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UniProtKB/Swiss-Prot entry P37253


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

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Entry information
Entry name ILVC_BACSU
Primary accession number P37253
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1994
Sequence was last modified on October 1, 1994 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 69)
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: BSU28290
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Vandeyar M.A., Vander Horn P.B., Rafael J.A., Grandoni J.A., Zahler S.A.;
"The ilv-leu operon of Bacillus subtilis: sequences of the ilvB, ilvN and ilvC genes, and the control of transcription.";
Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=8969504 [NCBI, ExPASy, EBI, Israel, Japan]
Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J., Emmerson P.T., Harwood C.R.;
"The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis chromosome containing genes responsible for stress responses, the utilization of plant cell walls and primary metabolism.";
Microbiology 142:3067-3078(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[4]
PROTEIN SEQUENCE OF 17-31.
STRAIN=168 / JH642;
PubMed=8755892 [NCBI, ExPASy, EBI, Israel, Japan]
Graumann P., Schroeder K., Schmid R., Marahiel M.A.;
"Cold shock stress-induced proteins in Bacillus subtilis.";
J. Bacteriol. 178:4611-4619(1996).
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
L03181; AAA22548.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z75208; CAA99563.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99118; CAB14789.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C69644; C69644.
RefSeq NP_390707.1; -.
3D structure databases
HSSP Q9HVA2; 1NP3. [HSSP ENTRY / PDB]
ModBase P37253.
Enzyme and pathway databases
BioCyc BSUB224308:BSU2825-MON; -.
Organism-specific databases
SubtiList BG10672; ilvC. [Micado]
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 P37253.
Genome annotation databases
GeneID 937475; -.
GenomeReviews AL009126_GR; BSU28290.
KEGG bsu:BSU28290; -.
NMPDR fig|224308.1.peg.2832; -.
Phylogenomic databases
HOGENOM P37253; -.
Genome annotation databases
CMR P37253; BSU28290.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Complete proteome; Direct protein sequencing; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   342  342     Ketol-acid reductoisomerase. PRO_0000151277
ACT_SITE   107   107        Potential. 
Sequence information
Length: 342 AA [This is the length of the unprocessed precursor] Molecular weight: 37458 Da [This is the MW of the unprocessed precursor] CRC64: D6FA741EB5E90CE9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVKVYYNGDI KENVLAGKTV AVIGYGSQGH AHALNLKESG VDVIVGVRQG KSFTQAQEDG 

        70         80         90        100        110        120 
HKVFSVKEAA AQAEIIMVLL PDEQQQKVYE AEIKDELTAG KSLVFAHGFN VHFHQIVPPA 

       130        140        150        160        170        180 
DVDVFLVAPK GPGHLVRRTY EQGAGVPALF AIYQDVTGEA RDKALAYAKG IGGARAGVLE 

       190        200        210        220        230        240 
TTFKEETETD LFGEQAVLCG GLSALVKAGF ETLTEAGYQP ELAYFECLHE LKLIVDLMYE 

       250        260        270        280        290        300 
EGLAGMRYSI SDTAQWGDFV SGPRVVDAKV KESMKEVLKD IQNGTFAKEW IVENQVNRPR 

       310        320        330        340 
FNAINASENE HQIEVVGRKL REMMPFVKQG KKKEAVVSVA QN 

P37253 in FASTA format

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View entry in raw text format (no links)
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