IDHP_ASPNG
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 03-AUG-2022, entry version 100.
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;
OC Aspergillus subgen. 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 STRING; 5061.CADANGAP00002693; -.
DR PRIDE; 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: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 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
