Ketol-acid reductoisomerase - Escherichia coli (strain K12)

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P05793 (ILVC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 127. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	b3774, JW3747

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

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)

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
Induction	In the presence of acetohydroxybutyrate and acetolactate, the substrates of ketol-acid reductoisomerase. 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	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	isoleucine biosynthetic process Inferred from direct assay PubMed 4562389. Source: EcoCyc valine biosynthetic process Inferred from direct assay PubMed 2653423. Source: EcoCyc
Cellular_component	cytosol Inferred from direct assay PubMed 2653423. Source: EcoCyc
Molecular_function	NADP binding Inferred from electronic annotation. Source: InterPro ketol-acid reductoisomerase activity Inferred from direct assay PubMed 2653423. Source: EcoCyc
Complete GO annotation...

Binary interactions

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.5

Chain

2 – 491

490

Ketol-acid reductoisomerase HAMAP-Rule MF_00435

PRO_0000151309

Sites

Active site

132

Potential

Experimental info

Sequence conflict

251

E → K in AAA24029. Ref.1

Secondary structure

491

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P05793 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 9CA34BA61C9AEBBA
Show »

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

« Hide

References

	« 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / EMG2.
+	Additional computationally mapped references.

Cross-references

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

NP_418222.1. NC_000913.2.
YP_491664.1. NC_007779.1.

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	[»]
3ULK	X-ray	2.30	A/B	1-491	[»]

ProteinModelPortal

P05793.

SMR

P05793. Positions 3-489.

ModBase

Search...

Protein-protein interaction databases

IntAct

P05793. 3 interactions.

STRING

511145.b3774.

2D gel databases

SWISS-2DPAGE

P05793.

Proteomic databases

PaxDb

P05793.

PRIDE

P05793.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76779; AAC76779; b3774.
BAE77523; BAE77523; BAE77523.

GeneID

12934337.
948286.

KEGG

ecj:Y75_p3401.
eco:b3774.

PATRIC

32123043. VBIEscCol129921_3891.

Organism-specific databases

EchoBASE

EB0490.

EcoGene

EG10495. ilvC.

Phylogenomic databases

eggNOG

COG0059.

HOGENOM

HOG000286135.

K00053.

OMA

NMMDRLS.

ProtClustDB

PRK05225.

Enzyme and pathway databases

BioCyc

EcoCyc:KETOLREDUCTOISOM-MONOMER.
ECOL316407:JW3747-MONOMER.
MetaCyc:KETOLREDUCTOISOM-MONOMER.

UniPathway

UPA00047; UER00056.
UPA00049; UER00060.

Gene expression databases

Genevestigator

P05793.

Family and domain databases

Gene3D

1.10.1040.10. 1 hit.
3.40.50.720. 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.
IPR014359. KetolA_reductoisomerase_bac.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

PANTHER

PTHR21371. PTHR21371. 1 hit.
PTHR21371:SF2. PTHR21371:SF2. 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...

Other

BindingDB

P05793.

EvolutionaryTrace

P05793.

Entry information

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:	May 1, 2013
This is version 127 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents