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   16-JUN-2009, entry version 57.
DE   RecName: Full=Isocitrate dehydrogenase [NADP];
DE            Short=IDH;
DE            EC=1.1.1.42;
DE   AltName: Full=Oxalosuccinate decarboxylase;
DE   AltName: Full=NADP(+)-specific ICDH;
DE   AltName: Full=IDP;
GN   Name=icd; OrderedLocusNames=aq_1512;
OS   Aquifex aeolicus.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=63363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   MEDLINE=98196666; 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
RT   aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- CATALYTIC ACTIVITY: Isocitrate + NADP(+) = 2-oxoglutarate + CO(2)
CC       + NADPH.
CC   -!- CATALYTIC ACTIVITY: Oxalosuccinate + NADP(+) = 2-oxoglutarate +
CC       CO(2) + NADPH.
CC   -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family.
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DR   EMBL; AE000657; AAC07444.1; -; Genomic_DNA.
DR   PIR; F70431; F70431.
DR   RefSeq; NP_214045.1; -.
DR   HSSP; P08200; 1ISO.
DR   GeneID; 1193103; -.
DR   GenomeReviews; AE000657_GR; aq_1512.
DR   KEGG; aae:aq_1512; -.
DR   NMPDR; fig|224324.1.peg.1060; -.
DR   HOGENOM; O67480; -.
DR   OMA; O67480; RDWGYEL.
DR   BioCyc; AAEO224324:AQ_1512-MON; -.
DR   BRENDA; 1.1.1.42; 189781.
DR   GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR001804; Isocitrate/isopropylmalate_DH.
DR   InterPro; IPR004439; Isocitrate_DH_NADP_prok.
DR   Gene3D; G3DSA:3.40.718.10; IDH_IMDH; 1.
DR   PANTHER; PTHR11835; IDH_IMDH_dimeric; 1.
DR   PANTHER; PTHR11835:SF1; NADP_IDH_prok; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glyoxylate bypass; Magnesium; Manganese;
KW   Metal-binding; NADP; Oxidoreductase; Phosphoprotein;
KW   Tricarboxylic acid cycle.
FT   CHAIN         1    426       Isocitrate dehydrogenase [NADP].
FT                                /FTId=PRO_0000083548.
FT   METAL       312    312       Magnesium or manganese (By similarity).
FT   BINDING     123    123       Substrate (By similarity).
FT   BINDING     125    125       Substrate (By similarity).
FT   BINDING     129    129       Substrate (By similarity).
FT   BINDING     139    139       Substrate (By similarity).
FT   BINDING     162    162       Substrate (By similarity).
FT   SITE        169    169       Critical for catalysis (By similarity).
FT   SITE        239    239       Critical for catalysis (By similarity).
FT   MOD_RES     123    123       Phosphoserine (By similarity).
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
//