Reviewed, UniProtKB/Swiss-Prot O13285 (IDH1_CANTR)

Names and origin

Protein names

Recommended name:
    Isocitrate dehydrogenase [NADP], mitochondrial
      Short name=IDH
    EC=1.1.1.42
Alternative name(s):
    Oxalosuccinate decarboxylase
    NADP(+)-specific ICDH
    IDP
    CtIDP1

Gene names

Name:

IDP1

Organism

Candida tropicalis (Yeast)

Taxonomic identifier

5482 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	430 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Mitochondrial IDP1 may regulate flux through the tricarboxylic acid cycle and respiration. Its probably critical function is the production of NADPH.
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.
Subunit structure	Homodimer By similarity.
Subcellular location	Mitochondrion.
Sequence similarities	Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Ontologies

Keywords
Biological process	Glyoxylate bypass Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Magnesium Manganese Metal-binding NADP
Molecular function	Oxidoreductase
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	mitochondrion 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
	Transit peptide	1 – 27	27	Mitochondrion By similarity
	Chain	28 – 430	403	Isocitrate dehydrogenase [NADP], mitochondrial		PRO_0000014424
Regions
	Nucleotide binding	101 – 103	3	NADP By similarity
	Nucleotide binding	335 – 340	6	NADP By similarity
	Region	120 – 126	7	Substrate binding By similarity
Sites
	Metal binding	277	1	Magnesium or manganese By similarity
	Metal binding	300	1	Magnesium or manganese By similarity
	Binding site	103	1	Substrate By similarity
	Binding site	108	1	NADP By similarity
	Binding site	135	1	Substrate By similarity
	Binding site	158	1	Substrate By similarity
	Binding site	285	1	NADP By similarity
	Binding site	353	1	NADP; via amide nitrogen and carbonyl oxygen By similarity
	Site	165	1	Critical for catalysis By similarity
	Site	237	1	Critical for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	O13285-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 205A319496F0CCEB	FASTA	430	48,009
	10 20 30 40 50 60 MIRASAIQRT AMLLRQLRGF STSATLADKI KVKNPIVELD GDEMTRIIWQ KIKDQLILPY 70 80 90 100 110 120 LDVDLKYYDL GIESRDATDD QITIDAANAI KEYGVGVKCA TITPDEARVK EFHLKKMWLS 130 140 150 160 170 180 PNGTIRNILG GTVFRESIII PCIPRLIPGW EKPIVIGRHA FGDQYKATDL VINEPGRLEL 190 200 210 220 230 240 RFTPASGGEA QTQKVYDYTG PGVGLAMYNT DESITGFAHA SFKMALAKGL PLYMSTKNTI 250 260 270 280 290 300 LKKYDGRFKD IFQQIYEQDY AAEFEKQGLW YEHRLIDDMV AQMIKSKGGF VMALKNYDGD 310 320 330 340 350 360 VQSDIVAQGF GSLGLMTSAL MTPDGKAYEA EAAHGTVTRH YRQHQQGKET STNSIASIFA 370 380 390 400 410 420 WTRGLAQRGK LDETPDVVDF ASKLEQATID TVEVDRIMTK DLALAMGKTD RSAYVTTTEF 430 LDAVADRLKK

References

[1]

"Immunochemically distinct NADP-linked isocitrate dehydrogenase isozymes in mitochondria and peroxisomes of Candida tropicalis." Imajo T., Kawachi H., Atomi H., Sanuki S., Yamamoto S., Ueda M., Tanaka A. Arch. Microbiol. 168:389-395(1997) [PubMed: 9325427] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 20336 / pK233 / NCYC 997.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB004556 Genomic DNA. Translation: BAA22945.1.
3D structure databases
HSSP	HSSP built from PDB template 1LWD based on UniProtKB P33198.
SMR	O13285. Positions 29-430.
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

IDH1_CANTR

Accession

Primary (citable) accession number: O13285

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)