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Protein

Ketol-acid reductoisomerase

Gene

ilvC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi: L-isoleucine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase isozyme 1 small subunit (ilvN), Acetolactate synthase isozyme 1 large subunit (ilvB), Acetolactate synthase isozyme 2 small subunit (ilvM), Acetolactate synthase isozyme 3 large subunit (ilvI), Acetolactate synthase isozyme 3 small subunit (ilvH), Acetolactate synthase isozyme 2 large subunit (ilvG)
  2. Ketol-acid reductoisomerase (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. Branched-chain-amino-acid aminotransferase (ilvE)
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.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase isozyme 1 small subunit (ilvN), Acetolactate synthase isozyme 1 large subunit (ilvB), Acetolactate synthase isozyme 2 small subunit (ilvM), Acetolactate synthase isozyme 3 large subunit (ilvI), Acetolactate synthase isozyme 3 small subunit (ilvH), Acetolactate synthase isozyme 2 large subunit (ilvG)
  2. Ketol-acid reductoisomerase (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. Branched-chain-amino-acid aminotransferase (ilvE)
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
Active sitei132 – 1321Sequence analysis

GO - Molecular functioni

  • ketol-acid reductoisomerase activity Source: EcoCyc
  • magnesium ion binding Source: EcoCyc
  • NADP binding Source: EcoCyc

GO - Biological processi

  • isoleucine biosynthetic process Source: EcoCyc
  • valine biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciEcoCyc:KETOLREDUCTOISOM-MONOMER.
ECOL316407:JW3747-MONOMER.
MetaCyc:KETOLREDUCTOISOM-MONOMER.
BRENDAi1.1.1.86. 2026.
UniPathwayiUPA00047; UER00056.
UPA00049; UER00060.

Names & Taxonomyi

Protein namesi
Recommended name:
Ketol-acid reductoisomerase (EC:1.1.1.86)
Alternative name(s):
Acetohydroxy-acid isomeroreductase
Alpha-keto-beta-hydroxylacyl reductoisomerase
Gene namesi
Name:ilvC
Ordered Locus Names:b3774, JW3747
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10495. ilvC.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2366462.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 491490Ketol-acid reductoisomerasePRO_0000151309Add
BLAST

Proteomic databases

EPDiP05793.
PaxDbiP05793.
PRIDEiP05793.

2D gel databases

SWISS-2DPAGEP05793.

Expressioni

Inductioni

In the presence of acetohydroxybutyrate and acetolactate, the substrates of ketol-acid reductoisomerase.

Interactioni

Protein-protein interaction databases

BioGridi4263331. 5 interactions.
IntActiP05793. 4 interactions.
STRINGi511145.b3774.

Chemistry

BindingDBiP05793.

Structurei

Secondary structure

1
491
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 73Combined sources
Helixi10 – 178Combined sources
Beta strandi20 – 223Combined sources
Helixi25 – 284Combined sources
Turni29 – 324Combined sources
Helixi33 – 353Combined sources
Beta strandi38 – 447Combined sources
Helixi47 – 5812Combined sources
Beta strandi62 – 676Combined sources
Helixi69 – 735Combined sources
Helixi77 – 848Combined sources
Beta strandi88 – 914Combined sources
Helixi92 – 954Combined sources
Helixi96 – 983Combined sources
Beta strandi100 – 1045Combined sources
Helixi108 – 1103Combined sources
Helixi111 – 1188Combined sources
Helixi119 – 1213Combined sources
Beta strandi127 – 1326Combined sources
Helixi134 – 1374Combined sources
Beta strandi147 – 15610Combined sources
Helixi158 – 1669Combined sources
Beta strandi173 – 1775Combined sources
Helixi179 – 1813Combined sources
Helixi187 – 19711Combined sources
Helixi200 – 2023Combined sources
Beta strandi205 – 2073Combined sources
Helixi210 – 22213Combined sources
Turni223 – 2264Combined sources
Helixi227 – 24216Combined sources
Helixi247 – 27529Combined sources
Helixi279 – 30931Combined sources
Helixi311 – 32111Combined sources
Turni322 – 3243Combined sources
Helixi325 – 33612Combined sources
Helixi338 – 3414Combined sources
Helixi351 – 3566Combined sources
Helixi359 – 37719Combined sources
Turni378 – 3803Combined sources
Helixi383 – 3886Combined sources
Helixi391 – 3933Combined sources
Helixi394 – 41219Combined sources
Helixi415 – 43117Combined sources
Helixi433 – 4375Combined sources
Beta strandi443 – 4464Combined sources
Helixi455 – 46612Combined sources
Helixi469 – 48719Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YRLX-ray2.60A/B/C/D1-491[»]
3ULKX-ray2.30A/B1-491[»]
ProteinModelPortaliP05793.
SMRiP05793. Positions 3-489.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05793.

Family & Domainsi

Sequence similaritiesi

Belongs to the ketol-acid reductoisomerase family.Curated

Phylogenomic databases

eggNOGiENOG4105C6M. Bacteria.
COG0059. LUCA.
HOGENOMiHOG000286135.
InParanoidiP05793.
KOiK00053.
OMAiKLFEMNR.
OrthoDBiEOG625K07.
PhylomeDBiP05793.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_00435. IlvC.
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. 2 hits.
PF07991. IlvN. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00465. ilvC. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P05793-1 [UniParc]FASTAAdd 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti251 – 2511E → K in AAA24029 (PubMed:3003115).Curated

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.
PIRiA65181. ISECKR.
RefSeqiNP_418222.1. NC_000913.3.
WP_000024939.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76779; AAC76779; b3774.
BAE77523; BAE77523; BAE77523.
GeneIDi948286.
KEGGiecj:JW3747.
eco:b3774.
PATRICi32123043. VBIEscCol129921_3891.

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.
PIRiA65181. ISECKR.
RefSeqiNP_418222.1. NC_000913.3.
WP_000024939.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YRLX-ray2.60A/B/C/D1-491[»]
3ULKX-ray2.30A/B1-491[»]
ProteinModelPortaliP05793.
SMRiP05793. Positions 3-489.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263331. 5 interactions.
IntActiP05793. 4 interactions.
STRINGi511145.b3774.

Chemistry

BindingDBiP05793.
ChEMBLiCHEMBL2366462.

2D gel databases

SWISS-2DPAGEP05793.

Proteomic databases

EPDiP05793.
PaxDbiP05793.
PRIDEiP05793.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76779; AAC76779; b3774.
BAE77523; BAE77523; BAE77523.
GeneIDi948286.
KEGGiecj:JW3747.
eco:b3774.
PATRICi32123043. VBIEscCol129921_3891.

Organism-specific databases

EchoBASEiEB0490.
EcoGeneiEG10495. ilvC.

Phylogenomic databases

eggNOGiENOG4105C6M. Bacteria.
COG0059. LUCA.
HOGENOMiHOG000286135.
InParanoidiP05793.
KOiK00053.
OMAiKLFEMNR.
OrthoDBiEOG625K07.
PhylomeDBiP05793.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00056.
UPA00049; UER00060.
BioCyciEcoCyc:KETOLREDUCTOISOM-MONOMER.
ECOL316407:JW3747-MONOMER.
MetaCyc:KETOLREDUCTOISOM-MONOMER.
BRENDAi1.1.1.86. 2026.

Miscellaneous databases

EvolutionaryTraceiP05793.
PROiP05793.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_00435. IlvC.
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. 2 hits.
PF07991. IlvN. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00465. ilvC. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiILVC_ECOLI
AccessioniPrimary (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: April 13, 2016
This is version 151 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.