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UniProtKB/Swiss-Prot entry P05645


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

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Entry information
Entry name LEU3_BACSU
Primary accession number P05645
Secondary accession number P94566
Integrated into Swiss-Prot on November 1, 1988
Sequence was last modified on May 30, 2000 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 77)
Name and origin of the protein
Protein name 3-isopropylmalate dehydrogenase
Synonyms EC 1.1.1.85
Beta-IPM dehydrogenase
IMDH
3-IPM-DH
Gene name
Name: leuB
Synonyms: leuC
OrderedLocusNames: BSU28270
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
DOI=10.1093/nar/15.12.4988; PubMed=3110742 [NCBI, ExPASy, EBI, Israel, Japan]
Imai R., Sekiguchi T., Nosoh Y., Tsuda K.;
"The nucleotide sequence of 3-isopropylmalate dehydrogenase gene from Bacillus subtilis.";
Nucleic Acids Res. 15:4988-4988(1987).
[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).
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
Y00353; CAA68432.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z75208; CAA99532.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99118; CAB14787.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A26522; A26522.
RefSeq NP_390705.1; -.
3D structure databases
HSSP P12010; 2AYQ. [HSSP ENTRY / PDB]
ModBase P05645.
Enzyme and pathway databases
BioCyc BSUB224308:BSU2823-MON; -.
Organism-specific databases
SubtiList BG10675; leuB. [Micado]
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0003862; Molecular function: 3-isopropylmalate dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0009098; Biological process: leucine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01033; -; 1.
PBIL [Tree]
InterPro IPR004429; 3-isopropylmalate_DHase.
IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.718.10; IDH_IMDH; 1.
PANTHER PTHR11835; IDH_IMDH_dimeric; 1.
PTHR11835:SF13; IPMDH; 1.
Pfam PF00180; Iso_dh; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00169; leuB; 1.
PROSITE PS00470; IDH_IMDH; 1.
BLOCKS P05645.
Genome annotation databases
GeneID 936221; -.
GenomeReviews AL009126_GR; BSU28270.
KEGG bsu:BSU28270; -.
NMPDR fig|224308.1.peg.2830; -.
Phylogenomic databases
HOGENOM P05645; -.
Genome annotation databases
CMR P05645; BSU28270.
Other
ProtoNet P05645.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Complete proteome; Cytoplasm; Leucine biosynthesis; Magnesium; Manganese; Metal-binding; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   365  365     3-isopropylmalate dehydrogenase. PRO_0000083642
NP_BIND   76    89  14     NAD (By similarity). 
NP_BIND   282   294  13     NAD (By similarity). 
METAL   224   224        Magnesium or manganese (By similarity). 
METAL   248   248        Magnesium or manganese (By similarity). 
METAL   252   252        Magnesium or manganese (By similarity). 
BINDING   96    96        Substrate (By similarity). 
BINDING   106   106        Substrate (By similarity). 
BINDING   134   134        Substrate (By similarity). 
BINDING   224   224        Substrate (By similarity). 
SITE   141   141  1     Important for catalysis (By similarity). 
SITE   192   192  1     Important for catalysis (By similarity). 
CONFLICT   182   182        A -> T (in Ref. 1; CAA68432). 
Sequence information
Length: 365 AA [This is the length of the unprocessed precursor] Molecular weight: 39945 Da [This is the MW of the unprocessed precursor] CRC64: 379A03A082C47EC3 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKKRIALLPG DGIGPEVLES ATDVLKSVAE RFNHEFEFEY GLIGGAAIDE HHNPLPEETV 

        70         80         90        100        110        120 
AACKNADAIL LGAVGGPKWD QNLSELRPEK GLLSIRKQLD LFANLRPVKV FESLSDRSPL 

       130        140        150        160        170        180 
KKEYIDNVDF VIVRELTGGL YFGQPSKRYV NTEGEQEAVD TLFYKRTEIE RVIREGFKMA 

       190        200        210        220        230        240 
AARKGKVTSV DKANVLESSR LWREVAEDVA QEFPDVKLEH MLVDNAAMQL IYAPNQFDVV 

       250        260        270        280        290        300 
VTENMFGDIL SDEASMLTGS LGMLPSASLS SSGLHLFEPV HGSAPDIAGK GMANPFAAIL 

       310        320        330        340        350        360 
SAAMLLRTSF GLEEEAKAVE DAVNKVLASG KRTRDLARSE EFSSTQAITE EVKAAIMSEN 


TISNV 

P05645 in FASTA format

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