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UniProtKB/Swiss-Prot entry Q7VY73


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

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Entry information
Entry name LEU3_BORPE
Primary accession number Q7VY73
Secondary accession numbers None
Integrated into Swiss-Prot on December 15, 2003
Sequence was last modified on October 1, 2003 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 37)
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: BP1483
From
Bordetella pertussis [TaxID: 520] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Alcaligenaceae; Bordetella.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
DOI=10.1038/ng1227; PubMed=12910271 [NCBI, ExPASy, EBI, Israel, Japan]
Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica.";
Nat. Genet. 35:32-40(2003).
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
BX640415; CAE41772.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_880220.1; -.
3D structure databases
ModBase Q7VY73.
Enzyme and pathway databases
BioCyc BPER257313:BP1483-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 Q7VY73.
Genome annotation databases
GeneID 2666599; -.
GenomeReviews BX470248_GR; BP1483.
KEGG bpe:BP1483; -.
NMPDR fig|257313.1.peg.1298; -.
Phylogenomic databases
HOGENOM Q7VY73; -.
Genome annotation databases
CMR Q7VY73; BP1483.
Other
ProtoNet Q7VY73.
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   358  358     3-isopropylmalate dehydrogenase. PRO_0000083651
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   92    92        Substrate (By similarity). 
BINDING   102   102        Substrate (By similarity). 
BINDING   130   130        Substrate (By similarity). 
BINDING   224   224        Substrate (By similarity). 
SITE   137   137  1     Important for catalysis (By similarity). 
SITE   192   192  1     Important for catalysis (By similarity). 
Sequence information
Length: 358 AA [This is the length of the unprocessed precursor] Molecular weight: 38557 Da [This is the MW of the unprocessed precursor] CRC64: 145DB5DBB951CEED [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTHQIAVLPG DGIGPEIVEQ AERVLKALDL PLELRQAPVG GAAFDQFEHP LPPATLELAQ 

        70         80         90        100        110        120 
GSHAVLFGAV GDWKYDTLPR EFRPEQAILG LRKALGLFAN LRPAILYPEL ASASSLKPEI 

       130        140        150        160        170        180 
VSGLDILIIR ELTGDIYFGT PRGVRTAADG AFAGEREGYD TMRYAESEVR RIARIGFESA 

       190        200        210        220        230        240 
RKRNKKLCSV DKANVLETSQ FWRDLVIEVS RDYLDVELSH MYVDNAAMQL VRNPRQFDVI 

       250        260        270        280        290        300 
VTGNLFGDIL SDEAAMLTGS IGMLPSASLN AAGQGLYEPS HGSAPDIAGQ GIANPLATIL 

       310        320        330        340        350 
SAAMLLRYSL NLAPQADRVE AAVRKVLADG LRTADIHEAG TTKVSTSQMG DAVLKALG 

Q7VY73 in FASTA format

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