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
//