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Protein

Ketol-acid reductoisomerase (NADP(+))

Gene

ilvC

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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.UniRule annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotationNote: Binds 2 magnesium ions per subunit.UniRule annotation

Pathwayi: L-isoleucine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase large subunit (ilvB)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. no protein annotated in this organism
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 annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase large subunit (ilvB)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. no protein annotated in this organism
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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei49 – 491NADPUniRule annotation
Binding sitei52 – 521NADPUniRule annotation
Binding sitei54 – 541NADPUniRule annotation
Active sitei109 – 1091UniRule annotation
Binding sitei135 – 1351NADP; via amide nitrogenUniRule annotation
Metal bindingi192 – 1921Magnesium 1UniRule annotation
Metal bindingi192 – 1921Magnesium 2UniRule annotation
Metal bindingi196 – 1961Magnesium 1UniRule annotation
Metal bindingi228 – 2281Magnesium 2UniRule annotation
Metal bindingi232 – 2321Magnesium 2UniRule annotation
Binding sitei253 – 2531SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 294NADPUniRule annotation
Nucleotide bindingi84 – 874NADPUniRule annotation

GO - Molecular functioni

  • 2-dehydropantoate 2-reductase activity Source: CACAO
  • ketol-acid reductoisomerase activity Source: UniProtKB-HAMAP

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00047; UER00056.
UPA00049; UER00060.

Names & Taxonomyi

Protein namesi
Recommended name:
Ketol-acid reductoisomerase (NADP(+))UniRule annotation (EC:1.1.1.86UniRule annotation)
Short name:
KARIUniRule annotation
Alternative name(s):
Acetohydroxy-acid isomeroreductaseUniRule annotation
Short name:
AHIRUniRule annotation
Alpha-keto-beta-hydroxylacyl reductoisomeraseUniRule annotation
Ketol-acid reductoisomerase type 1UniRule annotation
Ketol-acid reductoisomerase type IUniRule annotation
Gene namesi
Name:ilvCUniRule annotation
Ordered Locus Names:Cgl1273, cg1437
OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Taxonomic identifieri196627 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
Proteomesi
  • UP000000582 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 338338Ketol-acid reductoisomerase (NADP(+))PRO_0000151306Add
BLAST

2D gel databases

World-2DPAGE0001:Q57179.

Interactioni

Protein-protein interaction databases

STRINGi196627.cg1437.

Structurei

3D structure databases

ProteinModelPortaliQ57179.
SMRiQ57179. Positions 4-329.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 179164IlvNUniRule annotationAdd
BLAST
Domaini185 – 328144IlvCUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ketol-acid reductoisomerase family.UniRule annotation
Contains 1 IlvC domain.UniRule annotation
Contains 1 IlvN domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG0059. LUCA.
HOGENOMiHOG000016230.
KOiK00053.
OMAiFETCHEL.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
HAMAPiMF_00435. IlvC. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR000506. AcH_isomrdctse_C.
IPR013116. IlvN.
IPR013023. Ketol-acid_reductoisomrdctse.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR21371. PTHR21371. 1 hit.
PfamiPF01450. IlvC. 1 hit.
PF07991. IlvN. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00465. ilvC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q57179-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIELLYDAD ADLSLIQGRK VAIVGYGSQG HAHSQNLRDS GVEVVIGLRE
60 70 80 90 100
GSKSAEKAKE AGFEVKTTAE AAAWADVIML LAPDTSQAEI FTNDIEPNLN
110 120 130 140 150
AGDALLFGHG LNIHFDLIKP ADDIIVGMVA PKGPGHLVRR QFVDGKGVPC
160 170 180 190 200
LIAVDQDPTG TAQALTLSYA AAIGGARAGV IPTTFEAETV TDLFGEQAVL
210 220 230 240 250
CGGTEELVKV GFEVLTEAGY EPEMAYFEVL HELKLIVDLM FEGGISNMNY
260 270 280 290 300
SVSDTAEFGG YLSGPRVIDA DTKSRMKDIL TDIQDGTFTK RLIANVENGN
310 320 330
TELEGLRASY NNHPIEETGA KLRDLMSWVK VDARAETA
Length:338
Mass (Da):36,159
Last modified:November 1, 1996 - v1
Checksum:i9BA1697FA7D2A082
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09232 Genomic DNA. Translation: AAA62431.1.
D14551 Genomic DNA. Translation: BAA03414.1.
BA000036 Genomic DNA. Translation: BAB98666.1.
BX927151 Genomic DNA. Translation: CAF19976.1.
PIRiC48648.
RefSeqiNP_600495.1. NC_003450.3.
WP_003854117.1. NC_006958.1.

Genome annotation databases

EnsemblBacteriaiBAB98666; BAB98666; BAB98666.
CAF19976; CAF19976; cg1437.
GeneIDi1019254.
KEGGicgb:cg1437.
cgl:NCgl1224.
PATRICi21494588. VBICorGlu203724_1250.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09232 Genomic DNA. Translation: AAA62431.1.
D14551 Genomic DNA. Translation: BAA03414.1.
BA000036 Genomic DNA. Translation: BAB98666.1.
BX927151 Genomic DNA. Translation: CAF19976.1.
PIRiC48648.
RefSeqiNP_600495.1. NC_003450.3.
WP_003854117.1. NC_006958.1.

3D structure databases

ProteinModelPortaliQ57179.
SMRiQ57179. Positions 4-329.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196627.cg1437.

2D gel databases

World-2DPAGE0001:Q57179.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB98666; BAB98666; BAB98666.
CAF19976; CAF19976; cg1437.
GeneIDi1019254.
KEGGicgb:cg1437.
cgl:NCgl1224.
PATRICi21494588. VBICorGlu203724_1250.

Phylogenomic databases

eggNOGiCOG0059. LUCA.
HOGENOMiHOG000016230.
KOiK00053.
OMAiFETCHEL.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00056.
UPA00049; UER00060.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
HAMAPiMF_00435. IlvC. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR000506. AcH_isomrdctse_C.
IPR013116. IlvN.
IPR013023. Ketol-acid_reductoisomrdctse.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR21371. PTHR21371. 1 hit.
PfamiPF01450. IlvC. 1 hit.
PF07991. IlvN. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00465. ilvC. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiILVC_CORGL
AccessioniPrimary (citable) accession number: Q57179
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: September 7, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.