ilvC

Functionⁱ

Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. Also able to use 2-ketopantoate, 2-ketoisovalerate, 2-ketovalerate, 2-ketobutyrate, 3-hydroxypyruvate, 3-hydroxy-2-ketobutyrate and pyruvate (PubMed:15654896).4 Publications

Catalytic activityⁱ

(2R)-2,3-dihydroxy-3-methylbutanoate + NADP⁺ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH.UniRule annotation4 Publications

(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP⁺ = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH.UniRule annotation

Cofactorⁱ

Mg²⁺UniRule annotation3 PublicationsNote: Binds 2 magnesium ions per subunit.UniRule annotation2 Publications

Activity regulationⁱ

Inhibited by N-hydroxy-N-isopropyloxamate (IpOHA).1 Publication

Kineticsⁱ

Kcat is 7.2 min(-1) for reductoisomerase activity with NADPH as substrate (PubMed:9015391). Kcat is 3.1 min(-1) for reductoisomerase activity with NADPH as substrate (PubMed:9015391). Kcat is 0.11 min(-1) for reductoisomerase activity with NADH as substrate (PubMed:9015391). Kcat is 5.376 sec(-1) for reductoisomerase activity with 3-hydroxypyruvate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896). Kcat is 3.6 sec(-1) for reductoisomerase activity with NADPH as substrate (PubMed:21515217). Kcat is 3.511 sec(-1) for reductoisomerase activity with 3-hydroxy-3-methyl-2-ketobutyrate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896). Kcat is 2.231 sec(-1) for reductoisomerase activity with 2-acetolactate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896). Kcat is 0.594 sec(-1) for reductoisomerase activity with 3-hydroxy-2-ketobutyrate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896). Kcat is 0.3 sec(-1) for reductoisomerase activity with NADH as substrate (PubMed:21515217). Kcat is 0.194 sec(-1) for reductoisomerase activity with 2-ketopantoate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896). Kcat is 0.182 sec(-1) for reductoisomerase activity with 2-ketoisovalerate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896). Kcat is 0.167 sec(-1) for reductoisomerase activity with 2-ketobutyrate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896). Kcat is 0.05 sec(-1) for reductoisomerase activity with 2-ketovalerate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896). Kcat is 0.021 sec(-1) for reductoisomerase activity with pyruvate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896).3 Publications

V_max=
5.421 µmol/min/mg enzyme with 3-hydroxypyruvate as substrate (at pH 8 and 37 degrees Celsius)
1 Publication
Manual assertion based on experiment inⁱ
- Ref.10
  "Probing the mechanism of the bifunctional enzyme ketol-acid reductoisomerase by site-directed mutagenesis of the active site."
  Tyagi R., Lee Y.T., Guddat L.W., Duggleby R.G.
  FEBS J. 272:593-602(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, MUTAGENESIS OF HIS-132; LYS-155; GLU-213; ASP-217; GLU-221; GLU-389; GLU-393 AND SER-414, SUBSTRATE SPECIFICITY.
V_max=
3.541 µmol/min/mg enzyme with 3-hydroxy-3-methyl-2-ketobutyrate as substrate (at pH 8 and 37 degrees Celsius)
1 Publication
Manual assertion based on experiment inⁱ
- Ref.10
  "Probing the mechanism of the bifunctional enzyme ketol-acid reductoisomerase by site-directed mutagenesis of the active site."
  Tyagi R., Lee Y.T., Guddat L.W., Duggleby R.G.
  FEBS J. 272:593-602(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, MUTAGENESIS OF HIS-132; LYS-155; GLU-213; ASP-217; GLU-221; GLU-389; GLU-393 AND SER-414, SUBSTRATE SPECIFICITY.
V_max=
2.25 µmol/min/mg enzyme with 2-acetolactate as substrate (at pH 8 and 37 degrees Celsius)
1 Publication
Manual assertion based on experiment inⁱ
- Ref.10
  "Probing the mechanism of the bifunctional enzyme ketol-acid reductoisomerase by site-directed mutagenesis of the active site."
  Tyagi R., Lee Y.T., Guddat L.W., Duggleby R.G.
  FEBS J. 272:593-602(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, MUTAGENESIS OF HIS-132; LYS-155; GLU-213; ASP-217; GLU-221; GLU-389; GLU-393 AND SER-414, SUBSTRATE SPECIFICITY.
V_max=
0.599 µmol/min/mg enzyme with 3-hydroxy-2-ketobutyrate as substrate (at pH 8 and 37 degrees Celsius)
1 Publication
Manual assertion based on experiment inⁱ
- Ref.10
  "Probing the mechanism of the bifunctional enzyme ketol-acid reductoisomerase by site-directed mutagenesis of the active site."
  Tyagi R., Lee Y.T., Guddat L.W., Duggleby R.G.
  FEBS J. 272:593-602(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, MUTAGENESIS OF HIS-132; LYS-155; GLU-213; ASP-217; GLU-221; GLU-389; GLU-393 AND SER-414, SUBSTRATE SPECIFICITY.
V_max=
0.196 µmol/min/mg enzyme with 2-ketopantoate as substrate (at pH 8 and 37 degrees Celsius)
1 Publication
Manual assertion based on experiment inⁱ
- Ref.10
  "Probing the mechanism of the bifunctional enzyme ketol-acid reductoisomerase by site-directed mutagenesis of the active site."
  Tyagi R., Lee Y.T., Guddat L.W., Duggleby R.G.
  FEBS J. 272:593-602(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, MUTAGENESIS OF HIS-132; LYS-155; GLU-213; ASP-217; GLU-221; GLU-389; GLU-393 AND SER-414, SUBSTRATE SPECIFICITY.
V_max=
0.184 µmol/min/mg enzyme with 2-ketoisovalerate as substrate (at pH 8 and 37 degrees Celsius)
1 Publication
Manual assertion based on experiment inⁱ
- Ref.10
  "Probing the mechanism of the bifunctional enzyme ketol-acid reductoisomerase by site-directed mutagenesis of the active site."
  Tyagi R., Lee Y.T., Guddat L.W., Duggleby R.G.
  FEBS J. 272:593-602(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, MUTAGENESIS OF HIS-132; LYS-155; GLU-213; ASP-217; GLU-221; GLU-389; GLU-393 AND SER-414, SUBSTRATE SPECIFICITY.
V_max=
0.168 µmol/min/mg enzyme with 2-ketobutyrate as substrate (at pH 8 and 37 degrees Celsius)
1 Publication
Manual assertion based on experiment inⁱ
- Ref.10
  "Probing the mechanism of the bifunctional enzyme ketol-acid reductoisomerase by site-directed mutagenesis of the active site."
  Tyagi R., Lee Y.T., Guddat L.W., Duggleby R.G.
  FEBS J. 272:593-602(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, MUTAGENESIS OF HIS-132; LYS-155; GLU-213; ASP-217; GLU-221; GLU-389; GLU-393 AND SER-414, SUBSTRATE SPECIFICITY.
V_max=
0.05 µmol/min/mg enzyme with 2-ketovalerate as substrate (at pH 8 and 37 degrees Celsius)
1 Publication
Manual assertion based on experiment inⁱ
- Ref.10
  "Probing the mechanism of the bifunctional enzyme ketol-acid reductoisomerase by site-directed mutagenesis of the active site."
  Tyagi R., Lee Y.T., Guddat L.W., Duggleby R.G.
  FEBS J. 272:593-602(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, MUTAGENESIS OF HIS-132; LYS-155; GLU-213; ASP-217; GLU-221; GLU-389; GLU-393 AND SER-414, SUBSTRATE SPECIFICITY.
V_max=
0.021 µmol/min/mg enzyme with pyruvate as substrate (at pH 8 and 37 degrees Celsius)
1 Publication
Manual assertion based on experiment inⁱ
- Ref.10
  "Probing the mechanism of the bifunctional enzyme ketol-acid reductoisomerase by site-directed mutagenesis of the active site."
  Tyagi R., Lee Y.T., Guddat L.W., Duggleby R.G.
  FEBS J. 272:593-602(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, MUTAGENESIS OF HIS-132; LYS-155; GLU-213; ASP-217; GLU-221; GLU-389; GLU-393 AND SER-414, SUBSTRATE SPECIFICITY.

Pathwayⁱ: L-isoleucine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.UniRule annotation1 Publication
Proteins known to be involved in the 4 steps of the subpathway in this organism are:

This subpathway is part of the pathway L-isoleucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-isoleucine from 2-oxobutanoate, the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.

Pathwayⁱ: L-valine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-valine from pyruvate.UniRule annotation1 Publication
Proteins known to be involved in the 4 steps of the subpathway in this organism are:

This subpathway is part of the pathway L-valine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-valine from pyruvate, the pathway L-valine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	68	NADPUniRule annotation1 Publication	1
Binding siteⁱ	76	NADPUniRule annotation1 Publication1 Publication	1
Binding siteⁱ	78	NADPUniRule annotation1 Publication	1
Active siteⁱ	132	UniRule annotation	1
Binding siteⁱ	158	NADP; via amide nitrogenUniRule annotation	1
Metal bindingⁱ	217	Magnesium 1UniRule annotation1 Publication	1
Metal bindingⁱ	217	Magnesium 2UniRule annotation1 Publication	1
Metal bindingⁱ	221	Magnesium 1UniRule annotation	1
Metal bindingⁱ	389	Magnesium 2UniRule annotation1 Publication	1
Metal bindingⁱ	393	Magnesium 2UniRule annotation1 Publication	1
Binding siteⁱ	414	SubstrateUniRule annotation	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	45 – 48	NADPUniRule annotation1 Publication		4
Nucleotide bindingⁱ	108 – 110	NADPUniRule annotation1 Publication		3

GO - Molecular functionⁱ

identical protein binding
Source: EcoCyc
Inferred from direct assayⁱ
- 23036858
ketol-acid reductoisomerase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 21515217
magnesium ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 23036858
NADP binding
Source: UniProtKB
Inferred from direct assayⁱ
- 23036858

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

isoleucine biosynthetic process
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 14832239
protein homotetramerization
Source: EcoCyc
Inferred from direct assayⁱ
- 23036858
valine biosynthetic process
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 14832239

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Biological process	Amino-acid biosynthesis, Branched-chain amino acid biosynthesis
Ligand	Magnesium, Metal-binding, NADP

Enzyme and pathway databases

BioCycⁱ	EcoCyc:KETOLREDUCTOISOM-MONOMER MetaCyc:KETOLREDUCTOISOM-MONOMER
BRENDAⁱ	1.1.1.86 2026
UniPathwayⁱ	UPA00047;UER00056 UPA00049;UER00060

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Ketol-acid reductoisomerase (NADP(+))1 PublicationUniRule annotation (EC:1.1.1.86UniRule annotation4 Publications) Short name: KARI1 PublicationUniRule annotation Alternative name(s): Acetohydroxy-acid isomeroreductase1 PublicationUniRule annotation Short name: AHIR1 PublicationUniRule annotation Alpha-keto-beta-hydroxylacyl reductoisomeraseUniRule annotation Ketol-acid reductoisomerase type 21 PublicationUniRule annotation Ketol-acid reductoisomerase type II1 PublicationUniRule annotation
Gene namesⁱ	Name:ilvCUniRule annotation Ordered Locus Names:b3774, JW3747
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG10495 ilvC

EcoGeneⁱ

EG10495 ilvC

Subcellular locationⁱ

Cytoplasm
1 Publication
Manual assertion inferred by curator fromⁱ
- Ref.7
  "Mechanism of ketol acid reductoisomerase--steady-state analysis and metal ion requirement."
  Chunduru S.K., Mrachko G.T., Calvo K.C.
  Biochemistry 28:486-493(1989) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBCELLULAR LOCATION, PATHWAY.

GO - Cellular componentⁱ

cytosol
Source: EcoCyc
Inferred from direct assayⁱ
- 18304323
- 2653423

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cytoplasm

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	68	R → D: Inversion of cofactor specificity from NADPH to NADH; when associated with L-69, V-75 and D-76. 1 Publication	1
Mutagenesisⁱ	68	R → Q: 18-fold decrease of the catalytic efficiency and 3-fold decrease of the affinity for NADPH. 1 Publication	1
Mutagenesisⁱ	69	K → L: Does not significantly alter the affinity for NADPH. Slight increase of the catalytic efficiency. Inversion of cofactor specificity from NADPH to NADH; when associated with D-68, V-75 and D-76. 1 Publication	1
Mutagenesisⁱ	71	A → S: 7- and 2.5-fold increase of the reductoisomerase activity with NADH and NADPH, respectively. 1 Publication	1
Mutagenesisⁱ	75	K → Q: 13-fold decrease of the catalytic efficiency and 3-fold increase of the affinity for NADPH. 1 Publication	1
Mutagenesisⁱ	75	K → V: Inversion of cofactor specificity from NADPH to NADH; when associated with D-68, L-69 and D-76. 1 Publication	1
Mutagenesisⁱ	76	R → D: 3-fold increase of the reductoisomerase activity with NADH and slight decrease of the reductoisomerase activity with NADPH. 1 Publication	1
Mutagenesisⁱ	76	R → D: Strong increase of catalytic efficiency and 2.5-fold increase of the affinity for NADH. 4-fold decrease of the catalytic efficiency and strong decrease of the affinity for NADPH. Inversion of cofactor specificity from NADPH to NADH; when associated with D-68, L-69 and V-75. 1 Publication	1
Mutagenesisⁱ	76	R → Q: 20-fold decrease of the catalytic efficiency and 5-fold decrease of the affinity for NADPH. 1 Publication	1
Mutagenesisⁱ	78	S → D: 12-fold increase of the reductoisomerase activity with NADH and slight decrease of the reductoisomerase activity with NADPH. 1 Publication	1
Mutagenesisⁱ	110	Q → V or A: 12- and 2-fold increase of the reductoisomerase activity with NADH and NADPH, respectively. 1 Publication	1
Mutagenesisⁱ	132	H → K: Loss of reductoisomerase activity. 1 Publication	1
Mutagenesisⁱ	132	H → Q: Loss of reductoisomerase activity. The reductase activity with 3-hydroxypyruvate and HMKB is nearly normal, and the isomerase activity decreases 24-fold. 1 Publication	1
Mutagenesisⁱ	155	K → E or Q: Loss of reductoisomerase activity. 1 Publication	1
Mutagenesisⁱ	155	K → R: Loss of reductoisomerase activity. The reductase activity with 3-hydroxypyruvate and HMKB is nearly normal, and the isomerase activity decreases 40-fold. 1 Publication	1
Mutagenesisⁱ	213	E → D: Loss of reductoisomerase activity. 1.5-fold decrease of the reductase activity with 3-hydroxypyruvate and the isomerase activity decreases 48-fold. 1 Publication	1
Mutagenesisⁱ	217	D → E or N: Loss of reductoisomerase activity. 1 Publication	1
Mutagenesisⁱ	221	E → D or Q: Loss of reductoisomerase activity. 1 Publication	1
Mutagenesisⁱ	389	E → D: Loss of reductoisomerase activity. 1.5-fold decrease of the reductase activity with 3-hydroxypyruvate and the isomerase activity decreases 4-fold. 1 Publication	1
Mutagenesisⁱ	389	E → Q: Loss of reductoisomerase activity. 1 Publication	1
Mutagenesisⁱ	393	E → D: Loss of reductoisomerase activity. The reductase activity with HMKB is nearly normal. 1 Publication	1
Mutagenesisⁱ	414	S → A: Loss of reductoisomerase activity. The isomerase activity decreases 15-fold. 1 Publication	1
Mutagenesisⁱ	414	S → T: Loss of reductoisomerase activity. The isomerase activity decreases 24-fold. 1 Publication	1

Chemistry databases

ChEMBLⁱ	CHEMBL2366462

ChEMBLⁱ

CHEMBL2366462

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed1 Publication
ChainⁱPRO_0000151309	2 – 491	Ketol-acid reductoisomerase (NADP(+))Add BLAST		490

Proteomic databases

EPDⁱ	P05793
PaxDbⁱ	P05793
PRIDEⁱ	P05793

2D gel databases

SWISS-2DPAGEⁱ	P05793

SWISS-2DPAGEⁱ

P05793

Expressionⁱ

Inductionⁱ

In the presence of acetohydroxybutyrate and acetolactate and by the activator IlvY.2 Publications

Interactionⁱ

Subunit structureⁱ

Homotetramer.2 Publications

GO - Molecular functionⁱ

identical protein binding
Source: EcoCyc
Inferred from direct assayⁱ
- 23036858

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	4263331, 21 interactors
IntActⁱ	P05793, 4 interactors
STRINGⁱ	316385.ECDH10B_3963

Chemistry databases

BindingDBⁱ

P05793

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	5 – 7	Combined sources	3
Helixⁱ	10 – 17	Combined sources	8
Beta strandⁱ	20 – 22	Combined sources	3
Helixⁱ	25 – 28	Combined sources	4
Turnⁱ	29 – 32	Combined sources	4
Helixⁱ	33 – 35	Combined sources	3
Beta strandⁱ	38 – 44	Combined sources	7
Helixⁱ	47 – 58	Combined sources	12
Beta strandⁱ	62 – 67	Combined sources	6
Helixⁱ	69 – 73	Combined sources	5
Helixⁱ	77 – 84	Combined sources	8
Beta strandⁱ	88 – 91	Combined sources	4
Helixⁱ	92 – 95	Combined sources	4
Helixⁱ	96 – 98	Combined sources	3
Beta strandⁱ	100 – 104	Combined sources	5
Helixⁱ	108 – 110	Combined sources	3
Helixⁱ	111 – 118	Combined sources	8
Helixⁱ	119 – 121	Combined sources	3
Beta strandⁱ	127 – 132	Combined sources	6
Helixⁱ	134 – 137	Combined sources	4
Beta strandⁱ	147 – 156	Combined sources	10
Helixⁱ	158 – 166	Combined sources	9
Beta strandⁱ	173 – 177	Combined sources	5
Helixⁱ	179 – 181	Combined sources	3
Helixⁱ	187 – 197	Combined sources	11
Helixⁱ	200 – 202	Combined sources	3
Beta strandⁱ	205 – 207	Combined sources	3
Helixⁱ	210 – 222	Combined sources	13
Turnⁱ	223 – 226	Combined sources	4
Helixⁱ	227 – 242	Combined sources	16
Helixⁱ	247 – 275	Combined sources	29
Helixⁱ	279 – 309	Combined sources	31
Helixⁱ	311 – 321	Combined sources	11
Turnⁱ	322 – 324	Combined sources	3
Helixⁱ	325 – 336	Combined sources	12
Helixⁱ	338 – 341	Combined sources	4
Helixⁱ	351 – 356	Combined sources	6
Helixⁱ	359 – 377	Combined sources	19
Turnⁱ	378 – 380	Combined sources	3
Helixⁱ	383 – 388	Combined sources	6
Helixⁱ	391 – 393	Combined sources	3
Helixⁱ	394 – 412	Combined sources	19
Helixⁱ	415 – 431	Combined sources	17
Helixⁱ	433 – 437	Combined sources	5
Beta strandⁱ	443 – 446	Combined sources	4
Helixⁱ	455 – 466	Combined sources	12
Helixⁱ	469 – 487	Combined sources	19

Show more details

3D structure databases

ProteinModelPortalⁱ	P05793
SMRⁱ	P05793
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P05793

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	15 – 208	KARI N-terminal RossmannPROSITE-ProRule annotation1 PublicationAdd BLAST	194
Domainⁱ	209 – 344	KARI C-terminal knotted 1PROSITE-ProRule annotation1 PublicationAdd BLAST	136
Domainⁱ	345 – 484	KARI C-terminal knotted 2PROSITE-ProRule annotation1 PublicationAdd BLAST	140

Sequence similaritiesⁱ

Belongs to the ketol-acid reductoisomerase family.UniRule annotation

Keywords - Domainⁱ

Repeat

Phylogenomic databases

eggNOGⁱ	ENOG4105C6M Bacteria COG0059 LUCA
HOGENOMⁱ	HOG000286135
InParanoidⁱ	P05793
KEGG Orthology (KO) More...KOⁱ	K00053
OMAⁱ	KLFEMNR
PhylomeDBⁱ	P05793

Family and domain databases

Gene3Dⁱ	1.10.1040.10, 1 hit
HAMAPⁱ	MF_00435 IlvC, 1 hit
InterProⁱ	View protein in InterPro IPR008927 6-PGluconate_DH-like_C_sf IPR013328 6PGD_dom2 IPR013023 KARI IPR000506 KARI_C IPR013116 KARI_N IPR036291 NAD(P)-bd_dom_sf
PANTHERⁱ	PTHR21371 PTHR21371, 2 hits
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01450 IlvC, 2 hits PF07991 IlvN, 1 hit
SUPFAMⁱ	SSF48179 SSF48179, 2 hits SSF51735 SSF51735, 1 hit
TIGRFAMsⁱ	TIGR00465 ilvC, 1 hit
PROSITEⁱ	View protein in PROSITE PS51851 KARI_C, 2 hits PS51850 KARI_N, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P05793-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MANYFNTLNL RQQLAQLGKC RFMGRDEFAD GASYLQGKKV VIVGCGAQGL 
        60         70         80         90        100
NQGLNMRDSG LDISYALRKE AIAEKRASWR KATENGFKVG TYEELIPQAD 
       110        120        130        140        150
LVINLTPDKQ HSDVVRTVQP LMKDGAALGY SHGFNIVEVG EQIRKDITVV 
       160        170        180        190        200
MVAPKCPGTE VREEYKRGFG VPTLIAVHPE NDPKGEGMAI AKAWAAATGG 
       210        220        230        240        250
HRAGVLESSF VAEVKSDLMG EQTILCGMLQ AGSLLCFDKL VEEGTDPAYA 
       260        270        280        290        300
EKLIQFGWET ITEALKQGGI TLMMDRLSNP AKLRAYALSE QLKEIMAPLF 
       310        320        330        340        350
QKHMDDIISG EFSSGMMADW ANDDKKLLTW REETGKTAFE TAPQYEGKIG 
       360        370        380        390        400
EQEYFDKGVL MIAMVKAGVE LAFETMVDSG IIEESAYYES LHELPLIANT 
       410        420        430        440        450
IARKRLYEMN VVISDTAEYG NYLFSYACVP LLKPFMAELQ PGDLGKAIPE 
       460        470        480        490 
GAVDNGQLRD VNEAIRSHAI EQVGKKLRGY MTDMKRIAVA G

Length:491

Mass (Da):54,069

Last modified:January 23, 2007 - v4

Checksum:ⁱ9CA34BA61C9AEBBA

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	251	E → K in AAA24029 (PubMed:3003115).Curated		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M11689 Genomic DNA Translation: AAA24029.1 M87049 Genomic DNA Translation: AAA67577.1 U00096 Genomic DNA Translation: AAC76779.1 AP009048 Genomic DNA Translation: BAE77523.1
PIRⁱ	A65181 ISECKR
NCBI Reference Sequences More...RefSeqⁱ	NP_418222.1, NC_000913.3 WP_000024939.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC76779; AAC76779; b3774 BAE77523; BAE77523; BAE77523
GeneIDⁱ	948286
KEGGⁱ	ecj:JW3747 eco:b3774
PATRICⁱ	fig\|511145.12.peg.3891

Protein	Similar proteins		Species	Score	Length	Source
P05793	Ketol-acid reductoisomerase (NADP(+))		ECOBW		491	UniRef100_C4ZZ44
Ketol-acid reductoisomerase (NADP(+))		ECODH		491
Ketol-acid reductoisomerase (NADP(+))		ECOHS		491
Ketol-acid reductoisomerase (NADP(+))		ECOLC		491
Ketol-acid reductoisomerase (NADP(+))		ECOLX		536
+33

Protein	Similar proteins		Species	Score	Length	Source
P05793	Ketol-acid reductoisomerase (NADP(+))		SALTY		491	UniRef90_P05989
Ketol-acid reductoisomerase (NADP(+))		ERWT9		492
Ketol-acid reductoisomerase (NADP(+))		YERPA		492
Ketol-acid reductoisomerase (NADP(+))		YERPE		492
Ketol-acid reductoisomerase (NADP(+))		YERPG		492
+1625

Protein	Similar proteins		Species	Score	Length	Source
P05793	Ketol-acid reductoisomerase (NADP(+))		SALTY		491	UniRef50_P05989
Ketol-acid reductoisomerase (NADP(+))		ERWT9		492
Ketol-acid reductoisomerase (NADP(+))		YERP3		492
Ketol-acid reductoisomerase (NADP(+))		YERPB		492
Ketol-acid reductoisomerase (NADP(+))		YERPS		492
+4524

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M11689 Genomic DNA Translation: AAA24029.1 M87049 Genomic DNA Translation: AAA67577.1 U00096 Genomic DNA Translation: AAC76779.1 AP009048 Genomic DNA Translation: BAE77523.1
PIRⁱ	A65181 ISECKR
RefSeqⁱ	NP_418222.1, NC_000913.3 WP_000024939.1, NZ_LN832404.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1YRL	X-ray	2.60	A/B/C/D	1-491	[»]
	3ULK	X-ray	2.30	A/B	1-491	[»]
ProteinModelPortalⁱ	P05793
SMRⁱ	P05793
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4263331, 21 interactors
IntActⁱ	P05793, 4 interactors
STRINGⁱ	316385.ECDH10B_3963

Chemistry databases

BindingDBⁱ	P05793
ChEMBLⁱ	CHEMBL2366462

2D gel databases

SWISS-2DPAGEⁱ	P05793

SWISS-2DPAGEⁱ

P05793

Proteomic databases

EPDⁱ	P05793
PaxDbⁱ	P05793
PRIDEⁱ	P05793

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC76779; AAC76779; b3774 BAE77523; BAE77523; BAE77523
GeneIDⁱ	948286
KEGGⁱ	ecj:JW3747 eco:b3774
PATRICⁱ	fig\|511145.12.peg.3891

Organism-specific databases

EchoBASEⁱ	EB0490
EcoGeneⁱ	EG10495 ilvC

Phylogenomic databases

eggNOGⁱ	ENOG4105C6M Bacteria COG0059 LUCA
HOGENOMⁱ	HOG000286135
InParanoidⁱ	P05793
KOⁱ	K00053
OMAⁱ	KLFEMNR
PhylomeDBⁱ	P05793

Enzyme and pathway databases

UniPathwayⁱ	UPA00047;UER00056 UPA00049;UER00060
BioCycⁱ	EcoCyc:KETOLREDUCTOISOM-MONOMER MetaCyc:KETOLREDUCTOISOM-MONOMER
BRENDAⁱ	1.1.1.86 2026

Miscellaneous databases

EvolutionaryTraceⁱ	P05793
Protein Ontology More...PROⁱ	PR:P05793

Family and domain databases

Gene3Dⁱ	1.10.1040.10, 1 hit
HAMAPⁱ	MF_00435 IlvC, 1 hit
InterProⁱ	View protein in InterPro IPR008927 6-PGluconate_DH-like_C_sf IPR013328 6PGD_dom2 IPR013023 KARI IPR000506 KARI_C IPR013116 KARI_N IPR036291 NAD(P)-bd_dom_sf
PANTHERⁱ	PTHR21371 PTHR21371, 2 hits
Pfamⁱ	View protein in Pfam PF01450 IlvC, 2 hits PF07991 IlvN, 1 hit
SUPFAMⁱ	SSF48179 SSF48179, 2 hits SSF51735 SSF51735, 1 hit
TIGRFAMsⁱ	TIGR00465 ilvC, 1 hit
PROSITEⁱ	View protein in PROSITE PS51851 KARI_C, 2 hits PS51850 KARI_N, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ILVC_ECOLI
Accessionⁱ	P05793Primary (citable) accession number: P05793 Secondary accession number(s): Q2M883
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
	Last sequence update:	January 23, 2007
	Last modified:	September 12, 2018
	This is version 169 of the entry and version 4 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families
PATHWAY comments
Index of metabolic and biosynthesis pathways
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

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UniProtKB - P05793 (ILVC_ECOLI)

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Ketol-acid reductoisomerase (NADP(+))

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

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Pathwayi: L-valine biosynthesis

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GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

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Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

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<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

2D gel databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

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Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

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Chemistry databases

2D gel databases

Proteomic databases

Protocols and materials databases

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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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Functionⁱ

Kineticsⁱ

Pathwayⁱ: L-isoleucine biosynthesis

Pathwayⁱ: L-valine biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ