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Database: UniProt/TrEMBL
Entry: Q6NIY5_CORDI
LinkDB: Q6NIY5_CORDI
Original site: Q6NIY5_CORDI 
ID   Q6NIY5_CORDI            Unreviewed;       737 AA.
AC   Q6NIY5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 108.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR009407};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR009407};
DE   AltName: Full=Oxalosuccinate decarboxylase {ECO:0000256|PIRNR:PIRNR009407};
GN   Name=icd {ECO:0000313|EMBL:CAE49148.1};
GN   OrderedLocusNames=DIP0631 {ECO:0000313|EMBL:CAE49148.1};
OS   Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS   gravis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=257309 {ECO:0000313|EMBL:CAE49148.1, ECO:0000313|Proteomes:UP000002198};
RN   [1] {ECO:0000313|EMBL:CAE49148.1, ECO:0000313|Proteomes:UP000002198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis
RC   {ECO:0000313|Proteomes:UP000002198};
RX   PubMed=14602910; DOI=10.1093/nar/gkg874;
RA   Cerdeno-Tarraga A.M., Efstratiou A., Dover L.G., Holden M.T.G., Pallen M.,
RA   Bentley S.D., Besra G.S., Churcher C., James K.D., De Zoysa A.,
RA   Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S.,
RA   Jagels K., Moule S., Quail M.A., Rabbinowitsch E., Rutherford K.,
RA   Thomson N.R., Unwin L., Whitehead S., Barrell B.G.Parkhill.J.;
RT   "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT   NCTC13129.";
RL   Nucleic Acids Res. 31:6516-6523(2003).
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         Evidence={ECO:0000256|PIRNR:PIRNR009407};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR009407-3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR009407-3};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC       {ECO:0000256|PIRSR:PIRSR009407-3};
CC   -!- SIMILARITY: Belongs to the monomeric-type IDH family.
CC       {ECO:0000256|PIRNR:PIRNR009407}.
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DR   EMBL; BX248355; CAE49148.1; -; Genomic_DNA.
DR   RefSeq; WP_010934434.1; NC_002935.2.
DR   AlphaFoldDB; Q6NIY5; -.
DR   STRING; 257309.DIP0631; -.
DR   KEGG; cdi:DIP0631; -.
DR   HOGENOM; CLU_025308_1_0_11; -.
DR   OMA; FRMCQTK; -.
DR   Proteomes; UP000002198; Chromosome.
DR   GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR004436; Isocitrate_DH_NADP_mono.
DR   NCBIfam; TIGR00178; monomer_idh; 1.
DR   PANTHER; PTHR36999; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR   PANTHER; PTHR36999:SF1; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR   Pfam; PF03971; IDH; 1.
DR   PIRSF; PIRSF009407; IDH_monmr; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE   3: Inferred from homology;
KW   Glyoxylate bypass {ECO:0000256|PIRNR:PIRNR009407};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR009407-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR009407-3};
KW   NADP {ECO:0000256|PIRNR:PIRNR009407, ECO:0000256|PIRSR:PIRSR009407-4};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR009407,
KW   ECO:0000313|EMBL:CAE49148.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002198};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT   BINDING         80..85
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         130..137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         133
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         346
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         543
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         544
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         548
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         580..581
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         585
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         596..598
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         645
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   SITE            253
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT   SITE            416
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ   SEQUENCE   737 AA;  79394 MW;  5AD6C98E856BD5E8 CRC64;
     MAKIIYTRTD EAPLLATYSL KPVVEAFAST AGIEVETRDI SLAGRILAQF PDYLNEDQKV
     DDALAELGEL AKTPEANIIK LPNISASVPQ LKAAIAELKA QGFALPEYPD SPATDEEKDV
     RARYDAVKGS AVNPVLREGN SDRRAPIAVK NFAKKNPHKM GVWSADSKTN VATMDANDFR
     HNEKSVIMPA ADTLTIKHIA TDGTETILKD GLKVLEGEVI DGTFLSAKAL DAFLTEQVQR
     AKNENVLFSA HLKATMMKVS DPIIFGHVVR AYFADVFATY GDQLNAAGLN GENGLAAIYS
     GLDALDNGAE IKAAFDAALE AGADVAMVNS AKGITNLHVP SDVIIDASMP AMIRTAGHMW
     NKDDQEQDTL AVIPDSSYAG VYQVVIEDCK KNGAFDPTTM GTVPNVGLMA QKAEEYGSHD
     KTFKIAADGK VVVVNAAGEA LIEHDVEAGD IWRACQAKDA PIQDWVKLAV TRSRLSGMPA
     VFWLDPKRAH DRSLITLVKK YLADHDTEGL DIQIMSPTEA TQFSIDRIRR GEDTISVTGN
     VLRDYNTDLF PILELGTSAK MLSVVPLMAG GGLFETGAGG SAPKHVQQLV EENHLRWDSL
     GEFLALAESL RHFANTEGNT KAGVLADALD RATETLLNEG YSPSRKAGEI DNRGSHFFLT
     LNWAKELAAQ TDDTALAETF APVAAQLEDN KDTIAAALID VQGTPVDLGG YYQPDDAKTA
     AVMRPVAEFN DIIDALK
//
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