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Database: UniProt/TrEMBL
Entry: D9QEM4_CORP2
LinkDB: D9QEM4_CORP2
Original site: D9QEM4_CORP2 
ID   D9QEM4_CORP2            Unreviewed;       736 AA.
AC   D9QEM4;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 64.
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   ORFNames=CPC231_02320 {ECO:0000313|EMBL:ADL09947.1};
OS   Corynebacterium pseudotuberculosis (strain C231).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=681645 {ECO:0000313|EMBL:ADL09947.1, ECO:0000313|Proteomes:UP000000276};
RN   [1] {ECO:0000313|EMBL:ADL09947.1, ECO:0000313|Proteomes:UP000000276}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C231 {ECO:0000313|EMBL:ADL09947.1,
RC   ECO:0000313|Proteomes:UP000000276};
RX   PubMed=21037006; DOI=.1128/JB.01211-10;
RG   Consortium: Rede Paraense de Genomica e Proteomica (RPGP);
RA   Silva A., Schneider M.P., Cerdeira L., Barbosa M.S., Ramos R.T.,
RA   Carneiro A.R., Santos R., Lima M., D'Afonseca V., Almeida S.S.,
RA   Santos A.R., Soares S.C., Pinto A.C., Ali A., Dorella F.A., Rocha F.,
RA   de Abreu V.A., Trost E., Tauch A., Shpigel N., Miyoshi A., Azevedo V.;
RT   "Complete genome sequence of Corynebacterium pseudotuberculosis I19, a
RT   strain isolated from a cow in Israel with bovine mastitis.";
RL   J. Bacteriol. 193:323-324(2011).
RN   [2] {ECO:0000313|EMBL:ADL09947.1, ECO:0000313|Proteomes:UP000000276}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C231 {ECO:0000313|EMBL:ADL09947.1,
RC   ECO:0000313|Proteomes:UP000000276};
RX   PubMed=21533164; DOI=10.1371/journal.pone.0018551;
RA   Ruiz J.C., D'Afonseca V., Silva A., Ali A., Pinto A.C., Santos A.R.,
RA   Rocha A.A., Lopes D.O., Dorella F.A., Pacheco L.G., Costa M.P., Turk M.Z.,
RA   Seyffert N., Moraes P.M., Soares S.C., Almeida S.S., Castro T.L.,
RA   Abreu V.A., Trost E., Baumbach J., Tauch A., Schneider M.P., McCulloch J.,
RA   Cerdeira L.T., Ramos R.T., Zerlotini A., Dominitini A., Resende D.M.,
RA   Coser E.M., Oliveira L.M., Pedrosa A.L., Vieira C.U., Guimaraes C.T.,
RA   Bartholomeu D.C., Oliveira D.M., Santos F.R., Rabelo E.M., Lobo F.P.,
RA   Franco G.R., Costa A.F., Castro I.M., Dias S.R., Ferro J.A., Ortega J.M.,
RA   Paiva L.V., Goulart L.R., Almeida J.F., Ferro M.I., Carneiro N.P.,
RA   Falcao P.R., Grynberg P., Teixeira S.M., Brommonschenkel S., Oliveira S.C.,
RA   Meyer R., Moore R.J., Miyoshi A., Oliveira G.C., Azevedo V.;
RT   "Evidence for reductive genome evolution and lateral acquisition of
RT   virulence functions in two Corynebacterium pseudotuberculosis strains.";
RL   PLoS ONE 6:E18551-E18551(2011).
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; CP001829; ADL09947.1; -; Genomic_DNA.
DR   RefSeq; WP_014401014.1; NC_017301.2.
DR   AlphaFoldDB; D9QEM4; -.
DR   STRING; 681645.CpC231_0460; -.
DR   GeneID; 69458679; -.
DR   KEGG; cpq:CPC231_02320; -.
DR   PATRIC; fig|681645.3.peg.486; -.
DR   eggNOG; COG2838; Bacteria.
DR   HOGENOM; CLU_025308_1_0_11; -.
DR   OMA; FRMCQTK; -.
DR   OrthoDB; 9807643at2; -.
DR   Proteomes; UP000000276; 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   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:ADL09947.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000276};
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         345
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         542
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         543
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         547
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         579..580
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         584
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         595..597
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         644
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   SITE            252
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT   SITE            415
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ   SEQUENCE   736 AA;  79816 MW;  39771BB46760A831 CRC64;
     MAKIIYTRTD EAPLLATYSL KPVVEAFAST AGIEVETRDI SLAGRILSQF PEFLTEDQKV
     DDALAELGEL AKTPEANIIK LPNISASVPQ LKAAVTELQS QGYKLPNYPD SPSTEEEKDI
     RARYDAVKGS AVNPVLREGN SDRRAPIAVK NFAKKHPHRM GAWSADSKTN VVTMESNDFR
     HNEKSVIMPD NDTLTIKLVT DNGEKVLKDG LKVLKGEVVD GTFISARALD EFLADQVKRA
     KDEGVLFSAH LKATMMKVSD PIIFGHVVRA YFADVFAKYG EQLEAAGLNG ENGLAAIYSG
     LESLPNGAEI KAAFDEALES GADIAMVNSA KGITNLHVPS DVIIDASMPA MIRTSGHMWN
     KNDEEQDTLA VIPDSSYAGV YQTVIADCKK NGAFDPTTMG TVPNVGLMAQ KAEEYGSHDK
     TFKIEANGTV QVVSSAGEVL IEHNVEAGDI WRACQAKDAP IQDWVKLAVT RSRLSGMPAV
     FWLDPERAHD RNLAALVEKY LADHDTEGLD IHIMSPVEAT QFSIDRIRRG EDTISVTGNV
     LRDYNTDLFP ILELGTSAKM LSVVPLMAGG GLFETGAGGS APKHVQQLVE ENHLRWDSLG
     EFLALAESLR HFANTEGNTK AGILADTLDR ATETLLNEGY SPSRKAGEID NRGSHFFLTK
     FWAKELSIQS EDADLAATFT PVAEALETHS EDIADALLAV QGAPADLGGY YHPDDAKTTA
     VMRPVASYND IISSIK
//
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