ID   IDH_HELPY               Reviewed;         425 AA.
AC   P56063;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-JUN-2009, entry version 61.
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=HP_0027;
OS   Helicobacter pylori (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=210;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   MEDLINE=97394467; PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R.,
RA   Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F.,
RA   Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G.,
RA   Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D.,
RA   Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D.,
RA   Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C.,
RA   Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D.,
RA   Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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; AE000511; AAD07098.1; -; Genomic_DNA.
DR   PIR; C64523; C64523.
DR   RefSeq; NP_206829.1; -.
DR   HSSP; P08200; 1PB1.
DR   DIP; DIP:3724N; -.
DR   GeneID; 899116; -.
DR   GenomeReviews; AE000511_GR; HP_0027.
DR   KEGG; hpy:HP0027; -.
DR   NMPDR; fig|85962.1.peg.27; -.
DR   TIGR; HP_0027; -.
DR   HOGENOM; P56063; -.
DR   OMA; P56063; RDWGYEL.
DR   BRENDA; 1.1.1.42; 1131.
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   TIGRFAMs; TIGR00183; prok_nadp_idh; 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    425       Isocitrate dehydrogenase [NADP].
FT                                /FTId=PRO_0000083552.
FT   NP_BIND     348    354       NADP (By similarity).
FT   METAL       316    316       Magnesium or manganese (By similarity).
FT   BINDING     114    114       NADP (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   BINDING     361    361       NADP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     400    400       NADP (By similarity).
FT   BINDING     404    404       NADP (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   425 AA;  47531 MW;  3741722B8818DC96 CRC64;
     MAYNPKILQK PKEGEEITIK DNKLHVPNHP IIPFIEGDGI GSDITPAMIK VVDSAVQKAY
     KGEKKIAWYE VFVGEKCYQK FKDYKELSPE EQWLLPDTIE AINHYKVSIK GPLTTPIGEG
     FRSLNVALRQ KMDLYVCLRP VRWYGSPSPV KEPQKVDMVI FRENSEDIYA GIEWQEGSAE
     AKKLIHFLQN ELKVKKIRFP ESSGIGVKPI SKEGTERLVR KAIEYAIDND KPSVTFVHKG
     NIMKYTEGAF MKWGYALAQK EFNAQVIDKG PWCSLKNPKN GKEIIIKDMI ADAFLQQILL
     RPSEYSVIAT MNLNGDYISD ALAAMVGGIG IAPGANLNDT VGMFEATHGT APKYAGLDKV
     NPGSIILSAE MMLRHMGWVE AADLIVSAME KAIKSKKVTY DFARLMDGAK EVKCSEFASV
     MIENM
//