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Information on EC 1.1.1.86 - ketol-acid reductoisomerase (NADP+) and Organism(s) Escherichia coli and UniProt Accession P05793

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IUBMB Comments
Also catalyses the reduction of 2-ethyl-2-hydroxy-3-oxobutanoate to 2,3-dihydroxy-3-methylpentanoate. The enzyme, found in many bacteria and archaea, is specific for NADPH (cf. EC 1.1.1.382, ketol-acid reductoisomerase (NAD+) and EC 1.1.1.383, ketol-acid reductoisomerase [NAD(P)+]).
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Escherichia coli
UNIPROT: P05793
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
reductoisomerase, ketol-acid reductoisomerase, acetohydroxy acid isomeroreductase, ilv5p, isomeroreductase, acetohydroxyacid isomeroreductase, ahair, acetohydroxy acid reductoisomerase, ilvc1, acetolactate reductoisomerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-hydroxy-3-keto acid reductoisomerase
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-
-
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acetohydroxy acid isomeroreductase
acetohydroxy acid reductoisomerase
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acetohydroxy-acid isomeroreductase
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acetohydroxy-acid reductoisomerase
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acetolactate reductoisomerase
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alpha-keto-beta-hydroxylacil reductoisomerase
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-
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alpha-keto-beta-hydroxylacyl reductoisomerase
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class II ketol-acid reductoisomerase
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dehydrogenase, dihydroxyisovalerate (isomerizing)
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dihydroxyisovalerate dehydrogenase (isomerizing)
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isomerase, ketol acid reducto-
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isomeroreductase
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reductoisomerase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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rearrangement
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SYSTEMATIC NAME
IUBMB Comments
(R)-2,3-dihydroxy-3-methylbutanoate:NADP+ oxidoreductase (isomerizing)
Also catalyses the reduction of 2-ethyl-2-hydroxy-3-oxobutanoate to 2,3-dihydroxy-3-methylpentanoate. The enzyme, found in many bacteria and archaea, is specific for NADPH (cf. EC 1.1.1.382, ketol-acid reductoisomerase (NAD+) and EC 1.1.1.383, ketol-acid reductoisomerase [NAD(P)+]).
CAS REGISTRY NUMBER
COMMENTARY hide
9075-02-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
show the reaction diagram
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-
-
-
r
(R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH
show the reaction diagram
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the enzyme is involved in biosynthesis of the branched chain amino acids valine and leucine, pathway overview
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-
?
2-acetolactate + NADH + H+
2,3-dihydroxy-3-methylbutanoate + NAD+ + H+
show the reaction diagram
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-
-
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
2-acetolactate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethyl-butanoate + NADP+
show the reaction diagram
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-
-
-
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methyl-butanoate + NADP+
show the reaction diagram
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-
-
-
?
2-ketobutyrate + NADPH + H+
?
show the reaction diagram
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r
2-ketoisovalerate + NADPH + H+
?
show the reaction diagram
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r
2-ketopantoate + NADPH + H+
?
show the reaction diagram
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-
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r
2-ketovalerate + NADPH + H+
?
show the reaction diagram
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-
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r
3-hydroxy-2-ketobutyrate + NADPH + H+
?
show the reaction diagram
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-
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r
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethyl-butanoate + NADP+
show the reaction diagram
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-
-
-
?
3-hydroxy-3-methyl-2-ketobutyrate + NADP+
?
show the reaction diagram
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-
-
-
r
3-hydroxy-3-methyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-methyl-butanoate + NADP+
show the reaction diagram
-
-
-
-
?
3-hydroxypyruvate + NADPH + H+
?
show the reaction diagram
acetolactate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
show the reaction diagram
NADP+ + 3-hydroxy-3-methyl-2-oxobutanoate
NADPH + acetolactate
show the reaction diagram
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-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
show the reaction diagram
pyruvate + NADPH + H+
?
show the reaction diagram
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-
r
additional information
?
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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
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
show the reaction diagram
-
-
-
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
binding of NADPH is enthalpy driven. NADPH binding may have an opposing effect to that of Mg2+ binding by inducing an increase in structural stability
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
the coordination geometry for Mg(1) is approximately octahedral, with three water ligands and three protein ligands, the carboxylate groups of D217, E389 and E393. Mg(2) is seven coordinate with six waters and a carboxylate oxygen from D217. A dissociation constant of about 500 microM applies to the interaction of Mg2+ with unliganded enzyme. In presence of NADPH the Kd increases to about 800 microM
Co2+
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the reaction requires a divalent metal ion
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-dihydroxy-3-methylbutyrate
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2-Methyllactate
3-aminopyridine-NADP+
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4,4'-(pentamethylenedioxy)dibenzamidne bis(2-hydroxyethanesulfonate)
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binding structure and inhibition mechanism, overview
Mn2+
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with acetolactate as substrate, Mn2+ behaves as a competitive inhibitor in presence of Mg2+
N-Hydroxy-N-isopropyloxamate
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very strong, nearly irreversible inhibition, inhibition also with N-alkyl substituted derivates, tightest binding in presence of Mg2+ and NADPH
additional information
-
computer-aided drug design, overview
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002
2-aceto-2-hydroxybutyrate
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pH 7.4, 25°C
0.014 - 2.028
2-acetolactate
0.3
2-hydroxy-2-ethyl-3-oxobutanoate
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pH 8.0 25°C
0.28
2-Hydroxy-2-methyl-3-oxobutanoate
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pH 8.0 25°C
4.56
2-Ketobutyrate
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pH 8.0, 37°C, wild-type enzyme
6.91
2-ketoisovalerate
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pH 8.0, 37°C, wild-type enzyme
0.17
2-ketopantoate
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pH 8.0, 37°C, wild-type enzyme
3.15
2-ketovalerate
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pH 8.0, 37°C, wild-type enzyme
0.21
3-hydroxy-2-ketobutyrate
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pH 8.0, 37°C, wild-type enzyme
0.29
3-hydroxy-3-ethyl-2-oxobutanoate
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pH 8.0 25°C
0.27
3-hydroxy-3-methyl-2-ketobutyrate
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pH 8.0, 37°C, wild-type enzyme
0.26
3-Hydroxy-3-methyl-2-oxobutanoate
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pH 8.0 25°C
0.334 - 15.3
3-hydroxypyruvate
0.019 - 0.207
NADH
0.0089 - 0.072
NADP+
0.00016 - 0.401
NADPH
1.54
pyruvate
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pH 8.0, 37°C, wild-type enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00417
2,3-Dihydroxy-3-methylbutanoate
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pH 7.4, 25°C
1.2 - 2.231
2-acetolactate
3.5
2-hydroxy-2-ethyl-3-oxobutanoate
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pH 8.0 25°C
2
2-Hydroxy-2-methyl-3-oxobutanoate
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pH 8.0 25°C
0.167
2-Ketobutyrate
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pH 8.0, 37°C
0.182
2-ketoisovalerate
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pH 8.0, 37°C
0.194
2-ketopantoate
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pH 8.0, 37°C
0.05
2-ketovalerate
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pH 8.0, 37°C
0.594
3-hydroxy-2-ketobutyrate
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pH 8.0, 37°C
3.8
3-hydroxy-3-ethyl-2-oxobutanoate
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pH 8.0 25°C
3.511
3-hydroxy-3-methyl-2-ketobutyrate
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pH 8.0, 37°C
3.1
3-Hydroxy-3-methyl-2-oxobutanoate
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pH 8.0 25°C
5.376 - 26
3-hydroxypyruvate
0.00183 - 0.0883
NADH
0.00015 - 0.000667
NADP+
0.0000933 - 0.212
NADPH
0.021
pyruvate
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pH 8.0, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.4
2-acetolactate
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at pH 8.0, temperature not specified in the publication
11.67
2-hydroxy-2-ethyl-3-oxobutanoate
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pH 8.0 25°C
7.14
2-Hydroxy-2-methyl-3-oxobutanoate
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pH 8.0 25°C
13.1
3-hydroxy-3-ethyl-2-oxobutanoate
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pH 8.0 25°C
11.92
3-Hydroxy-3-methyl-2-oxobutanoate
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pH 8.0 25°C
3.3
3-hydroxypyruvate
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at pH 8.0, temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012 - 0.0226
NADPH
additional information
additional information
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-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.9
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purified enzyme
additional information
-
the specific activity with pyruvate is 1% and with 2-ketovalerate, 2-ketopantoate and 2-ketobutyrate is 8% of that of 2-acetolactate, comparison of activities of wild-type and mutant enzymes
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
228000
sedimentation equilibrium analysis
230000
gel filtration
52428
4 * 52428, calculated
55000
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x * 55000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
4 * 52428, calculated
?
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x * 55000, SDS-PAGE
tetramer
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three-dimensional enzyme structure, subunit domain structures, surface contact and interlock, crystal structure analysis, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with Mg2+ and NADPH at 2.3 A resolution. The binding of Mg2+ increases structural disorder while the binding of NADPH increases the structural rigidity of the enzyme. The binding of Mg2+ and NADPH opens the interface between the N- and C-domains, thereby allowing access for the substrates to bind
purified recombinant His-tagged enzyme, 9 mg/ml protein in 20 mM sodium HEPES, pH 7.5, and NADPH in a ratio of 10 mol NADPH per mol of enzyme, hanging drop vapour diffusion method, equal volumes of 0.003 ml of protein and reservoir solution, the latter containing 1.6 M ammonium sulfate, and 0.1 M sodium bicine, pH 9.0, 17°C, 6 months, X-ray diffraction structure determination and analysis at 2.6 A resolution
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the enzyme is remarkably easy to crystallize
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D217E
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less than 4% reductoisomerase activity in comparison to wild-type enzyme
D217N
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less than 4% reductoisomerase activity in comparison to wild-type enzyme
E213D
-
75% reductoisomerase activity in comparison of wild-type enzyme
E213Q
-
less than 4% reductoisomerase activity in comparison of wild-type enzyme
E221D
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
E221Q
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
E389D
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
E389Q
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
E393D
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
E393Q
-
the mutant is insoluble, a soluble form is obtained only after denaturation
H132K
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less than 4% reductoisomerase activity in comparison of wild-type enzyme
H132Q
-
less than 4% reductoisomerase activity in comparison of wild-type enzyme
K155E
-
less than 4% reductoisomerase activity in comparison of wild-type enzyme
K155Q
-
less than 4% reductoisomerase activity in comparison of wild-type enzyme
K155R
-
less than 4% reductoisomerase activity in comparison of wild-type enzyme
K69L
-
Km-value for NADP+ in the reaction with 2,3-dihydroxy-3-methylbutanoate is 2.1fold higher than the Km-value of the wild-type enzyme, the turnover-number for the reaction with NADP+ and 2,3-dihydroxy-3-methylbutanoate is lower by a factor 163 compared to wild-type enzyme. Km-value for NADPH in the reaction with acetolactate is comparable to that of the wild-type emzyme, the turnover-number for the reaction with NADP+ and 2,3-dihydroxy-3-methylbutanoate is 1.8fold higher than that of the wild-type enzyme
K75Q
-
Km-value for NADP+ in the reaction with 2,3-dihydroxy-3-methylbutanoate is 2.7fold higher than the Km-value of the wild-type enzyme, the turnover-number for the reaction with NADP+ and 2,3-dihydroxy-3-methylbutanoate is lower by a factor 77.5 compared to wild-type enzyme. Km-value for NADPH in the reaction with acetolactate is lower by a factor 2.9 compared to the Km-value of the wild-type enzyme, the turnover-number for the reaction with NADP+ and 2,3-dihydroxy-3-methylbutanoate is lower by a factor 12.9 compared to wild-type enzyme
R68D/K69L/K75V/R76D
-
turnover-number for reaction with NADH and acetolactate is 48fold higher compared to wild-type enzyme, turnover-number for reaction with NADPH and acetolactate is lower by factor 3.7 compared to wild-type enzyme, Km-value for NADH in the reaction with NADH and acetolactate is lower by a factor 10.8 compared to wild-type enzyme, Km-value for NADH in the reaction with NADPH and acetolactate is 30fold higher compared to wild-type enzyme
R68Q
-
Km-value for NADP+ in the reaction with 2,3-dihydroxy-3-methylbutanoate is 6.9fold higher than the Km-value of the wild-type enzyme, the turnover-number for the reaction with NADP+ and 2,3-dihydroxy-3-methylbutanoate is lower by a factor 345 compared to wild-type enzyme. Km-value for NADPH in the reaction with acetolactate is 3.4fold higher thahn that of the wild-type enzyme, the turnover-number for the reaction with NADP+ and 2,3-dihydroxy-3-methylbutanoate is lower by a factor 18 compared to wild-type enzyme
R76D
-
turnover-number for reaction with NADH and acetolactate is 48fold higher compared to wild-type enzyme, turnover-number for reaction with NADPH and acetolactate is lower by factor 4 compared to wild-type enzyme, Km-value for NADH in the reaction with NADH and acetolactate is lower by a factor 2.5 compared to wild-type enzyme, Km-value for NADPH in the reaction with NADPH and acetolactate is 55fold higher compared to wild-type enzyme
R76Q
-
Km-value for NADP+ in the reaction with 2,3-dihydroxy-3-methylbutanoate is 17.1fold higher than the Km-value of the wild-type enzyme, the turnover-number for the reaction with NADP+ and 2,3-dihydroxy-3-methylbutanoate is lower by a factor 258 compared to wild-type enzyme. Km-value for NADPH in the reaction with acetolactate is 5fold higher than that of the wild-type enzyme, the turnover-number for the reaction with NADP+ and 2,3-dihydroxy-3-methylbutanoate is lower by a factor 19.5 compared to wild-type enzyme
R76Q/R68A
-
turnover-number for reaction with NADH and acetolactate is 20fold higher compared to wild-type enzyme, turnover-number for reaction with NADPH and acetolactate is lower by factor 28 compared to wild-type enzyme, Km-value for NADH in the reaction with NADH and acetolactate is comparable to that of wild-type enzyme, Km-value for NADPH in the reaction with NADPH and acetolactate is 22fold higher compared to wild-type enzyme
S414A
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
S414T
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
-
rapid loss of activity above pH 10 with 2-acetolactate as substrate
639178
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
of wild-type and mutants
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recombinant His6-tagged enzyme
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wild-type and mutant enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression as His6-tagged enzyme
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chunduru, S.K.; Mrachko, G.T.; Calvo, K.C.
Mechanism of ketol acid reductoisomerase--steady-state analysis and metal ion requirement
Biochemistry
28
486-493
1989
Escherichia coli
Manually annotated by BRENDA team
Aulabaugh, A.; Schloss, J.V.
Oxalyl hydroxamates as reaction-intermediate analogues for ketol-acid reductoisomerase
Biochemistry
29
2824-2830
1990
Escherichia coli
Manually annotated by BRENDA team
Mrachko, G.T.; Chunduru, S.K.; Calvo, K.C.
The pH dependence of the kinetic parameters of ketol acid reductoisomerase indicates a proton shuttle mechanism for alkyl migration
Arch. Biochem. Biophys.
294
446-453
1992
Escherichia coli
Manually annotated by BRENDA team
Rane, M.J.; Calvo, K.C.
Reversal of the nucleotide specificity of ketol acid reductoisomerase by site-directed mutagenesis identifies the NADPH binding site
Arch. Biochem. Biophys.
338
83-89
1997
Escherichia coli
Manually annotated by BRENDA team
Dumas, R.; Biou, V.; Halgand, F.; Douce, R.; Duggleby, R.G.
Enzymology, structure, and dynamics of acetohydroxy acid isomeroreductase
Acc. Chem. Res.
34
399-408
2001
Escherichia coli, Triticum aestivum, Spinacia oleracea (Q01292)
Manually annotated by BRENDA team
McCourt, J.A.; Tyagi, R.; Guddat, L.W.; Biou, V.; Duggleby, R.G.
Facile crystallization of Escherichia coli ketol-acid reductoisomerase
Acta Crystallogr. Sect. D
60
1432-1434
2004
Escherichia coli
Manually annotated by BRENDA team
Tyagi, R.; Lee, Y.T.; Guddat, L.W.; Duggleby, R.G.
Probing the mechanism of the bifunctional enzyme ketol-acid reductoisomerase by site-directed mutagenesis of the active site
FEBS J.
272
593-602
2005
Escherichia coli
Manually annotated by BRENDA team
Tyagi, R.; Duquerroy, S.; Navaza, J.; Guddat, L.W.; Duggleby, R.G.
The crystal structure of a bacterial class II ketol-acid reductoisomerase: domain conservation and evolution
Protein Sci.
14
3089-3100
2005
Escherichia coli
Manually annotated by BRENDA team
Wang, B.; Li, Y.; Wang, J.; Ma, Y.; Li, Z.
Molecular design, synthesis and biological activities of amidines as new ketol-acid reductoisomerase inhibitors
Chin. Chem. Lett.
19
651-654
2008
Escherichia coli, Oryza sativa, Spinacia oleracea
-
Manually annotated by BRENDA team
Wong, S.H.; Lonhienne, T.G.; Winzor, D.J.; Schenk, G.; Guddat, L.W.
Bacterial and plant ketol-acid reductoisomerases have different mechanisms of induced fit during the catalytic cycle
J. Mol. Biol.
424
168-179
2012
Escherichia coli (P05793), Escherichia coli
Manually annotated by BRENDA team
Tadrowski, S.; Pedroso, M.M.; Sieber, V.; Larrabee, J.A.; Guddat, L.W.; Schenk, G.
Metal ions play an essential catalytic role in the mechanism of ketol-acid reductoisomerase
Chemistry
22
7427-7436
2016
Escherichia coli, Oryza sativa
Manually annotated by BRENDA team
Verdel-Aranda, K.; Lopez-Cortina, S.T.; Hodgson, D.A.; Barona-Gomez, F.
Molecular annotation of ketol-acid reductoisomerases from Streptomyces reveals a novel amino acid biosynthesis interlock mediated by enzyme promiscuity
Microb. Biotechnol.
8
239-252
2015
Corynebacterium glutamicum, Escherichia coli, Streptomyces ambofaciens (A0A0K2AZ61), Streptomyces ambofaciens ATCC 23877 (A0A0K2AZ61), Streptomyces avermitilis (Q59818), Streptomyces avermitilis DSM 46492 (Q59818), Streptomyces coelicolor (Q9FBT8), Streptomyces coelicolor (Q9Z565), Streptomyces coelicolor, Streptomyces coelicolor ATCC BAA-471 (Q9Z565), Streptomyces coelicolor BAA-471 (Q9FBT8), Streptomyces griseus, Streptomyces lividans (D6EC76), Streptomyces lividans (D6ERQ9), Streptomyces lividans, Streptomyces lividans TK24 (D6EC76), Streptomyces lividans TK24 (D6ERQ9), Streptomyces pristinaespiralis, Streptomyces viridifaciens
Manually annotated by BRENDA team