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UniProtKB/Swiss-Prot entry Q7VZU4


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

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Entry information
Entry name ILVC_BORPE
Primary accession number Q7VZU4
Secondary accession numbers None
Integrated into Swiss-Prot on July 19, 2004
Sequence was last modified on October 1, 2003 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 30)
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: BP0791
From
Bordetella pertussis [TaxID: 520] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Alcaligenaceae; Bordetella.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
DOI=10.1038/ng1227; PubMed=12910271 [NCBI, ExPASy, EBI, Israel, Japan]
Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica.";
Nat. Genet. 35:32-40(2003).
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
BX640413; CAE41096.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_879606.1; -.
3D structure databases
SMR Q7VZU4; 1-327.
ModBase Q7VZU4.
Enzyme and pathway databases
BioCyc BPER257313:BP0791-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: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 Q7VZU4.
Genome annotation databases
GeneID 2664321; -.
GenomeReviews BX470248_GR; BP0791.
KEGG bpe:BP0791; -.
NMPDR fig|257313.1.peg.685; -.
Phylogenomic databases
HOGENOM Q7VZU4; -.
Genome annotation databases
CMR Q7VZU4; BP0791.
Other
ProtoNet Q7VZU4.
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_0000151282
ACT_SITE   107   107        Potential. 
Sequence information
Length: 338 AA [This is the length of the unprocessed precursor] Molecular weight: 36206 Da [This is the MW of the unprocessed precursor] CRC64: 836AC62B01D367DC [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKVFYDKDCD LSLVKGKTVA IIGYGSQGHA HALNLHDSGV KVVVGLRKGG ASWNKAANAG 

        70         80         90        100        110        120 
LEVAEVAEAV KRADIVMMLL PDENIAAVYR DEVHANIKAG AALAFAHGFN VHYGQVVPRE 

       130        140        150        160        170        180 
DIDVIMAAPK APGHTVRSTY SQGGGVPHLI AVYQDKSGSA RDVALSYASA NGGGRAGIIE 

       190        200        210        220        230        240 
TNFREETETD LFGEQAVLCG GTVELIKAGF DTLVEAGYAP EMAYFECLHE LKLIVDLIYE 

       250        260        270        280        290        300 
GGIANMNYSI SNNAEFGEYE TGPKVVTDAT RQAMRECLTA IQTGEYAKKF ILENAAGAPT 

       310        320        330 
LTSRRRINAE SQIEQVGGKL RAMMPWIAAN KLVDKAKN 

Q7VZU4 in FASTA format

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