ID K0C4Y6_CYCSP Unreviewed; 743 AA. AC K0C4Y6; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 27-MAR-2024, entry version 44. 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=Q91_1570 {ECO:0000313|EMBL:AFT67605.1}; OS Cycloclasticus sp. (strain P1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Cycloclasticus. OX NCBI_TaxID=385025 {ECO:0000313|EMBL:AFT67605.1, ECO:0000313|Proteomes:UP000006282}; RN [1] {ECO:0000313|EMBL:AFT67605.1, ECO:0000313|Proteomes:UP000006282} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P1 {ECO:0000313|EMBL:AFT67605.1, RC ECO:0000313|Proteomes:UP000006282}; RX PubMed=23144416; DOI=10.1128/JB.01837-12; RA Lai Q., Li W., Wang B., Yu Z., Shao Z.; RT "Complete genome sequence of the pyrene-degrading bacterium Cycloclasticus RT sp. strain P1."; RL J. Bacteriol. 194:6677-6677(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; CP003230; AFT67605.1; -; Genomic_DNA. DR RefSeq; WP_015006375.1; NC_018697.1. DR AlphaFoldDB; K0C4Y6; -. DR STRING; 385025.Q91_1570; -. DR KEGG; cyq:Q91_1570; -. DR PATRIC; fig|385025.3.peg.1606; -. DR HOGENOM; CLU_025308_1_0_6; -. DR Proteomes; UP000006282; 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:UP000006282}; 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 352 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT BINDING 549 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 550 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT BINDING 554 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT BINDING 586..587 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 591 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 602..604 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 651 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT SITE 257 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1" FT SITE 422 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1" SQ SEQUENCE 743 AA; 82427 MW; C6EC019216DC833D CRC64; MTVKKSKIIY TLTDEAPLLA TASFLPIVEA FAGAAGIDVE VSDISLASRV LATFADQLPD DQKVPDALSE LGRLTQNPET NIIKLPNISA SVPQLKAIIN ELQGKGFDIP NYPEDPQTDE EKALQQKYGK VLGSAVNPVL REGNSDRRAP KAVKEYAKKN PHSMGKWSQA SRTHVSHMRS GDFYSSEKSL TLDKACKVNI EFVAKNGEVT VLKKGLALQE GEIIDSMFMS KKQLCAYLED EMNDAKETGV MFSFHVKATM MKVSHPIVFG HAVKVYYKDL FEKHGKLFDE LGVNPNDGLS SVYEHIEKLP ASIKEEILSD MHACYEKRPE LAMVDSAKGI SNLHTPNEVI VDASMPAMIR AGGKMWGPDG KMKDTKAVMP ESTFARIYQE IINFCKTHGE FDPTTMGTVP NVGLMAQKAE EYGSHDKTFE MKADGSTRIV DEEGNVLLEM DVEEGDIWRM CQVKDAPIQD WVKLAVKRAR LSNTPAVFWL DKYRPHENEL IKKVEKYLKD HDLTGVDIKI KSQTRAMRYT LERILRGKDT ISVTGNILRD YLTDLFPILE LGTSAKMLSI VPLMAGGGLF ETGAGGSAPK HVKQLIEENH LRWDSLGEFL ALCASLEHTA ISDDNAKAAV LAKTLDEATA KLLDTGKSPS RKTGELDNRG SHFYLALYWA QALAEQTEDE ALQAHFQPLA ASLTENEEKI VGTLTTEQWH AVDIGGYYKP DVDKVREVMR PSEIFNEALA SLK //