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UniProtKB/Swiss-Prot entry A1UT97

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

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Entry information
Entry name ILVC_BARBK
Primary accession number A1UT97
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on February 6, 2007 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 17)
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: BARBAKC583_0917
From
Bartonella bacilliformis (strain ATCC 35685 / KC583) [TaxID: 360095] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bartonellaceae; Bartonella.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S., Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R., Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J., Fraser-Ligget C., Seshadri R.;
Submitted (DEC-2006) 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
CP000524; ABM44512.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_989200.1; -.
3D structure databases
ModBase A1UT97.
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 A1UT97.
ProtoNet A1UT97.
Genome annotation databases
GeneID 4683917; -.
GenomeReviews CP000524_GR; BARBAKC583_0917.
KEGG bbk:BARBAKC583_0917; -.
NMPDR fig|360095.3.peg.521; -.
TIGR BARBAKC583_0917; -.
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   339  339     Ketol-acid reductoisomerase. PRO_1000050480
ACT_SITE   108   108        Potential. 
Sequence information
Length: 339 AA [This is the length of the unprocessed precursor] Molecular weight: 37357 Da [This is the MW of the unprocessed precursor] CRC64: 7AB4449FF07D0EE5 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MRVYYDCDVN VNLIKEKKVA IVGYGAQGHA HALNLKDSGV QNVRIALHSG SMTTKKAEAD 

        70         80         90        100        110        120 
GFEVMSVAEA VQWADFIMIA TPDELQADIY KEHIHDHLRD GAAISFAHGL SIHFGLIKVK 

       130        140        150        160        170        180 
KTVDVVMIAP KGAGRAVRSE YQHGRGIPCL IAVEQDVSGN AHDLALSYAC GIGGGRSGIM 

       190        200        210        220        230        240 
KTTFREECET DLFGEQAVLC GGLVELIRAG FETLTEAGYA PEMAYFECLH EIKIIADLIY 

       250        260        270        280        290        300 
ECGIANMNYS ISNTAEWGEY VSGPRVITHE TKAEMKRILK DIQTGKFTSE WIQEYRAGAA 

       310        320        330 
RFKDMRRLNS NHLIEQTGDK IRSMMALTKS SAPVDKKHS
A1UT97 in FASTA format

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