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UniProtKB/Swiss-Prot entry Q6FEV6

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

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Entry information
Entry name LEU3_ACIAD
Primary accession number Q6FEV6
Secondary accession numbers None
Integrated into Swiss-Prot on January 10, 2006
Sequence was last modified on July 19, 2004 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 33)
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: ACIAD0469
From
Acinetobacter sp. (strain ADP1) [TaxID: 62977] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Moraxellaceae; Acinetobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/nar/gkh910; PubMed=15514110 [NCBI, ExPASy, EBI, Israel, Japan]
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium.";
Nucleic Acids Res. 32:5766-5779(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
CR543861; CAG67402.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_045224.1; -.
3D structure databases
ModBase Q6FEV6.
Enzyme and pathway databases
BioCyc ASP62977:ACIAD0469-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 Q6FEV6.
Genome annotation databases
GeneID 2880113; -.
GenomeReviews CR543861_GR; ACIAD0469.
KEGG aci:ACIAD0469; -.
NMPDR fig|62977.3.peg.1122; -.
Phylogenomic databases
HOGENOM Q6FEV6; -.
Genome annotation databases
CMR Q6FEV6; ACIAD0469.
Other
ProtoNet Q6FEV6.
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   359  359     3-isopropylmalate dehydrogenase. PRO_0000083626
NP_BIND   76    89  14     NAD (By similarity). 
NP_BIND   283   295  13     NAD (By similarity). 
METAL   225   225        Magnesium or manganese (By similarity). 
METAL   249   249        Magnesium or manganese (By similarity). 
METAL   253   253        Magnesium or manganese (By similarity). 
BINDING   96    96        Substrate (By similarity). 
BINDING   106   106        Substrate (By similarity). 
BINDING   134   134        Substrate (By similarity). 
BINDING   225   225        Substrate (By similarity). 
SITE   141   141  1     Important for catalysis (By similarity). 
SITE   192   192  1     Important for catalysis (By similarity). 
Sequence information
Length: 359 AA [This is the length of the unprocessed precursor] Molecular weight: 38544 Da [This is the MW of the unprocessed precursor] CRC64: 8C8A50F44C9A791B [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSKQILILAG DGIGPEIVGA AEQVLTKVNE KFELGLTWEH GLLGGSAIDA HGEPYPAVTS 

        70         80         90        100        110        120 
EQAKKADAIL LGAVGGPKWD TIERSIRPER GLLKIRSELN LFANLRPALL YPQLADASSL 

       130        140        150        160        170        180 
KPEIVAGLDI LIVRELTGGI YFGQPRGIRE LENGEKQGYN TDVYSESEIK RIAKVAFELA 

       190        200        210        220        230        240 
ALRGSKVCSV DKANVLEVTE LWKQTVTELQ QAQYPNIQLS HMYVDNAAMQ LVRAPKQFDV 

       250        260        270        280        290        300 
IVTGNLFGDI LSDEAAMLTG SIGMLPSASL DENGKGMYEP CHGSAPDIAG QNVANPLATI 

       310        320        330        340        350 
LSVAMMLRYT FREEAAAKAI EDAVGQVLDQ GLRTADIMSE GMQRVGTVEM GQAVVAALA
Q6FEV6 in FASTA format

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