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UniProtKB/Swiss-Prot entry Q0VSB5

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ILVC_ALCBS
Primary accession number Q0VSB5
Secondary accession numbers None
Integrated into Swiss-Prot on October 17, 2006
Sequence was last modified on October 17, 2006 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 20)
Name and origin of the protein
Protein name Ketol-acid reductoisomerase
Synonyms EC 1.1.1.86
Acetohydroxy-acid isomeroreductase
Alpha-keto-beta-hydroxylacil reductoisomerase
Gene name
Name: ilvC
OrderedLocusNames: ABO_0485
From
Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [TaxID: 393595] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; Alcanivoracaceae; Alcanivorax.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nbt1232; PubMed=16878126 [NCBI, ExPASy, EBI, Israel, Japan]
Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
"Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium Alcanivorax borkumensis.";
Nat. Biotechnol. 24:997-1004(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AM286690; CAL15933.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_692205.1; -.
3D structure databases
SMR Q0VSB5; 1-327.
ModBase Q0VSB5.
Enzyme and pathway databases
BioCyc ABOR393595:ABO_0485-MON; -.
Ontologies
GO
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0004455; Molecular function: ketol-acid reductoisomerase activity (inferred from electronic annotation from HAMAP).
GO:0009097; Biological process: isoleucine biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0009099; Biological process: valine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00435; -; 1.
PBIL [Tree]
InterPro IPR013023; AcH_isomrdctse.
IPR000506; AcH_isomrdctse_C.
IPR013116; IlvN.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR21371; AcH_isomrdctse; 1.
Pfam PF01450; IlvC; 1.
PF07991; IlvN; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00465; ilvC; 1.
Genome annotation databases
GeneID 4211352; -.
GenomeReviews AM286690_GR; ABO_0485.
KEGG abo:ABO_0485; -.
NMPDR fig|393595.12.peg.482; -.
Phylogenomic databases
HOGENOM Q0VSB5; -.
Genome annotation databases
CMR Q0VSB5; ABO_0485.
Other
ProtoNet Q0VSB5.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Complete proteome; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   338  338     Ketol-acid reductoisomerase. PRO_0000252748
ACT_SITE   107   107        Potential. 
Sequence information
Length: 338 AA [This is the length of the unprocessed precursor] Molecular weight: 36297 Da [This is the MW of the unprocessed precursor] CRC64: 3E503EF2FAFB470F [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MQVYYDKDCD LSIIQGKKVA ILGYGSQGHA HACNLKDSGV DVVVGLRTGS TSIAKAEAHG 

        70         80         90        100        110        120 
LSVTDVPSAV AAADVVMVLT PDEFQAHLYK SDIEPNLKEG ATLAFAHGFA IHYNQIVPRA 

       130        140        150        160        170        180 
DLDVIMIAPK APGHTVRTEF TKGGGIPDLI AIFQDASGSA KELALSYACG VGGGRTGIIE 

       190        200        210        220        230        240 
TTFKDETETD LFGEQAVLCG GAVELVKAGF ETLTEAGYAP EMAYFECLHE LKLIVDLMYE 

       250        260        270        280        290        300 
GGIANMNYSI SNNAEYGEYV TGPEVINDES RAAMRNALKR IQSGEYAKMF IAEGAHNYPS 

       310        320        330 
MTAARRNNAA HPIEQVGEKL RGMMPWIQAN QIVDKTKN
Q0VSB5 in FASTA format

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