ID H2G1D1_OCESG Unreviewed; 743 AA. AC H2G1D1; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAR-2024, entry version 56. 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 OrderedLocusNames=GU3_00335 {ECO:0000313|EMBL:AEX99823.1}; OS Oceanimonas sp. (strain GK1 / IBRC-M 10197). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Oceanimonas. OX NCBI_TaxID=511062 {ECO:0000313|EMBL:AEX99823.1, ECO:0000313|Proteomes:UP000007742}; RN [1] {ECO:0000313|EMBL:AEX99823.1, ECO:0000313|Proteomes:UP000007742} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GK1 {ECO:0000313|EMBL:AEX99823.1, RC ECO:0000313|Proteomes:UP000007742}; RX PubMed=22461556; DOI=10.1128/JB.00023-12; RA Parsa Yeganeh L., Azarbaijani R., Sarikhan S., Mousavi H., Ramezani M., RA Amoozegar M.A., Shahzadeh Fazeli A., Salekdeh G.H.; RT "Complete genome sequence of Oceanimonas sp. GK1, a halotolerant bacterium RT from Gavkhouni Wetland in Iran."; RL J. Bacteriol. 194:2123-2124(2012). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP003171; AEX99823.1; -; Genomic_DNA. DR RefSeq; WP_014290560.1; NC_016745.1. DR AlphaFoldDB; H2G1D1; -. DR STRING; 511062.GU3_00335; -. DR KEGG; oce:GU3_00335; -. DR eggNOG; COG2838; Bacteria. DR HOGENOM; CLU_025308_1_0_6; -. DR OrthoDB; 9807643at2; -. DR Proteomes; UP000007742; 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 Reference proteome {ECO:0000313|Proteomes:UP000007742}; KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}. FT BINDING 84..89 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 134..141 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 137 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 147 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 351 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT BINDING 548 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 549 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT BINDING 553 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT BINDING 585..586 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 590 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 601..603 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 650 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT SITE 256 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1" FT SITE 421 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1" SQ SEQUENCE 743 AA; 82090 MW; 91323AD118B672FA CRC64; MTNKTSTIVY TLTDEAPALA TYSLLPIIRT FTDAAGIDVT LSDISLAGRV LAAFPERLTD EQRVADGLAE LGKLTQDPHA NIIKLPNISA SVPQLRACIK ELQSQGYNVP DFPEEPKTDE DKAIREAYSK ILGSAVNPVL RQGNSDRRAP AAVKAFARKY PHSMGAWSKA SRSHADYMNG GDFFSSEQSV TMDKAQTVRI EFIGQDGKPQ LKKELALQAG EVLDSMFMSA KALEAFFEQT LQDCKDAGVM WSLHVKATMM KVSHPIVFGH AVKVFYKEVF DKYGKLFEEL GVNPNNGMSS VLEKIKTLPQ STQEEIEQAI HDCYEHRPEM AMVDSVKGIT NLHVPSDVIV DASMPAMIRN SGQMWGRDGK LKDTKAVMPE STYARIYQEV INFCKTNGAF DPRTMGSVSN VGLMAMKAEE YGSHDKTFEM TENGTMRVVN EAGEVLMQHE VEKGDIWRAC QTKDAAIRDW VKLAVNRARN SATPAVFWLD DERAHDNELR KKVNTYLQEH DLTGLDIHIM SYNEAIRFSM ERMKRGKDTI SVTGNVLRDY LTDLFPIMEL GTSAKMLSIV PMLAGGGMYE TGAGGSAPKH VQQLMEENHL RWDSLGEFLA LAVSLEELGI KEGNDRAKLL AKCLDKATEL LLDNGKSPSR RAGELDNRGS HFYLALYWAQ ELAAQTEDEA LAAHFAPLAK ALADNEAKIV AELNAVQGKS AGVHGYYHAS PAELEQVMRP SATLNQTLAQ LNG //