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UniProtKB/Swiss-Prot entry Q81S27


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

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Entry information
Entry name ILVC2_BACAN
Primary accession number Q81S27
Secondary accession numbers Q6I0A6 Q6KU80
Integrated into Swiss-Prot on July 19, 2004
Sequence was last modified on June 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 40)
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
Synonyms: ilvC-2
OrderedLocusNames: BA_1852, GBAA1852, BAS1716
From
Bacillus anthracis [TaxID: 1392] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus cereus group.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Ames / isolate Porton;
DOI=10.1038/nature01586; PubMed=12721629 [NCBI, ExPASy, EBI, Israel, Japan]
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.;
"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria.";
Nature 423:81-86(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Ames ancestor;
Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.;
"Bacillus anthracis comparative genomics.";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Sterne;
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.;
"Complete genome sequence of Bacillus anthracis Sterne.";
Submitted (JAN-2004) 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
AE016879; AAP25755.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE017334; AAT30967.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE017225; AAT54032.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_844269.1; -.
YP_018492.1; -.
YP_027981.1; -.
3D structure databases
HSSP Q9HVA2; 1NP3. [HSSP ENTRY / PDB]
ModBase Q81S27.
Enzyme and pathway databases
BioCyc BANT260799:BAS1716-MON; -.
BANT261594:GBAA1852-MON; -.
Ontologies
GO
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
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.
ProtoNet Q81S27.
Genome annotation databases
GeneID 1086430; -.
2819743; -.
2848291; -.
GenomeReviews AE016879_GR; BA_1852.
AE017225_GR; BAS1716.
AE017334_GR; GBAA1852.
KEGG ban:BA1852; -.
bar:GBAA1852; -.
bat:BAS1716; -.
TIGR BA_1852; -.
GBAA1852; -.
Phylogenomic databases
HOGENOM Q81S27; -.
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   335  335     Ketol-acid reductoisomerase 2. PRO_0000151271
ACT_SITE   106   106        Potential. 
Sequence information
Length: 335 AA [This is the length of the unprocessed precursor] Molecular weight: 36918 Da [This is the MW of the unprocessed precursor] CRC64: EB73BC4965FF2003 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKTYYEQDAN VGLLQGKTVA VIGYGSQGHA QAQNLRDSGV EVVVGVRPGK SFEVAKADGF 

        70         80         90        100        110        120 
EVMSVSEAVR TAQVVQMLLP DEQQAHVYKA EVEENLREGQ MLLFSHGFNI HFGQINPPSY 

       130        140        150        160        170        180 
VDVAMVAPKS PGHLVRRVFQ EGNGVPALVA VHQDATGTAL HVALAYAKGV GCTRAGVIET 

       190        200        210        220        230        240 
TFQEETETDL FGEQAVLCGG VTALVKAGFE TLTEGGYRPE IAYFECLHEL KLIVDLMYEG 

       250        260        270        280        290        300 
GLTNMRHSIS DTAEFGDYVT GSRIVTDETK KEMKRVLTEI QQGEFAKKWI LENQAGRPTY 

       310        320        330 
NAMKKAEQNH QLEKVGEELR EMMSWIHAPK ELVKK 

Q81S27 in FASTA format

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