Q57179 (ILVC_CORGL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ketol-acid reductoisomerase
EC=1.1.1.86

Alternative name(s):
Acetohydroxy-acid isomeroreductase
Alpha-keto-beta-hydroxylacyl reductoisomerase

Gene names

Name:	ilvC
Ordered Locus Names:	Cgl1273, cg1437

Organism

Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]

Taxonomic identifier

196627 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium › Corynebacterium glutamicum

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	(R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH. HAMAP-Rule MF_00435 (2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP+ = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH. HAMAP-Rule MF_00435
Pathway	Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4. HAMAP-Rule MF_00435 Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4. HAMAP-Rule MF_00435
Sequence similarities	Belongs to the ketol-acid reductoisomerase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	isoleucine biosynthetic process Inferred from electronic annotation. Source: HAMAP valine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	coenzyme binding Inferred from electronic annotation. Source: InterPro ketol-acid reductoisomerase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 338	338	Ketol-acid reductoisomerase HAMAP-Rule MF_00435		PRO_0000151306
Sites
	Active site	109	1	Potential

Sequences

	Sequence		Length	Mass (Da)
	Q57179 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 9BA1697FA7D2A082	FASTA	338	36,159
	10 20 30 40 50 60 MAIELLYDAD ADLSLIQGRK VAIVGYGSQG HAHSQNLRDS GVEVVIGLRE GSKSAEKAKE 70 80 90 100 110 120 AGFEVKTTAE AAAWADVIML LAPDTSQAEI FTNDIEPNLN AGDALLFGHG LNIHFDLIKP 130 140 150 160 170 180 ADDIIVGMVA PKGPGHLVRR QFVDGKGVPC LIAVDQDPTG TAQALTLSYA AAIGGARAGV 190 200 210 220 230 240 IPTTFEAETV TDLFGEQAVL CGGTEELVKV GFEVLTEAGY EPEMAYFEVL HELKLIVDLM 250 260 270 280 290 300 FEGGISNMNY SVSDTAEFGG YLSGPRVIDA DTKSRMKDIL TDIQDGTFTK RLIANVENGN 310 320 330 TELEGLRASY NNHPIEETGA KLRDLMSWVK VDARAETA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isoleucine synthesis in Corynebacterium glutamicum: molecular analysis of the ilvB-ilvN-ilvC operon." Keilhauer C., Eggeling L., Sahm H. J. Bacteriol. 175:5595-5603(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]	"Identification and sequence determination of the acetohydroxy acid isomeroreductase gene from Brevibacterium flavum MJ233." Inui M., Vertes A.A., Kobayashi M., Kurusu Y., Yukawa H. DNA Seq. 4:95-103(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: MJ233.
[3]	"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes." Ikeda M., Nakagawa S. Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[4]	"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L09232 Genomic DNA. Translation: AAA62431.1. D14551 Genomic DNA. Translation: BAA03414.1. BA000036 Genomic DNA. Translation: BAB98666.1. BX927151 Genomic DNA. Translation: CAF19976.1.
PIR	C48648.
RefSeq	NP_600495.1. NC_003450.3. YP_225562.1. NC_006958.1.
3D structure databases
ProteinModelPortal	Q57179.
SMR	Q57179. Positions 4-329.
ModBase	Search...
Protein-protein interaction databases
STRING	196627.cg1437.
2D gel databases
World-2DPAGE	0001:Q57179.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB98666; BAB98666; BAB98666. CAF19976; CAF19976; cg1437.
GeneID	1019254. 3343961.
KEGG	cgb:cg1437. cgl:NCgl1224.
PATRIC	21494588. VBICorGlu203724_1250.
Phylogenomic databases
eggNOG	COG0059.
HOGENOM	HOG000016230.
KO	K00053.
OMA	WDITLAY.
ProtClustDB	PRK05479.
Enzyme and pathway databases
BioCyc	CGLU196627:GJDM-1257-MONOMER.
UniPathway	UPA00047; UER00056. UPA00049; UER00060.
Family and domain databases
Gene3D	1.10.1040.10. 1 hit.
HAMAP	MF_00435. IlvC.
InterPro	IPR008927. 6-PGluconate_DH_C-like. IPR013023. AcH_isomrdctse. IPR000506. AcH_isomrdctse_C. IPR013328. DH_multihelical. IPR013116. IlvN. [Graphical view]
PANTHER	PTHR21371. PTHR21371. 1 hit.
Pfam	PF01450. IlvC. 1 hit. PF07991. IlvN. 1 hit. [Graphical view]
SUPFAM	SSF48179. 6DGDH_C_like. 1 hit.
TIGRFAMs	TIGR00465. ilvC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ILVC_CORGL

Accession

Primary (citable) accession number: Q57179

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program