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Protein

Ketol-acid reductoisomerase (NADP(+))

Gene

ilvC

Organism
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.UniRule annotation

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

Cofactori

Mg2+UniRule annotationNote: Binds 2 magnesium ions per subunit.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 (BMEI0617)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. no protein annotated in this organism
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 (BMEI0617)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. no protein annotated in this organism
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)DescriptionActionsGraphical viewLength
Binding sitei48NADPUniRule annotation1
Binding sitei51NADPUniRule annotation1
Binding sitei53NADPUniRule annotation1
Active sitei108UniRule annotation1
Binding sitei134NADP; via amide nitrogenUniRule annotation1
Metal bindingi191Magnesium 1UniRule annotation1
Metal bindingi191Magnesium 2UniRule annotation1
Metal bindingi195Magnesium 1UniRule annotation1
Metal bindingi227Magnesium 2UniRule annotation1
Metal bindingi231Magnesium 2UniRule annotation1
Binding sitei252SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi24 – 27NADPUniRule annotation4
Nucleotide bindingi83 – 86NADPUniRule annotation4

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

Magnesium, Metal-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00047; UER00056.
UPA00049; UER00060.

Names & Taxonomyi

Protein namesi
Recommended name:
Ketol-acid reductoisomerase (NADP(+))UniRule annotation (EC:1.1.1.86UniRule annotation)
Short name:
KARIUniRule annotation
Alternative name(s):
Acetohydroxy-acid isomeroreductaseUniRule annotation
Short name:
AHIRUniRule annotation
Alpha-keto-beta-hydroxylacyl reductoisomeraseUniRule annotation
Ketol-acid reductoisomerase type 1UniRule annotation
Ketol-acid reductoisomerase type IUniRule annotation
Gene namesi
Name:ilvCUniRule annotation
Ordered Locus Names:BMEI0624
OrganismiBrucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Taxonomic identifieri224914 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
Proteomesi
  • UP000000419 Componenti: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001512841 – 339Ketol-acid reductoisomerase (NADP(+))Add BLAST339

Interactioni

Protein-protein interaction databases

STRINGi224914.BAWG_2600.

Structurei

3D structure databases

ProteinModelPortaliQ8YI21.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 178IlvNUniRule annotationAdd BLAST165
Domaini184 – 327IlvCUniRule annotationAdd BLAST144

Sequence similaritiesi

Belongs to the ketol-acid reductoisomerase family.UniRule annotation
Contains 1 IlvC domain.UniRule annotation
Contains 1 IlvN domain.UniRule annotation

Phylogenomic databases

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

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
HAMAPiMF_00435. IlvC. 1 hit.
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.

Q8YI21-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVYYDRDAD VNLIKSKKVV IVGYGSQGRA HALNLKDSGA ANVRVALREG
60 70 80 90 100
SATVQKAQAD GFEVMNVADA AKWADLMMMA TPDELQADIY RDHIHNNLRD
110 120 130 140 150
GAAIAFAHGL NVHCGLIEPK KTVDVMMIAP KGPGHTVRGE YQKGGGVPCL
160 170 180 190 200
IAIHQDASGN AHDLALSYAS GVGGGRSGVI ETTFKEECET DLFGEQAVLC
210 220 230 240 250
GGVVELIRTG FEVLVEAGYA PEMAYFECLN EMKLIVDLIY EGGIANMNYS
260 270 280 290 300
ISNTAEWGEY VTGPRIITAE TKAEMKRVLK DIQTGKFTSD WMQEWKAGAA
310 320 330
RFKGIRRLND AHQIEEVGGK LRAMMPWIEK NKLVDKARN
Length:339
Mass (Da):37,080
Last modified:March 1, 2002 - v1
Checksum:i1A4967D9205EEE92
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008917 Genomic DNA. Translation: AAL51805.1.
PIRiAB3330.
RefSeqiWP_004683995.1. NZ_GG703780.1.

Genome annotation databases

EnsemblBacteriaiAAL51805; AAL51805; BMEI0624.
KEGGibme:BMEI0624.
bmel:DK63_801.
PATRICi17801362. VBIBruMel146950_3006.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008917 Genomic DNA. Translation: AAL51805.1.
PIRiAB3330.
RefSeqiWP_004683995.1. NZ_GG703780.1.

3D structure databases

ProteinModelPortaliQ8YI21.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224914.BAWG_2600.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL51805; AAL51805; BMEI0624.
KEGGibme:BMEI0624.
bmel:DK63_801.
PATRICi17801362. VBIBruMel146950_3006.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00047; UER00056.
UPA00049; UER00060.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
HAMAPiMF_00435. IlvC. 1 hit.
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...

Entry informationi

Entry nameiILVC_BRUME
AccessioniPrimary (citable) accession number: Q8YI21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2003
Last sequence update: March 1, 2002
Last modified: November 2, 2016
This is version 92 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

Documents

  1. Brucella melitensis
    Brucella melitensis (strain 16M): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.