ID   IDH_COREF               Reviewed;         729 AA.
AC   Q8RQL9;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-NOV-2008, entry version 40.
DE   RecName: Full=Isocitrate dehydrogenase [NADP];
DE            Short=IDH;
DE            EC=1.1.1.42;
DE   AltName: Full=Oxalosuccinate decarboxylase;
GN   Name=icd; OrderedLocusNames=CE0682;
OS   Corynebacterium efficiens.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=152794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RA   Nonaka G., Kimura E., Kawahara Y., Sugimoto S.;
RT   "Corynebacterium efficiens icd gene for isocitrate dehydrogenase,
RT   complete cds.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   MEDLINE=22723752; PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E.,
RA   Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K.,
RA   Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
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   -!- ENZYME REGULATION: Weakly inhibited by oxaloacetate, 2-
CC       oxoglutarate, and citrate. Severely inhibited by oxaloacetate plus
CC       glyoxylate (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SIMILARITY: Belongs to the monomeric-type IDH family.
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DR   EMBL; AB083179; BAB88832.1; -; Genomic_DNA.
DR   EMBL; BA000035; BAC17492.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_737292.1; -.
DR   HSSP; P16100; 1ITW.
DR   SMR; Q8RQL9; 2-727.
DR   GeneID; 1033167; -.
DR   GenomeReviews; BA000035_GR; CE0682.
DR   KEGG; cef:CE0682; -.
DR   NMPDR; fig|196164.1.peg.682; -.
DR   HOGENOM; Q8RQL9; -.
DR   BioCyc; CEFF196164:CE0682-MON; -.
DR   GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
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:InterPro.
DR   InterPro; IPR004436; IsoCit_DHase_NAD_mono.
DR   Pfam; PF03971; IDH; 1.
DR   PIRSF; PIRSF009407; IDH_monmr; 1.
DR   TIGRFAMs; TIGR00178; monomer_idh; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glyoxylate bypass; Magnesium; Metal-binding; NADP;
KW   Oxidoreductase; Phosphoprotein; Tricarboxylic acid cycle.
FT   CHAIN         1    729       Isocitrate dehydrogenase [NADP].
FT                                /FTId=PRO_0000083594.
FT   NP_BIND      80     85       NADP (By similarity).
FT   NP_BIND     571    572       NADP (By similarity).
FT   NP_BIND     587    589       NADP (By similarity).
FT   REGION      121    128       Substrate binding (By similarity).
FT   METAL       337    337       Magnesium or manganese (By similarity).
FT   METAL       535    535       Magnesium or manganese (By similarity).
FT   BINDING     124    124       NADP (By similarity).
FT   BINDING     134    134       Substrate (By similarity).
FT   BINDING     534    534       Substrate (By similarity).
FT   BINDING     576    576       NADP (By similarity).
FT   BINDING     636    636       NADP (By similarity).
FT   SITE        244    244       Critical for catalysis (By similarity).
FT   SITE        407    407       Critical for catalysis (By similarity).
SQ   SEQUENCE   729 AA;  79285 MW;  84BCDECA8687627B CRC64;
     MAKIIWTRTD EAPLLATYSL KPVVEAFAAT AGIEVETRDI SLAGRILAQF ADQLPEEQKV
     SDALAELGEL AKTPEANIIK LPNISASVPQ LKAAVKELQE QGYDLPEYED AKDRYAAVIG
     SNVNPVLREG NSDRRAPVAV KNFVKKFPHR MGEWSADSKT NVATMGADDF RSNEKSVIMD
     EADTVVIKHV AADGTETVLK DSLPLLKGEV IDGTFISAKA LDAFLLDQVK RAKEEGILFS
     AHMKATMMKV SDPIIFGHIV RAYFADVYAQ YGEQLLAAGL NGENGLAAIY AGLDKLDNGA
     EIKAAFDKGL EEGPDLAMVN SAKGITNLHV PSDVIIDASM PAMIRTSGKM WNKDDQTQDA
     LAVIPDSSYA GVYQTVIEDC RKNGAFDPTT MGTVPNVGLM AQKAEEYGSH DKTFRIEADG
     KVQVVASNGD VLIEHDVEKG DIWRACQTKD APIQDWVKLA VNRARLSGMP AVFWLDPARA
     HDRNLTTLVE KYLADHDTEG LDIQILSPVE ATQHAIDRIR RGEDTISVTG NVLRDYNTDL
     FPILELGTSA KMLSVVPLMA GGGLFETGAG GSAPKHVQQV IEENHLRWDS LGEFLALAES
     FRHELNTRNN TKAGVLADAL DRATEKLLNE EKSPSRKVGE IDNRGSHFWL ATYWADELAN
     QTEDAELAET FAPVAEALNN QAADIDAALI GEQGKPVDLG GYYAPSDEKT SAIMRPVAAF
     NEIIDSLKK
//