ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q47HR1


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name LEU31_DECAR
Primary accession number Q47HR1
Secondary accession numbers None
Integrated into Swiss-Prot on January 10, 2006
Sequence was last modified on September 13, 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 1
Synonyms EC 1.1.1.85
Beta-IPM dehydrogenase 1
IMDH 1
3-IPM-DH 1
Gene name
Name: leuB1
OrderedLocusNames: Daro_0864
From
Dechloromonas aromatica (strain RCB) [TaxID: 159087] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Rhodocyclaceae; Dechloromonas.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Trong S., Kellar K., Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.;
"Complete sequence of Dechloromonas aromatica RCB.";
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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
CP000089; AAZ45620.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_284090.1; -.
3D structure databases
ModBase Q47HR1.
Enzyme and pathway databases
BioCyc DARO159087:DARO_0864-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 Q47HR1.
Genome annotation databases
GeneID 3569851; -.
GenomeReviews CP000089_GR; Daro_0864.
KEGG dar:Daro_0864; -.
NMPDR fig|159087.4.peg.1183; -.
Phylogenomic databases
HOGENOM Q47HR1; -.
Genome annotation databases
CMR Q47HR1; Daro_0864.
Other
ProtoNet Q47HR1.
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   350  350     3-isopropylmalate dehydrogenase 1. PRO_0000083683
NP_BIND   70    83  14     NAD (By similarity). 
NP_BIND   275   287  13     NAD (By similarity). 
METAL   217   217        Magnesium or manganese (By similarity). 
METAL   241   241        Magnesium or manganese (By similarity). 
METAL   245   245        Magnesium or manganese (By similarity). 
BINDING   90    90        Substrate (By similarity). 
BINDING   100   100        Substrate (By similarity). 
BINDING   128   128        Substrate (By similarity). 
BINDING   217   217        Substrate (By similarity). 
SITE   135   135  1     Important for catalysis (By similarity). 
SITE   185   185  1     Important for catalysis (By similarity). 
Sequence information
Length: 350 AA [This is the length of the unprocessed precursor] Molecular weight: 38018 Da [This is the MW of the unprocessed precursor] CRC64: 71E1EABEEE4743A9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKICVLPGDG IGPEITAQAV RVLNSLDLKF EMEEALLGGG AVDATGNPYP EATQKLARAA 

        70         80         90        100        110        120 
DAVLLGAVGG PKWDSLPREQ RPERGLLGIR KDLNLFANLR PAILYPELAN ASTLKPEVVA 

       130        140        150        160        170        180 
GLDILIIREL TGDIYFGQPR GVREENGERV GFNTMVYSES EIRRIGHVAF QAAQKRDKRL 

       190        200        210        220        230        240 
CSVDKMNVLE CTQLWRDVMI EISRDYPDVE LSHMLVDNAA MQLVKAPKQF DVMVTGNMFG 

       250        260        270        280        290        300 
DILSDEASML TGSIGMLPSA SLDDKNKGLY EPSHGSAPDI AGKGVANPLA TILSAAMMLR 

       310        320        330        340        350 
YTFGLEEQAL RVENAVKKVL AQGYRTGDIY ERGTNKVGTR EMGDAVLAAL 

Q47HR1 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by kr flag YPRC Korea Mirror sites: Australia  Brazil  Canada  China  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!