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Reviewed, UniProtKB/Swiss-Prot O13294 (IDH2_CANTR)

Last modified February 9, 2010. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Isocitrate dehydrogenase [NADP] peroxisomal
      Short name=IDH
    EC=1.1.1.42
Alternative name(s):
    Oxalosuccinate decarboxylase
    PS-NADP-IDH
    CtIDP2
Gene names
Name: IDP2
OrganismCandida tropicalis (Yeast)
Taxonomic identifier5482 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length411 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

May play a role in N-alkane metabolism, glutamate synthesis, and/or NADPH generation in the peroxisomes.

Catalytic activity

Isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH.

Oxalosuccinate + NADP+ = 2-oxoglutarate + CO2 + NADPH.

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity.

Subcellular location

Peroxisome.

Induction

By N-alkanes.

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 411410Isocitrate dehydrogenase [NADP] peroxisomal
PRO_0000083583

Regions

Nucleotide binding78 – 803NADP By similarity
Nucleotide binding312 – 3176NADP By similarity
Region97 – 1037Substrate binding By similarity

Sites

Metal binding2541Magnesium or manganese By similarity
Metal binding2771Magnesium or manganese By similarity
Binding site801Substrate By similarity
Binding site851NADP By similarity
Binding site1121Substrate By similarity
Binding site1351Substrate By similarity
Binding site2621NADP By similarity
Binding site3301NADP; via amide nitrogen and carbonyl oxygen By similarity
Site1421Critical for catalysis By similarity
Site2141Critical for catalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
O13294-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 3E47A093C45F5915

FASTA41146,171
        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 

« Hide

References

[1]"Gene analysis of an NADP-linked isocitrate dehydrogenase localized in peroxisomes of the n-alkane-assimilating yeast Candida tropicalis."
Kawachi H., Shimizu K., Atomi H., Sanuki S., Ueda M., Tanaka A.
Eur. J. Biochem. 250:205-211(1997) [PubMed: 9432010] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-16.
Strain: ATCC 20336 / pK233 / NCYC 997.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB007994 Genomic DNA. Translation: BAA22846.1.

3D structure databases

SMRO13294. Positions 6-409.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.1.1.42. 1242.

Family and domain databases

InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR004790. Isocitrate_DH_NADP-dep_euk.
[Graphical view]
Gene3DG3DSA:3.40.718.10. IDH_IMDH. 1 hit.
PANTHERPTHR11822. IDH_NADP_euk. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000108. IDH_NADP. 1 hit.
TIGRFAMsTIGR00127. nadp_idh_euk. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIDH2_CANTR
AccessionPrimary (citable) accession number: O13294
Entry history
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: January 23, 2007
Last modified: February 9, 2010
This is version 54 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents