ID   IDH_CALNO               Reviewed;         429 AA.
AC   P96318;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 2.
DT   28-JUN-2023, entry version 96.
DE   RecName: Full=Isocitrate dehydrogenase [NADP];
DE            Short=IDH;
DE            EC=1.1.1.42;
DE   AltName: Full=IDP;
DE   AltName: Full=NADP(+)-specific ICDH;
DE   AltName: Full=Oxalosuccinate decarboxylase;
GN   Name=icd;
OS   Caldococcus noboribetus.
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Caldococcus.
OX   NCBI_TaxID=57174;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NC12;
RX   PubMed=8951037; DOI=10.1006/abbi.1996.0534;
RA   Aoshima M., Yamagishi A., Oshima T.;
RT   "Eubacteria-type isocitrate dehydrogenase from an Archaeon: cloning,
RT   sequencing, and expression of a gene encoding isocitrate dehydrogenase from
RT   a hyperthermophilic archaebacterium Caldococcus noboribetus.";
RL   Arch. Biochem. Biophys. 336:77-85(1996).
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is 98 degrees Celsius. Thermostable.;
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; D86855; BAA13177.2; -; Genomic_DNA.
DR   PIR; T44658; T44658.
DR   AlphaFoldDB; P96318; -.
DR   SMR; P96318; -.
DR   BRENDA; 1.1.1.42; 1058.
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:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR004439; Isocitrate_DH_NADP_dimer_prok.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   PANTHER; PTHR43504; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR   PANTHER; PTHR43504:SF1; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   1: Evidence at protein level;
KW   Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP;
KW   Oxidoreductase; Phosphoprotein; Tricarboxylic acid cycle.
FT   CHAIN           1..429
FT                   /note="Isocitrate dehydrogenase [NADP]"
FT                   /id="PRO_0000083573"
FT   BINDING         108
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         308
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P08200"
FT   BINDING         340..346
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   BINDING         393
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         397
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            163
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            230
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         117
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   429 AA;  47620 MW;  F06A559FCAA1C42B CRC64;
     MVSHPCTADE AKPPSEGQLA RFENGKLIVP DNLIVAYFKG DGIGPEIVES AKKVLDAAVD
     KAYGGTRRIV WWEVTAGEEA QKECGSLLPD GTLQAFKLAR VNLKGPLTTP VGGGFRSLNV
     TLRMVLDLYS NVRPVKWYGQ PTPHCHPENI DWVIFRENTE DVYAGIEWPF DSPEAQKIRD
     FLKKEFGIEL TPDTGIGIKP ISKWRTQRHV RRAMEWAIRN GYKHVTIMHK GNIMKYTEGA
     FRQWAYDLIL SEFRDYVVTE EEVNTKYGGK APEGKIIVND RIADNMLQQI ITRPGEYNVI
     VTPNLNGDYI SDEANALVGG IGMAAGLDMG DGIAVAEPVH GSAPKYAGKN VINPTAEILS
     GMYLLSDFVG WPEVKLLVEY AVKQAIAHKQ VTYDLAREMG GVTPISTTEY TDVLVDYIRH
     ADLKALKGQ
//