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UniProtKB/Swiss-Prot entry Q8FVF3

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

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Entry information
Entry name LEU3_BRUSU
Primary accession number Q8FVF3
Secondary accession numbers None
Integrated into Swiss-Prot on November 7, 2003
Sequence was last modified on March 1, 2003 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 41)
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: BRA0890
From
Brucella suis [TaxID: 29461] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Brucellaceae; Brucella.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=1330 / Biovar 1;
DOI=10.1073/pnas.192319099; PubMed=12271122 [NCBI, ExPASy, EBI, Israel, Japan]
Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts.";
Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
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
AE014292; AAN34062.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_700057.1; -.
3D structure databases
HSSP Q56268; 1A05. [HSSP ENTRY / PDB]
ModBase Q8FVF3.
Enzyme and pathway databases
BioCyc BSUI204722:BR_A0890-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:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145; Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009098; Biological process: leucine biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.
Genome annotation databases
GeneID 1165333; -.
GenomeReviews AE014292_GR; BRA0890.
KEGG bms:BRA0890; -.
NMPDR fig|204722.1.peg.2966; -.
TIGR BRA0890; -.
Phylogenomic databases
HOGENOM Q8FVF3; -.
Other
ProtoNet Q8FVF3.
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   370  370     3-isopropylmalate dehydrogenase. PRO_0000083654
NP_BIND   77    90  14     NAD (By similarity). 
NP_BIND   290   302  13     NAD (By similarity). 
METAL   226   226        Magnesium or manganese (By similarity). 
METAL   250   250        Magnesium or manganese (By similarity). 
METAL   254   254        Magnesium or manganese (By similarity). 
BINDING   97    97        Substrate (By similarity). 
BINDING   107   107        Substrate (By similarity). 
BINDING   135   135        Substrate (By similarity). 
BINDING   226   226        Substrate (By similarity). 
SITE   142   142  1     Important for catalysis (By similarity). 
SITE   193   193  1     Important for catalysis (By similarity). 
Sequence information
Length: 370 AA [This is the length of the unprocessed precursor] Molecular weight: 39756 Da [This is the MW of the unprocessed precursor] CRC64: F9E81A0B300537CB [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MASRKLLLLP GDGIGPEAMA EVRKVIAFLN SDLNLGFETE EGLVGGCAYD AHGQAISDAD 

        70         80         90        100        110        120 
MEKALAADAV LFGAVGGPKW DSVPYEVRPE AGLLRLRKDM QLYANLRPAI CYPALAHSSS 

       130        140        150        160        170        180 
LKPEVIEGLD ILILRELTGG VYFGEPKEII DLGNGQKRGI DTQVYDTYEI ERIADVAFEL 

       190        200        210        220        230        240 
ARTRRNKVTS MEKRNVMKSG VLWNQVVTAR HKEKHADVQL EHMLADAGGM QLVRWPKQFD 

       250        260        270        280        290        300 
VILTDNLFGD LLSDVAAMLT GSLGMLPSAS LGAADSKTGK RKALYEPVHG SAPDIAGKGI 

       310        320        330        340        350        360 
ANPIAMIASL AMCLRYSFGL VAEADRLEAA IAGVLDDGIR TADIWSEGNT KVGTTEMGDA 

       370 
ILAKFKALSA
Q8FVF3 in FASTA format

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