annotated by BRENDA team
Chapman, A.D.M.; Cortes, A.; Dafforn, T.R.; Clarke, A.R.; Brady, R.L.
Structural basis of substrate specificity in malate dehydrogenases: Crystal structure of a ternary complex of porcine cytoplasmic malate dehydrogenase, alpha-ketomalonate and tetrahydoNAD
J. Mol. Biol.
285
703-712
1999
Escherichia coli, Thermus thermophilus, Sus scrofa
Manually annotated by BRENDA team
Park, J.S.; Han, K.Y.; Song, J.A.; Ahn, K.Y.; Seo, H.S.; Lee, J.
Escherichia coli malate dehydrogenase, a novel solubility enhancer for heterologous proteins synthesized in Escherichia coli
Biotechnol. Lett.
29
1513-1518
2007
Escherichia coli (P61889), Escherichia coli
Manually annotated by BRENDA team
Yin, Y.; Kirsch, J.F.
Identification of functional paralog shift mutations: conversion of Escherichia coli malate dehydrogenase to a lactate dehydrogenase
Proc. Natl. Acad. Sci. USA
104
17353-17357
2007
Escherichia coli (P61889), Escherichia coli, Escherichia coli MG1655 (P61889)
Manually annotated by BRENDA team
Zaitseva, J.; Meneely, K.M.; Lamb, A.L.
Structure of Escherichia coli malate dehydrogenase at 1.45 A resolution
Acta Crystallogr. Sect. F
65
866-869
2009
Escherichia coli (P61889), Escherichia coli
Manually annotated by BRENDA team
Takahashi-Iniguez, T.; Aburto-Rodriguez, N.; Vilchis-Gonzalez, A.; Flores, M.
Function, kinetic properties, crystallization, and regulation of microbial malate dehydrogenase
J. Zhejiang Univ. Sci. B
17
247-261
2016
Aeropyrum pernix, Archaeoglobus fulgidus, Bacillus subtilis, uncultured bacterium, Corynebacterium glutamicum, Escherichia coli, Glaesserella parasuis, Haloarcula marismortui, Helicobacter pylori, Methanothermobacter thermautotrophicus, Methanocaldococcus jannaschii, Nitrosomonas europaea, Pseudomonas stutzeri, Kitasatospora aureofaciens, Streptomyces coelicolor, uncultured bacterium MPOB, Bacillus subtilis B1
-
Manually annotated by BRENDA team