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UniProtKB/Swiss-Prot entry O13294

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

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Entry information
Entry name IDH2_CANTR
Primary accession number O13294
Secondary accession numbers None
Integrated into Swiss-Prot on January 17, 2003
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 47)
Name and origin of the protein
Protein name Isocitrate dehydrogenase [NADP] peroxisomal
Synonyms IDH
EC 1.1.1.42
Oxalosuccinate decarboxylase
PS-NADP-IDH
CtIDP2
Gene name
Name: IDP2
From
Candida tropicalis (Yeast) [TaxID: 5482] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales; Candida.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-16.
STRAIN=ATCC 20336 / pK233 / NCYC 997;
PubMed=9432010 [NCBI, ExPASy, EBI, Israel, Japan]
Kawachi H., Shimizu K., Atomi H., Sanuki S., Ueda M., Tanaka A.;
"Gene analysis of an NADP-linked isocitrate dehydrogenase localized in peroxisomes of the n-alkane-assimilating yeast Candida tropicalis.";
Eur. J. Biochem. 250:205-211(1997).
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
AB007994; BAA22846.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP P33198; 1LWD. [HSSP ENTRY / PDB]
ModBase O13294.
Ontologies
GO
GO:0005777; Cellular component: peroxisome (inferred from electronic annotation from UniProtKB-KW).
GO:0004450; Molecular function: isocitrate dehydrogenase (NADP+) activity (inferred from electronic annotation from InterPro).
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:0006097; Biological process: glyoxylate cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0006102; Biological process: isocitrate metabolic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006099; Biological process: tricarboxylic acid cycle (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR004790; IsoCit_DHase_NADP-dep_euk.
IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.718.10; IDH_IMDH; 1.
PANTHER PTHR11822; IDH_NADP_euk; 1.
Pfam PF00180; Iso_dh; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000108; IDH_NADP; 1.
TIGRFAMs TIGR00127; nadp_idh_euk; 1.
PROSITE PS00470; IDH_IMDH; 1.
Other
ProtoNet O13294.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Direct protein sequencing; Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP; Oxidoreductase; Peroxisome; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   411  410     Isocitrate dehydrogenase [NADP] peroxisomal. PRO_0000083583
NP_BIND   78    80  3     NADP (By similarity). 
NP_BIND   312   317  6     NADP (By similarity). 
REGION   97   103  7     Substrate binding (By similarity). 
METAL   254   254        Magnesium or manganese (By similarity). 
METAL   277   277        Magnesium or manganese (By similarity). 
BINDING   80    80        Substrate (By similarity). 
BINDING   85    85        NADP (By similarity). 
BINDING   112   112        Substrate (By similarity). 
BINDING   135   135        Substrate (By similarity). 
BINDING   262   262        NADP (By similarity). 
BINDING   330   330        NADP; via amide nitrogen and carbonyl oxygen (By similarity). 
SITE   142   142  1     Critical for catalysis (By similarity). 
SITE   214   214  1     Critical for catalysis (By similarity). 
Sequence information
Length: 411 AA [This is the length of the unprocessed precursor] Molecular weight: 46171 Da [This is the MW of the unprocessed precursor] CRC64: 3E47A093C45F5915 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MGEIQKITVK NPIVEMDGDE MTRIIWQFIK DKLILPYLNV DLKYYDLGIE YRDKTDDKVT 

        70         80         90        100        110        120 
TDAAEAILQY GVGVKCATIT PDEARVKEFN LKKMWLSPNG TLRNVIGGTV FREPIVIDNI 

       130        140        150        160        170        180 
PRIVPSWEKP IIIGRHAFGD QYKATDVVIP AAGDLKLVFK PKDGGEVQEF PVYQFDGPGV 

       190        200        210        220        230        240 
ALSMYNTDAS ITDFAESSFQ LAIERKLNLF SSTKNTILKK YDGKFKDIFE GLYASKYKTK 

       250        260        270        280        290        300 
MDELGIWYEH RLIDDMVAQM LKSKGGYIIA MKNYDGDVQS DIVAQGFGSL GLMTSVLVTP 

       310        320        330        340        350        360 
DGKAFESEAA HGTVTRHYRQ HQQGKETSTN SIASIYAWTR GLIQRGKLDD TPEVVKFAEE 

       370        380        390        400        410 
LEKAVIETVS KDNIMTKDLA LTQGKTDRSS YVTTEEFIDG VANRLNKNLG Y
O13294 in FASTA format

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