IDH1_CANTR
ID IDH1_CANTR Reviewed; 430 AA.
AC O13285;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Isocitrate dehydrogenase [NADP], mitochondrial;
DE Short=IDH;
DE EC=1.1.1.42;
DE AltName: Full=CtIDP1;
DE AltName: Full=IDP;
DE AltName: Full=NADP(+)-specific ICDH;
DE AltName: Full=Oxalosuccinate decarboxylase;
DE Flags: Precursor;
GN Name=IDP1;
OS Candida tropicalis (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5482;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 20336 / pK233 / NCYC 997;
RX PubMed=9325427; DOI=10.1007/s002030050513;
RA Imajo T., Kawachi H., Atomi H., Sanuki S., Yamamoto S., Ueda M., Tanaka A.;
RT "Immunochemically distinct NADP-linked isocitrate dehydrogenase isozymes in
RT mitochondria and peroxisomes of Candida tropicalis.";
RL Arch. Microbiol. 168:389-395(1997).
CC -!- FUNCTION: Mitochondrial IDP1 may regulate flux through the
CC tricarboxylic acid cycle and respiration. Its probably critical
CC function is the production of NADPH.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH;
CC Xref=Rhea:RHEA:19629, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.42;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB004556; BAA22945.1; -; Genomic_DNA.
DR AlphaFoldDB; O13285; -.
DR SMR; O13285; -.
DR PRIDE; O13285; -.
DR VEuPathDB; FungiDB:CTMYA2_016810; -.
DR VEuPathDB; FungiDB:CTRG_01521; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR GO; GO:0006102; P:isocitrate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004790; Isocitrate_DH_NADP.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR PANTHER; PTHR11822; PTHR11822; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR PIRSF; PIRSF000108; IDH_NADP; 1.
DR SMART; SM01329; Iso_dh; 1.
DR TIGRFAMs; TIGR00127; nadp_idh_euk; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 3: Inferred from homology;
KW Glyoxylate bypass; Magnesium; Manganese; Metal-binding; Mitochondrion;
KW NADP; Oxidoreductase; Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 28..430
FT /note="Isocitrate dehydrogenase [NADP], mitochondrial"
FT /id="PRO_0000014424"
FT BINDING 101..103
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 120..126
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 335..340
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 165
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT SITE 237
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 430 AA; 48009 MW; 205A319496F0CCEB CRC64;
MIRASAIQRT AMLLRQLRGF STSATLADKI KVKNPIVELD GDEMTRIIWQ KIKDQLILPY
LDVDLKYYDL GIESRDATDD QITIDAANAI KEYGVGVKCA TITPDEARVK EFHLKKMWLS
PNGTIRNILG GTVFRESIII PCIPRLIPGW EKPIVIGRHA FGDQYKATDL VINEPGRLEL
RFTPASGGEA QTQKVYDYTG PGVGLAMYNT DESITGFAHA SFKMALAKGL PLYMSTKNTI
LKKYDGRFKD IFQQIYEQDY AAEFEKQGLW YEHRLIDDMV AQMIKSKGGF VMALKNYDGD
VQSDIVAQGF GSLGLMTSAL MTPDGKAYEA EAAHGTVTRH YRQHQQGKET STNSIASIFA
WTRGLAQRGK LDETPDVVDF ASKLEQATID TVEVDRIMTK DLALAMGKTD RSAYVTTTEF
LDAVADRLKK
