Reviewed, UniProtKB/Swiss-Prot P05793 (ILVC_ECOLI)

Names and originHide

Protein names

Recommended name:
Ketol-acid reductoisomerase
EC=1.1.1.86

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

Gene names

Name:	ilvC
Ordered Locus Names:	b3774, JW3747

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributesHide

Sequence length	491 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)Hide

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

OntologiesHide

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	isoleucine biosynthetic process Inferred from direct assay. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW valine biosynthetic process Inferred from direct assay. Source: UniProtKB
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	NADP or NADPH binding Inferred from electronic annotation. Source: InterPro ketol-acid reductoisomerase activity Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactionsHide

With	Entry	#Exp.	IntAct	Notes
rhsC	P16918	1	EBI-1133427,EBI-546818

Sequence annotation (Features)Hide

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 491

490

Ketol-acid reductoisomerase HAMAP MF_00435

PRO_0000151309

Sites

Active site

132

1

Potential

Experimental info

Sequence conflict

251

1

E → K in AAA24029. Ref.1

Secondary structure

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491

Helix Strand Turn

Details...

Helix

5 – 7

3

Helix

10 – 17

8

Beta strand

20 – 22

3

Helix

25 – 28

4

Turn

29 – 32

4

Helix

33 – 35

3

Beta strand

40 – 43

4

Helix

47 – 58

12

Beta strand

63 – 67

5

Helix

69 – 73

5

Helix

77 – 84

8

Beta strand

88 – 91

4

Helix

92 – 95

4

Helix

96 – 98

3

Beta strand

100 – 104

5

Helix

108 – 121

14

Beta strand

127 – 132

6

Helix

134 – 137

4

Beta strand

147 – 155

9

Helix

160 – 166

7

Beta strand

173 – 177

5

Helix

179 – 181

3

Helix

187 – 198

12

Helix

200 – 203

4

Beta strand

205 – 208

4

Helix

210 – 222

13

Turn

223 – 226

4

Helix

227 – 242

16

Helix

247 – 275

29

Helix

279 – 308

30

Helix

311 – 320

10

Turn

321 – 324

4

Helix

325 – 334

10

Helix

338 – 341

4

Helix

351 – 356

6

Helix

359 – 377

19

Turn

378 – 380

3

Helix

383 – 389

7

Turn

390 – 393

4

Helix

394 – 412

19

Helix

415 – 437

23

Beta strand

443 – 446

4

Helix

455 – 467

13

Helix

469 – 486

18

SequencesHide

	Sequence		Length	Mass (Da)
	P05793-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 9CA34BA61C9AEBBA	FASTA	491	54,069
	10 20 30 40 50 60 MANYFNTLNL RQQLAQLGKC RFMGRDEFAD GASYLQGKKV VIVGCGAQGL NQGLNMRDSG 70 80 90 100 110 120 LDISYALRKE AIAEKRASWR KATENGFKVG TYEELIPQAD LVINLTPDKQ HSDVVRTVQP 130 140 150 160 170 180 LMKDGAALGY SHGFNIVEVG EQIRKDITVV MVAPKCPGTE VREEYKRGFG VPTLIAVHPE 190 200 210 220 230 240 NDPKGEGMAI AKAWAAATGG HRAGVLESSF VAEVKSDLMG EQTILCGMLQ AGSLLCFDKL 250 260 270 280 290 300 VEEGTDPAYA EKLIQFGWET ITEALKQGGI TLMMDRLSNP AKLRAYALSE QLKEIMAPLF 310 320 330 340 350 360 QKHMDDIISG EFSSGMMADW ANDDKKLLTW REETGKTAFE TAPQYEGKIG EQEYFDKGVL 370 380 390 400 410 420 MIAMVKAGVE LAFETMVDSG IIEESAYYES LHELPLIANT IARKRLYEMN VVISDTAEYG 430 440 450 460 470 480 NYLFSYACVP LLKPFMAELQ PGDLGKAIPE GAVDNGQLRD VNEAIRSHAI EQVGKKLRGY 490 MTDMKRIAVA G

ReferencesHide

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence and in vivo expression of the ilvY and ilvC genes in Escherichia coli K12. Transcription from divergent overlapping promoters." Wek R.C., Hatfield G.W. J. Biol. Chem. 261:2441-2450(1986) [PubMed: 3003115] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes." Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R. Science 257:771-778(1992) [PubMed: 1379743] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / EMG2.
+	Additional computationally mapped references.

Cross-referencesHide

Sequence databases

EMBL
GenBank
DDBJ

M11689 Genomic DNA. Translation: AAA24029.1.
M87049 Genomic DNA. Translation: AAA67577.1.
U00096 Genomic DNA. Translation: AAC76779.1.
AP009048 Genomic DNA. Translation: BAE77523.1.

PIR

ISECKR. A65181.

RefSeq

AP_004022.1.
NP_418222.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YRL	X-ray	2.60	A/B/C/D	1-491	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P05793. 3 interactions.

STRING

P05793.

2-D gel databases

SWISS-2DPAGE

P05793.

Genome annotation databases

EnsemblBacteria

EBESCT00000004501; EBESCP00000004501; EBESCG00000003676.
EBESCT00000016191; EBESCP00000015482; EBESCG00000015251.

GeneID

948286.

GenomeReviews

Gene locus JW3747 in contig AP009048_GR.
Gene locus b3774 in contig U00096_GR.

KEGG

ecj:JW3747.
eco:b3774.

Organism-specific databases

EchoBASE

EB0490.

EcoGene

EG10495. ilvC.

CMR

Search...

Phylogenomic databases

eggNOG

COG0059.

HOGENOM

HBG297205.

OMA

EKHMDDI.

ProtClustDB

PRK05225.

Enzyme and pathway databases

BioCyc

EcoCyc:KETOLREDUCTOISOM-MONOMER.
ECOL168927:B3774-MONOMER.
MetaCyc:KETOLREDUCTOISOM-MONOMER.

Gene expression databases

Genevestigator

P05793.

Family and domain databases

HAMAP

MF_00435. IlvC.
[Tree]

InterPro

IPR008927. 6-PGluconate_DH_C_like.
IPR013023. AcH_isomrdctse.
IPR000506. AcH_isomrdctse_C.
IPR013116. IlvN.
IPR014359. KetolA_reductoisomerase_bac.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

PANTHER

PTHR21371. AcH_isomrdctse. 1 hit.

Pfam

PF01450. IlvC. 2 hits.
PF07991. IlvN. 1 hit.
[Graphical view]

PIRSF

PIRSF000116. IlvC_gammaproteo. 1 hit.

SUPFAM

SSF48179. 6DGDH_C_like. 2 hits.

TIGRFAMs

TIGR00465. ilvC. 1 hit.

ProtoNet

Search...

Entry informationHide

Entry name

ILVC_ECOLI

Accession

Primary (citable) accession number: P05793
Secondary accession number(s): Q2M883

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	January 23, 2007
Last modified:	July 13, 2010
This is version 100 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)