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UniProtKB/Swiss-Prot entry Q9FBT8


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

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Entry information
Entry name ILVC2_STRCO
Primary accession number Q9FBT8
Secondary accession numbers None
Integrated into Swiss-Prot on August 29, 2001
Sequence was last modified on March 1, 2001 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 52)
Name and origin of the protein
Protein name Ketol-acid reductoisomerase 2
Synonyms EC 1.1.1.86
Acetohydroxy-acid isomeroreductase 2
Alpha-keto-beta-hydroxylacil reductoisomerase 2
Gene name
Name: ilvC2
OrderedLocusNames: SCO7154
ORFNames: SC9A4.16c
From
Streptomyces coelicolor [TaxID: 1902] [HAMAP proteome]
Taxonomy Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Streptomycineae; Streptomycetaceae; Streptomyces.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-471 / A3(2) / M145;
DOI=10.1038/417141a; PubMed=12000953 [NCBI, ExPASy, EBI, Israel, Japan]
Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2).";
Nature 417:141-147(2002).
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
AL939130; CAC01643.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_631213.1; -.
3D structure databases
HSSP Q9HVA2; 1NP3. [HSSP ENTRY / PDB]
ModBase Q9FBT8.
Enzyme and pathway databases
BioCyc SCOE100226:SCO7154-MON; -.
Ontologies
GO
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.
BLOCKS Q9FBT8.
ProtoNet Q9FBT8.
Genome annotation databases
GeneID 1102592; -.
GenomeReviews AL645882_GR; SCO7154.
KEGG sco:SCO7154; -.
NMPDR fig|100226.1.peg.7088; -.
Phylogenomic databases
HOGENOM Q9FBT8; -.
Genome annotation databases
CMR Q9FBT8; SCO7154.
Other
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   332  332     Ketol-acid reductoisomerase 2. PRO_0000151364
ACT_SITE   108   108        Potential. 
Sequence information
Length: 332 AA [This is the length of the unprocessed precursor] Molecular weight: 36348 Da [This is the MW of the unprocessed precursor] CRC64: D984A88B0BFF9655 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAELFYDADA DLSIIQGRKV AVIGYGSQGH AHALSLRDSG VDVRVGLHEG SKSKAKAEEQ 

        70         80         90        100        110        120 
GLRVVPVAEA AAEADVIMIL VPDPIQAEVY EKDIKDNLKD GDALFFGHGL NIRYGFVKPP 

       130        140        150        160        170        180 
AGVDVCMVAP KGPGHLVRRQ YEEGRGVPCL VAVEQDATGN AFALALSYAK GIGGTRAGVI 

       190        200        210        220        230        240 
RTTFTEETET DLFGEQAVLA GGVTALVKAG FETLTEAGYQ PEIAYFECLH ELKLIVDLMY 

       250        260        270        280        290        300 
EGGLEKMRWS ISETAEWGDY VTGPRIITDV TKAEMRKVLA EIQDGTFAKN WMDEYHGGLK 

       310        320        330 
KYNEYKKQDS EHLLETTGKE LRKLMSWVDE EA 

Q9FBT8 in FASTA format

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