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UniProtKB/Swiss-Prot entry Q63DX7

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

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Entry information
Entry name LEU3_BACCZ
Primary accession number Q63DX7
Secondary accession numbers None
Integrated into Swiss-Prot on January 10, 2006
Sequence was last modified on October 25, 2004 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 32)
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
OrderedLocusNames: BCE33L1286
From
Bacillus cereus (strain ZK / E33L) [TaxID: 288681] [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].
DOI=10.1128/JB.188.9.3382-3390.2006; PubMed=16621833 [NCBI, ExPASy, EBI, Israel, Japan]
Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P.;
"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis.";
J. Bacteriol. 188:3382-3390(2006).
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
CP000001; AAU18962.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_082885.1; -.
3D structure databases
ModBase Q63DX7.
Enzyme and pathway databases
BioCyc BCER288681:BCE33L1286-MON; -.
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 Q63DX7.
Genome annotation databases
GeneID 3022955; -.
GenomeReviews CP000001_GR; BCE33L1286.
KEGG bcz:BCZK1286; -.
Phylogenomic databases
HOGENOM Q63DX7; -.
Genome annotation databases
CMR Q63DX7; BCE33L1286.
Other
ProtoNet Q63DX7.
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   354  354     3-isopropylmalate dehydrogenase. PRO_0000083636
NP_BIND   76    87  12     NAD (By similarity). 
NP_BIND   273   285  13     NAD (By similarity). 
METAL   215   215        Magnesium or manganese (By similarity). 
METAL   239   239        Magnesium or manganese (By similarity). 
METAL   243   243        Magnesium or manganese (By similarity). 
BINDING   94    94        Substrate (By similarity). 
BINDING   104   104        Substrate (By similarity). 
BINDING   130   130        Substrate (By similarity). 
BINDING   215   215        Substrate (By similarity). 
SITE   137   137  1     Important for catalysis (By similarity). 
SITE   183   183  1     Important for catalysis (By similarity). 
Sequence information
Length: 354 AA [This is the length of the unprocessed precursor] Molecular weight: 38493 Da [This is the MW of the unprocessed precursor] CRC64: 67E055F07ED68F45 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MEKRIVCLAG DGVGPEVMES AKEVLHMVER LYGHHFHLQD EHFGGVAIDL TGQPLPQRTL 

        70         80         90        100        110        120 
AACLASDAVL LGAVGGPRWD GAKERPEKGL LALRKGLGVF ANVRPVTVES ETAHLSPLKK 

       130        140        150        160        170        180 
ADEIDFVVVR ELTGGIYFSY PKERTDEVAT DTLTYHRHEI ERIVSYAFQL ASKRKKKVTS 

       190        200        210        220        230        240 
IDKANVLESS KLWRTVTEEV ALRYPDVELE HILVDAAAME LIRNPGRFDV IVTENLFGDI 

       250        260        270        280        290        300 
LSDEASVLAG SLGMLPSASH AEKGPSLYEP IHGSAPDIAG KNKANPIAMM RSVAMMLGQS 

       310        320        330        340        350 
FGLTREGCAI EEAISAVLKS GKCTEDIGGT ETTTSFTKAV MQEMEEQALV GRGR
Q63DX7 in FASTA format

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