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Database: UniProt/TrEMBL
Entry: U3GVZ1_9CORY
LinkDB: U3GVZ1_9CORY
Original site: U3GVZ1_9CORY 
ID   U3GVZ1_9CORY            Unreviewed;       738 AA.
AC   U3GVZ1;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
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=CARG_07840 {ECO:0000313|EMBL:AGU15685.1};
OS   Corynebacterium argentoratense DSM 44202.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1348662 {ECO:0000313|EMBL:AGU15685.1, ECO:0000313|Proteomes:UP000016943};
RN   [1] {ECO:0000313|EMBL:AGU15685.1, ECO:0000313|Proteomes:UP000016943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44202 {ECO:0000313|EMBL:AGU15685.1};
RX   PubMed=24092787;
RA   Bomholt C., Glaub A., Gravermann K., Albersmeier A., Brinkrolf K.,
RA   Ruckert C., Tauch A.;
RT   "Whole-Genome Sequence of the Clinical Strain Corynebacterium
RT   argentoratense DSM 44202, Isolated from a Human Throat Specimen.";
RL   Genome Announc. 1:e00793-13(2013).
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; CP006365; AGU15685.1; -; Genomic_DNA.
DR   RefSeq; WP_021012075.1; NC_022198.1.
DR   AlphaFoldDB; U3GVZ1; -.
DR   STRING; 1348662.CARG_07840; -.
DR   GeneID; 78250316; -.
DR   KEGG; caz:CARG_07840; -.
DR   PATRIC; fig|1348662.3.peg.1549; -.
DR   eggNOG; COG2838; Bacteria.
DR   HOGENOM; CLU_025308_1_0_11; -.
DR   OrthoDB; 9807643at2; -.
DR   Proteomes; UP000016943; 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:AGU15685.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016943};
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   738 AA;  79591 MW;  2AC42207CD2C163A CRC64;
     MAKIIYTRTD EAPLLATYSL KPVVEAFAST AGIDVETRDI SLAGRILAQF PDYLGEDQKV
     ADALAELGEL AKTPEANIIK LPNISASVPQ LKAAVKELQA QGFALPDYPD NPSTDEEKDI
     RGRYDSVKGS AVNPVLREGN SDRRAPIAVK NFAKAHPHRM GAWTKDSKTN VATMSDNDFR
     HNEQSVIMPA ADELSIVHIA ADGTETALKS GLKVLEGEVV DATVMRAAAL DEFLAAQVKR
     AKEEGVLFST HLKATMMKVS DPIIFGHVVR AFFADVYAQY GEQLLAAGLD GENGLAAVYA
     GLDNLDNGAE IKAAFDKALA EGPAVAMVNS DKGITNLHVP SDVIVDASMP AMIRTSGHMW
     NAAGEEQDTL AVLPDSSYAG VYQTVIEDCR ANGAFDPATM GTVPNVGLMA QKAEEYGSHD
     KTFKIAGDGK VVVRNAAGET LMEHEVSEGD IWRACQAKDA PIRDWVKLAV TRSRLSGMPA
     VFWLDPERAH DRNLITLVEK YLGEHDTEGL DIRIMSPVEA TQFSIDRIRK GEDTISVTGN
     VLRDYLTDLF PILELGTSAK MLSVVPLMAG GGLFETGAGG SAPKHVQQLV EENHLRWDSL
     GEFLALGESL RHFSNTDGNT KAAVLADALD KATERLLNDG KSPSRKVGEI DNRGSHFYLT
     AYWADELAKQ TDDAELAEIF APVAKELSDN ADAIAAELLE VQGKAVELDG YYNPNDAKAT
     AAMRPSEKFN AIVDGLKK
//
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