IDH_AQUAE
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 03-AUG-2022, entry version 121.
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; 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 OMA; CVRPCRY; -.
DR OrthoDB; 1551125at2; -.
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 InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004439; Isocitrate_DH_NADP_dimer_prok.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR PANTHER; PTHR43504; PTHR43504; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 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