Reviewed, UniProtKB/Swiss-Prot O13294 (IDH2_CANTR)

Names and origin

Protein names

Recommended 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

Organism

Candida tropicalis (Yeast)

Taxonomic identifier

5482 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	411 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Glyoxylate bypass Tricarboxylic acid cycle
Cellular component	Peroxisome
Ligand	Magnesium Manganese Metal-binding NADP
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	glyoxylate cycle Inferred from electronic annotation. Source: UniProtKB-KW isocitrate metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro isocitrate dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.1
	Chain	2 – 411	410	Isocitrate dehydrogenase [NADP] peroxisomal		PRO_0000083583
Regions
	Nucleotide binding	78 – 80	3	NADP By similarity
	Nucleotide binding	312 – 317	6	NADP By similarity
	Region	97 – 103	7	Substrate binding By similarity
Sites
	Metal binding	254	1	Magnesium or manganese By similarity
	Metal binding	277	1	Magnesium or manganese By similarity
	Binding site	80	1	Substrate By similarity
	Binding site	85	1	NADP By similarity
	Binding site	112	1	Substrate By similarity
	Binding site	135	1	Substrate By similarity
	Binding site	262	1	NADP By similarity
	Binding site	330	1	NADP; via amide nitrogen and carbonyl oxygen By similarity
	Site	142	1	Critical for catalysis By similarity
	Site	214	1	Critical for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	O13294-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 3E47A093C45F5915	FASTA	411	46,171
	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

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
SMR	O13294. Positions 6-409.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.1.1.42. 1242.
Family and domain databases
InterPro	IPR019818. IsoCit/isopropylmalate_DH_CS. IPR001804. Isocitrate/isopropylmalate_DH. IPR004790. Isocitrate_DH_NADP-dep_euk. [Graphical view]
Gene3D	G3DSA:3.40.718.10. IDH_IMDH. 1 hit.
PANTHER	PTHR11822. IDH_NADP_euk. 1 hit.
Pfam	PF00180. Iso_dh. 1 hit. [Graphical view]
PIRSF	PIRSF000108. IDH_NADP. 1 hit.
TIGRFAMs	TIGR00127. nadp_idh_euk. 1 hit.
PROSITE	PS00470. IDH_IMDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

IDH2_CANTR

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)