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UniProtKB/Swiss-Prot entry A3MI87

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

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Entry information
Entry name ILVC_BURM7
Primary accession number A3MI87
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on April 3, 2007 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 14)
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: BMA10247_0398
From
Burkholderia mallei (strain NCTC 10247) [TaxID: 320389] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Burkholderiaceae; Burkholderia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DeShazer D., Woods D.E., Nierman W.C.;
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
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
CP000548; ABO07112.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001079973.1; -.
3D structure databases
SMR A3MI87; 1-327.
ModBase A3MI87.
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 A3MI87.
ProtoNet A3MI87.
Genome annotation databases
GeneID 4894061; -.
GenomeReviews CP000548_GR; BMA10247_0398.
KEGG bmn:BMA10247_0398; -.
TIGR BMA10247_0398; -.
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   338  338     Ketol-acid reductoisomerase. PRO_1000050486
ACT_SITE   107   107        Potential. 
Sequence information
Length: 338 AA [This is the length of the unprocessed precursor] Molecular weight: 36267 Da [This is the MW of the unprocessed precursor] CRC64: 7F06A53243A44DA0 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKVFYDKDAD LSLIKGKQVT IIGYGSQGHA HALNLKDSGV NVTVGLRRGG ASWSKAENAG 

        70         80         90        100        110        120 
LAVKEVAEAV KGADVVMMLL PDEQIAAVYA QEVHANIKEG AALAFAHGFN VHYGQVIPRA 

       130        140        150        160        170        180 
DLDVIMVAPK APGHTVRGTY AQGGGVPHLI AVAQDKSGAA RDIALSYAAA NGGGRAGIIE 

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

       250        260        270        280        290        300 
GGIANMNYSI SNNAEYGEYV TGPRVVTEET KKAMKQCLTD IQTGEYAKSF ILENKAGAPT 

       310        320        330 
LQSRRRLTAE HQIEQVGSKL RAMMPWIAKN KLVDQSKN
A3MI87 in FASTA format

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