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UniProtKB/Swiss-Prot entry Q63JL2

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

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Entry information
Entry name LEU3_BURPS
Primary accession number Q63JL2
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 31)
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: BPSS1705
From
Burkholderia pseudomallei (Pseudomonas pseudomallei) [TaxID: 28450] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei group.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K96243;
DOI=10.1073/pnas.0403302101; PubMed=15377794 [NCBI, ExPASy, EBI, Israel, Japan]
Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
"Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei.";
Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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
BX571966; CAH39178.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_111710.1; -.
3D structure databases
ModBase Q63JL2.
Enzyme and pathway databases
BioCyc BPSE272560:BPSS1705-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 Q63JL2.
Genome annotation databases
GeneID 3094947; -.
GenomeReviews BX571966_GR; BPSS1705.
KEGG bps:BPSS1705; -.
Phylogenomic databases
HOGENOM Q63JL2; -.
Genome annotation databases
CMR Q63JL2; BPSS1705.
Other
ProtoNet Q63JL2.
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   355  355     3-isopropylmalate dehydrogenase. PRO_0000083674
NP_BIND   280   292  13     NAD (By similarity). 
METAL   222   222        Magnesium or manganese (By similarity). 
METAL   246   246        Magnesium or manganese (By similarity). 
METAL   250   250        Magnesium or manganese (By similarity). 
BINDING   90    90        Substrate (By similarity). 
BINDING   100   100        Substrate (By similarity). 
BINDING   128   128        Substrate (By similarity). 
BINDING   222   222        Substrate (By similarity). 
SITE   135   135  1     Important for catalysis (By similarity). 
SITE   190   190  1     Important for catalysis (By similarity). 
Sequence information
Length: 355 AA [This is the length of the unprocessed precursor] Molecular weight: 38187 Da [This is the MW of the unprocessed precursor] CRC64: 8BB994DF67538F7A [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKIAVLPGDG IGPEIVNEAV KVLNALDEKF ELEQAPVGGA GYEASGHPLP DATLALAKEA 

        70         80         90        100        110        120 
DAILFGAVGD WKYDSLERAL RPEQAILGLR KHLELFANFR PAICYPQLVD ASPLKPELVA 

       130        140        150        160        170        180 
GLDILIVREL NGDIYFGQPR GVRAAPDGPF AGAREGFDTM RYSEPEVRRI AHVAFQAARK 

       190        200        210        220        230        240 
RAKKLLSVDK SNVLETSQFW RDVMIDVSKE YADVELSHMY VDNAAMQLAK APKQFDVIVT 

       250        260        270        280        290        300 
GNMFGDILSD EASMLTGSIG MLPSASLDQR NKGLYEPSHG SAPDIAGKGI ANPLATILSA 

       310        320        330        340        350 
AMLLRYSLNR AEQADRIERA VKAVLEQGYR TGDIATPGCK QVGTAAMGDA VVAAL
Q63JL2 in FASTA format

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