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Protein

Ketol-acid reductoisomerase

Gene

ilvC

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Reviewed-Annotation score: Annotation score: 3 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.UniRule annotation
(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP+ = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH.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 (ilvB), Acetolactate synthase small subunit (ilvH)
  2. Ketol-acid reductoisomerase (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD), 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.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase (ilvB), Acetolactate synthase small subunit (ilvH)
  2. Ketol-acid reductoisomerase (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD), 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 sitei109 – 1091UniRule annotation

GO - Molecular functioni

GO - Biological processi

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

BioCyciMSME246196:GJ4Y-2374-MONOMER.
UniPathwayiUPA00047; UER00056.
UPA00049; UER00060.

Names & Taxonomyi

Protein namesi
Recommended name:
Ketol-acid reductoisomeraseUniRule annotation (EC:1.1.1.86UniRule annotation)
Alternative name(s):
Acetohydroxy-acid isomeroreductaseUniRule annotation
Alpha-keto-beta-hydroxylacyl reductoisomeraseUniRule annotation
Gene namesi
Name:ilvCUniRule annotation
Ordered Locus Names:MSMEG_2374, MSMEI_2314
OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Taxonomic identifieri246196 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000006158 Componenti: Chromosome
  • UP000000757 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 337337Ketol-acid reductoisomerasePRO_1000050539Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi246196.MSMEG_2374.

Structurei

3D structure databases

ProteinModelPortaliA0QUX8.
SMRiA0QUX8. Positions 3-329.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ketol-acid reductoisomerase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C6M. Bacteria.
COG0059. LUCA.
HOGENOMiHOG000016230.
KOiK00053.
OMAiFETCHEL.
OrthoDBiEOG625K07.

Family and domain databases

Gene3Di1.10.1040.10. 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. 1 hit.
PF07991. IlvN. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00465. ilvC. 1 hit.

Sequencei

Sequence statusi: Complete.

A0QUX8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVEMFYDDD ADLSIIQGRK VAVIGYGSQG HAHSLSLRDS GVQVKVGLKE
60 70 80 90 100
GSKSREKAEE QGLEVDTPAE VAKWADVIML LAPDTAQASI FTNDIEPNLE
110 120 130 140 150
DGNALFFGHG LNIHFGLIKA PENVTVGMVA PKGPGHLVRR QFVDGKGVPC
160 170 180 190 200
LIAIDQDPKG EGQALALSYA AAIGGARAGV IKTTFKEETE TDLFGEQAVL
210 220 230 240 250
CGGTEELIKT GFEVMVEAGY APEMAYFEVL HELKLIVDLI YEGGIARMNY
260 270 280 290 300
SVSDTAEFGG YLSGPRVIDA DTKKRMQDIL KDIQDGSFVK RLVANVEGGN
310 320 330
KELEALRKAN AEHPIEVTGK KLRDLMSWVD RPITETA
Length:337
Mass (Da):36,421
Last modified:January 9, 2007 - v1
Checksum:i234D7C0B441B8A06
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK74365.1.
CP001663 Genomic DNA. Translation: AFP38784.1.
RefSeqiWP_003893742.1. NZ_CP009494.1.
YP_886716.1. NC_008596.1.

Genome annotation databases

EnsemblBacteriaiABK74365; ABK74365; MSMEG_2374.
AFP38784; AFP38784; MSMEI_2314.
GeneIDi4533720.
KEGGimsb:LJ00_11805.
msg:MSMEI_2314.
msm:MSMEG_2374.
PATRICi18077172. VBIMycSme59918_2340.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK74365.1.
CP001663 Genomic DNA. Translation: AFP38784.1.
RefSeqiWP_003893742.1. NZ_CP009494.1.
YP_886716.1. NC_008596.1.

3D structure databases

ProteinModelPortaliA0QUX8.
SMRiA0QUX8. Positions 3-329.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi246196.MSMEG_2374.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK74365; ABK74365; MSMEG_2374.
AFP38784; AFP38784; MSMEI_2314.
GeneIDi4533720.
KEGGimsb:LJ00_11805.
msg:MSMEI_2314.
msm:MSMEG_2374.
PATRICi18077172. VBIMycSme59918_2340.

Phylogenomic databases

eggNOGiENOG4105C6M. Bacteria.
COG0059. LUCA.
HOGENOMiHOG000016230.
KOiK00053.
OMAiFETCHEL.
OrthoDBiEOG625K07.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00056.
UPA00049; UER00060.
BioCyciMSME246196:GJ4Y-2374-MONOMER.

Family and domain databases

Gene3Di1.10.1040.10. 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. 1 hit.
PF07991. IlvN. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00465. ilvC. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  2. "Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
    Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
    Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  3. "Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
    Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
    Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 700084 / mc(2)155.

Entry informationi

Entry nameiILVC_MYCS2
AccessioniPrimary (citable) accession number: A0QUX8
Secondary accession number(s): I7G813
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 9, 2007
Last modified: November 11, 2015
This is version 72 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.