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UniProtKB/Swiss-Prot entry Q5HS77

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

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Entry information
Entry name LEU3_CAMJR
Primary accession number Q5HS77
Secondary accession numbers None
Integrated into Swiss-Prot on January 10, 2006
Sequence was last modified on February 15, 2005 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 28)
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: CJE1888
From
Campylobacter jejuni (strain RM1221) [TaxID: 195099] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; Campylobacteraceae; Campylobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1371/journal.pbio.0030015; PubMed=15660156 [NCBI, ExPASy, EBI, Israel, Japan]
Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M., Nelson K.E.;
"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species.";
PLoS Biol. 3:72-85(2005).
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
CP000025; AAW34488.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_179858.1; -.
3D structure databases
ModBase Q5HS77.
Enzyme and pathway databases
BioCyc CJEJ195099:CJE_1888-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.
ProtoNet Q5HS77.
Genome annotation databases
GeneID 3230647; -.
GenomeReviews CP000025_GR; CJE1888.
KEGG cjr:CJE1888; -.
NMPDR fig|195099.3.peg.1828; -.
TIGR CJE1888; -.
Phylogenomic databases
HOGENOM Q5HS77; -.
Other
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_0000083676
NP_BIND   77    90  14     NAD (By similarity). 
NP_BIND   279   291  13     NAD (By similarity). 
METAL   221   221        Magnesium or manganese (By similarity). 
METAL   245   245        Magnesium or manganese (By similarity). 
METAL   249   249        Magnesium or manganese (By similarity). 
BINDING   98    98        Substrate (By similarity). 
BINDING   108   108        Substrate (By similarity). 
BINDING   137   137        Substrate (By similarity). 
BINDING   221   221        Substrate (By similarity). 
SITE   144   144  1     Important for catalysis (By similarity). 
SITE   189   189  1     Important for catalysis (By similarity). 
Sequence information
Length: 358 AA [This is the length of the unprocessed precursor] Molecular weight: 39362 Da [This is the MW of the unprocessed precursor] CRC64: 037F612953AA7A8A [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKAYKVAVLA GDGIGPLVMK EALKILTFIS QKYNFSFEFN EAKIGGASID AYGVALSDET 

        70         80         90        100        110        120 
LKLCEQSDAI LFGSVGGPKW DNLPIDQRPE RASLLPLRKH FNLFANLRPC KIYESLTHAS 

       130        140        150        160        170        180 
PLKNEIIQKG VDILCVRELT GGIYFGKQDL GKESAYDTEI YTKKEIERIA HIAFESARIR 

       190        200        210        220        230        240 
KKKVHLIDKA NVLASSILWR EVVANVVKDY QDINLEYMYV DNAAMQIVKN PSIFDVMLCS 

       250        260        270        280        290        300 
NLFGDILSDE LAAINGSLGL LSSASLNDKG FGLYEPAGGS APDIAHLNIA NPIAQILSAA 

       310        320        330        340        350 
LMLKYSFKEE QAAQDIENAI SLALAQGKMT KDLNAKSYLN TDEMGDCILE ILKENNNG
Q5HS77 in FASTA format

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