ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q9RQ51


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name ILVC_BUCSC
Primary accession number Q9RQ51
Secondary accession numbers None
Integrated into Swiss-Prot on August 29, 2001
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 44)
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
From
Buchnera aphidicola subsp. Schlechtendalia chinensis [TaxID: 118110] 
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10555290 [NCBI, ExPASy, EBI, Israel, Japan]
Clark M.A., Moran N.A., Baumann P.;
"Sequence evolution in bacterial endosymbionts having extreme base compositions.";
Mol. Biol. Evol. 16:1586-1598(1999).
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
AF130813; AAF13803.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP Q9HVA2; 1NP3. [HSSP ENTRY / PDB]
ModBase Q9RQ51.
Ontologies
GO
GO:0004455; Molecular function: ketol-acid reductoisomerase activity (inferred from electronic annotation from HAMAP).
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from InterPro).
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.
IPR014359; KetolA_reductoisomerase_bac.
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.
PIRSF PIRSF000116; IlvC_gammaproteo; 1.
TIGRFAMs TIGR00465; ilvC; 1.
ProtoNet Q9RQ51.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   489  489     Ketol-acid reductoisomerase. PRO_0000151292
ACT_SITE   131   131        Potential. 
Sequence information
Length: 489 AA [This is the length of the unprocessed precursor] Molecular weight: 55710 Da [This is the MW of the unprocessed precursor] CRC64: BFB94B15F507641F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNYFNSLNFR QKLINLRKCK LVEKNFFSKK CDILKRKNIV IVGCGSQGLN QGLNMRDSGL 

        70         80         90        100        110        120 
HVSYALRGSS ILNKNKSWEN ATKNNFFVDT YENIIPTADL VINLTPDKQR KEVVTLLQKF 

       130        140        150        160        170        180 
MKENSVLGFS HGFHIVEIGQ KIRNDITVIM VAPKCPGTEV REEYKKGFGV PSLIAVHMEN 

       190        200        210        220        230        240 
DPKKIGFEIA KAWAYSLGSH RAGVLHSSFI AEVKSDLMGE QTILCGMLQT SSLVCYDQLV 

       250        260        270        280        290        300 
SQGKDPNYAG KLIQLGWESI TESVKHGGIT LMLNRLSNTA KIRAYILSKK LKVMFSSLFR 

       310        320        330        340        350        360 
KHMDDIISGE FSKNMIDDWN SDDKKLKEWR TQIKKTDFEK CKICHKEISE QEYFDQGLLM 

       370        380        390        400        410        420 
VAILKAGIEL SFEIMVETGI KEESAYYESL HELPLIANTI ARKRLYEMNL VISDTAEYGS 

       430        440        450        460        470        480 
YLFSQSAIPL LKEFMNELCP GDLGEKISDL QFDNVTLNKI NHDIENHPVE IIGKKLRKYM 


VDMKPIKLS 

Q9RQ51 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!