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 P59027

[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 LEU3_BUCPS
Primary accession number P59027
Secondary accession numbers None
Integrated into Swiss-Prot on October 19, 2002
Sequence was last modified on October 19, 2002 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 39)
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
From
Buchnera aphidicola subsp. Pemphigus spyrothecae [TaxID: 98799] 
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1128/AEM.68.5.2572-2575.2002; PubMed=11976137 [NCBI, ExPASy, EBI, Israel, Japan]
Sabater-Munoz B., Gomez-Valero L., van Ham R.C.H.J., Silva F.J., Latorre A.;
"Molecular characterization of the leucine cluster in Buchnera sp. strain PSY, a primary endosymbiont of the aphid Pemphigus spyrothecae.";
Appl. Environ. Microbiol. 68:2572-2575(2002).
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
AJ426489; CAD20138.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP P30125; 1CM7. [HSSP ENTRY / PDB]
ModBase P59027.
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.
Other
ProtoNet P59027.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Cytoplasm; Leucine biosynthesis; Magnesium; Manganese; Metal-binding; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   363  363     3-isopropylmalate dehydrogenase. PRO_0000083659
NP_BIND   77    90  14     NAD (By similarity). 
NP_BIND   284   296  13     NAD (By similarity). 
METAL   226   226        Magnesium or manganese (By similarity). 
METAL   250   250        Magnesium or manganese (By similarity). 
METAL   254   254        Magnesium or manganese (By similarity). 
BINDING   98    98        Substrate (By similarity). 
BINDING   108   108        Substrate (By similarity). 
BINDING   137   137        Substrate (By similarity). 
BINDING   226   226        Substrate (By similarity). 
SITE   144   144  1     Important for catalysis (By similarity). 
SITE   194   194  1     Important for catalysis (By similarity). 
Sequence information
Length: 363 AA [This is the length of the unprocessed precursor] Molecular weight: 40550 Da [This is the MW of the unprocessed precursor] CRC64: 760AAA94425D6632 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTKIYNLAIL PGDGIGPELL QKDLNFKVLK EQYKLKINTT EYDIGGIAID KYGKALPKET 

        70         80         90        100        110        120 
LDGCKESDSI LFGSVGGPKW QHLPPDQQPE RAALLPIRKY FNLFSNLRPA KLYSTLNHLS 

       130        140        150        160        170        180 
PLRRDISEKG FDILCVRELT GGIYFGKPKG YIKNIIDKKA FDTEIYYASE IKRIAHIGFK 

       190        200        210        220        230        240 
LAQNRKYKIT SVDKANVLES SVLWRETVNT ISKEYPDVKL SHLYIDHAAM QIIKNPDKFD 

       250        260        270        280        290        300 
VILTSNLFGD ILSDECAMIT GSIGMLPSAS LNDSNFGLYE PAGGSAPDIA GKNIANPIAQ 

       310        320        330        340        350        360 
ILSIAMLVRY TMKLPMISDH IESAVIDTLK KGYRTLDIAN DKEKYVSTND IGDIISDILK 


KRI
P59027 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 au flag APAF Australia Mirror sites: Brazil Canada China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!