ID   IDHP_ASPNG              Reviewed;         498 AA.
AC   P79089;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   02-SEP-2026, entry version 113.
DE   RecName: Full=Isocitrate dehydrogenase [NADP], mitochondrial;
DE            Short=IDH;
DE            EC=1.1.1.42;
DE   AltName: Full=IDP;
DE   AltName: Full=NADP(+)-specific ICDH;
DE   AltName: Full=Oxalosuccinate decarboxylase;
DE   Flags: Precursor;
GN   Name=icdA;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=WU-2223L;
RX   PubMed=16233178; DOI=10.1263/jbb.93.136;
RA   Kirimura K., Yoda M., Kumagai M., Ishii Y., Kino K., Usami S.;
RT   "Cloning and expression of Aspergillus niger icdA gene encoding
RT   mitochondrial NADP+-specific isocitrate dehydrogenase.";
RL   J. Biosci. Bioeng. 93:136-144(2002).
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   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000305}.
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DR   EMBL; AB000262; BAA19074.1; -; Genomic_DNA.
DR   EMBL; AB000261; BAA19073.1; -; mRNA.
DR   AlphaFoldDB; P79089; -.
DR   SMR; P79089; -.
DR   VEuPathDB; FungiDB:An02g12430; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1175390; -.
DR   VEuPathDB; FungiDB:ATCC64974_52850; -.
DR   VEuPathDB; FungiDB:M747DRAFT_293674; -.
DR   eggNOG; KOG1526; Eukaryota.
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:0006102; P:isocitrate metabolic process; IEA:InterPro.
DR   GO; GO:0006739; P:NADP+ metabolic process; IEA:TreeGrafter.
DR   FunFam; 3.40.718.10:FF:000002; Isocitrate dehydrogenase [NADP]; 1.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR004790; Isocitrate_DH_NADP.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   NCBIfam; TIGR00127; nadp_idh_euk; 1.
DR   NCBIfam; NF006156; PRK08299.1; 1.
DR   PANTHER; PTHR11822:SF21; ISOCITRATE DEHYDROGENASE [NADP], MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11822; NADP-SPECIFIC ISOCITRATE DEHYDROGENASE; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   PIRSF; PIRSF000108; IDH_NADP; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   2: Evidence at transcript level;
KW   Glyoxylate bypass; Magnesium; Manganese; Metal-binding; Mitochondrion;
KW   NADP; Oxidoreductase; Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT   CHAIN           ?..498
FT                   /note="Isocitrate dehydrogenase [NADP], mitochondrial"
FT                   /id="PRO_0000014423"
FT   BINDING         164..166
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         183..189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         339
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         347
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         362
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         397..402
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         415
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            228
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            299
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   498 AA;  55559 MW;  60FAB99B0A315CF0 CRC64;
     MSSVRFSSAL ARRSFAVASP PLSAPLSSSA RRFLSSSSST ISSSSSSVST RSPRSLTSAS
     SLLSSRTASA RWTGLSSLNL TQSRTMATEI PKIKVKNPVV ELDGDEMTRI IWQEIREKLI
     LPYLDVDLKY YDLGLEYRDQ TDDQVTVEAA EAIKKYGVGV KCATITPDEA RVEEFKLKKM
     WLSPNGTIRN ILGGTVFREP IIIPAIPRLV PGWNKPIIIG RHAFGDQYRA TDRVIPGPGK
     LELVYTPVNG EPETVKVYDF QGGGIAQTQY NTDESIRGFA HASFQMALLK GLPLYMSTKN
     TILKRYDGRF KDIFQEIYES TYQKDFEAKN LWYEHRLIDD MVAQMIKSEG GFVMALKNYD
     GDVQSDIVAQ GFGSLGLMTS TLVTPTGEAF ESEAAHGTVT RHYREHQKGR ETSTNPIASI
     FAWTRGLIQR GKLDETPDVV TFAEELERAC IEVVNDEGIM TKDLALACGR KEREAWVTTR
     EYMAAVERRL KANLKSRL
//