ID   IDH_AQUAE               Reviewed;         426 AA.
AC   O67480;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 125.
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; OrderedLocusNames=aq_1512;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000305}.
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DR   EMBL; AE000657; AAC07444.1; -; Genomic_DNA.
DR   PIR; F70431; F70431.
DR   RefSeq; NP_214045.1; NC_000918.1.
DR   RefSeq; WP_010880983.1; NC_000918.1.
DR   AlphaFoldDB; O67480; -.
DR   SMR; O67480; -.
DR   STRING; 224324.aq_1512; -.
DR   EnsemblBacteria; AAC07444; AAC07444; aq_1512.
DR   KEGG; aae:aq_1512; -.
DR   PATRIC; fig|224324.8.peg.1180; -.
DR   eggNOG; COG0538; Bacteria.
DR   HOGENOM; CLU_031953_7_1_0; -.
DR   InParanoid; O67480; -.
DR   OrthoDB; 9806254at2; -.
DR   Proteomes; UP000000798; Chromosome.
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   3: Inferred from homology;
KW   Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP;
KW   Oxidoreductase; Phosphoprotein; Reference proteome;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..426
FT                   /note="Isocitrate dehydrogenase [NADP]"
FT                   /id="PRO_0000083548"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         312
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   SITE            169
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            239
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         123
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   426 AA;  46925 MW;  06E47E36D844432A CRC64;
     MNKTTFENVY YWEGKAQIPQ EGQFIKLKED KTLEVPDNPI IPFIEGDGIG PEITQAMLLI
     INTAVEKTYN GSKKIYWVEL LAGDKAEEKT GERLPQETLD VLKESIVGIK GPLGTPVGKG
     VRSINSALRR AFDYYSAVRP VYWMGQATPI PNPERVDLVV FRENTDDVYA GVEFFAGTPE
     AKKVREFLIK EMGAKEEGFP EDVGITVKPM SEFKTKRHVR KALRYALENN KKNVAVIGKG
     NIMKATEGAF INWAFEVAEE PEFKGKVVTD PEAEPGEGQV KLTKVITDQM LMQLVLKPEA
     WDVIIAQNLN GDYVSDLAAS LIGGPGFVPS GNIGDGYALF ESTHGTAWDI AGKGIANPLS
     LTLSGAMMLE YIGWKEAAQK VYDAVRRTLA EHIGTPDIAS GFQKQGIEAK AVGTMEFAEE
     ISKRIE
//