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UniProtKB/Swiss-Prot entry Q3AEQ2

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

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Entry information
Entry name LEU3_CARHZ
Primary accession number Q3AEQ2
Secondary accession numbers None
Integrated into Swiss-Prot on September 19, 2006
Sequence was last modified on November 22, 2005 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 24)
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: CHY_0524
From
Carboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008) [TaxID: 246194] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; Thermoanaerobacteraceae; Carboxydothermus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1371/journal.pgen.0010065; PubMed=16311624 [NCBI, ExPASy, EBI, Israel, Japan]
Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J., Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J., Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.;
"Life in hot carbon monoxide: the complete genome sequence of Carboxydothermus hydrogenoformans Z-2901.";
PLoS Genet. 1:563-574(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
CP000141; ABB15752.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_359382.1; -.
3D structure databases
ModBase Q3AEQ2.
Enzyme and pathway databases
BioCyc CHYD246194:CHY_0524-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 Q3AEQ2.
Genome annotation databases
GeneID 3727861; -.
GenomeReviews CP000141_GR; CHY_0524.
KEGG chy:CHY_0524; -.
NMPDR fig|246194.3.peg.1091; -.
TIGR CHY_0524; -.
Phylogenomic databases
HOGENOM Q3AEQ2; -.
Other
ProtoNet Q3AEQ2.
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   374  374     3-isopropylmalate dehydrogenase. PRO_0000250110
NP_BIND   83    96  14     NAD (By similarity). 
NP_BIND   288   300  13     NAD (By similarity). 
METAL   231   231        Magnesium or manganese (By similarity). 
METAL   255   255        Magnesium or manganese (By similarity). 
METAL   259   259        Magnesium or manganese (By similarity). 
BINDING   104   104        Substrate (By similarity). 
BINDING   114   114        Substrate (By similarity). 
BINDING   142   142        Substrate (By similarity). 
BINDING   231   231        Substrate (By similarity). 
SITE   149   149  1     Important for catalysis (By similarity). 
SITE   199   199  1     Important for catalysis (By similarity). 
Sequence information
Length: 374 AA [This is the length of the unprocessed precursor] Molecular weight: 40975 Da [This is the MW of the unprocessed precursor] CRC64: FBA85D58E1DE8446 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSGRSCKGPF KILVLPGDGI GPEIIKEAVK VLKALGEKKG ITFNFQYGLI GGAAIDERGV 

        70         80         90        100        110        120 
PLPEETVELG KQCDAILLGA VGGPKWDNLP PEIRPELGGL LKIRKVFDLY ANLRPVMFFP 

       130        140        150        160        170        180 
ELKNASPLKP DIIEGVDILM VRELTGGLYF GEKKRFTTEQ GEQAVIDTLI YTEKEVERVV 

       190        200        210        220        230        240 
RLGFELAQKR RGKLTLVDKA NVLESSRFWR EITGEIKKEY PDVELSYMYV DNCAMQLIRN 

       250        260        270        280        290        300 
PRQFDVIVTE NMFGDILTDE GSVLAGSIGL LPSASLNGKF GLYEPIHGSA PDIAGQNKAN 

       310        320        330        340        350        360 
PLATILSAGM MLRYSLDCPE EALLIEKAVK AVLQKGYRTG DILEPGTTLV TCEEMGDLVA 

       370 
EEILGGVYDE GLPL
Q3AEQ2 in FASTA format

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