ID A4SDH0_CHLPM Unreviewed; 741 AA. AC A4SDH0; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 27-MAR-2024, entry version 87. 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=Cvib_0507 {ECO:0000313|EMBL:ABP36529.1}; OS Chlorobium phaeovibrioides (strain DSM 265 / 1930) (Prosthecochloris OS vibrioformis (strain DSM 265)). OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=290318 {ECO:0000313|EMBL:ABP36529.1}; RN [1] {ECO:0000313|EMBL:ABP36529.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 265 {ECO:0000313|EMBL:ABP36529.1}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J., RA Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J., RA Schuster S.C., Bryant D.A., Richardson P.; RT "Complete sequence of Prosthecochloris vibrioformis DSM 265."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. 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; CP000607; ABP36529.1; -; Genomic_DNA. DR AlphaFoldDB; A4SDH0; -. DR STRING; 290318.Cvib_0507; -. DR KEGG; pvi:Cvib_0507; -. DR eggNOG; COG2838; Bacteria. DR HOGENOM; CLU_025308_1_0_10; -. DR OrthoDB; 9807643at2; -. 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:ABP36529.1}; KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}. FT BINDING 83..88 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 133..140 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 136 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 146 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 741 AA; 80016 MW; 733144D98B33B164 CRC64; MAKNATIIYT KIDEAPALAT YSLLPVIQAF VKGTGIGVET RDISLAGRII ANFPENLTEE QKIPDYLAEL GELALKPEAN IIKLPNISAS IPQLQAAIKE LQSQGYKIPD YPESPSTDAE KALQARFAKV LGSAVNPVLR EGNSDRRAPL SVKKYAQNNP HRMAAWSADS KSSIASMASG DFYGSEKSVT IAAPTTVRIE FVGAEGSVTV LKDKTSLLQD EVIDTAVMNV RSLRSFFEAQ IDAAKKNGTL LSLHLKATMM KVSDPIMFGH AVSVFYRDVF EKHAAVIKEL GVNVRNGLGD LYAKIQNLPD AQRSEIEADI QAVYPTRPAL AMVDSDKGIT NLHVPNDIIV DASMPVVIRD GGKMWGPDGQ LHDTTAMIPD RCYATMYQAM VEDCKKNGAF DPATIGTVPN VGLMAQKAEE YGSHDKTFTA PAEGFIRVVD AAGTVLMEQA VETGDIFRMC QAKDAPIRDW VKLAVSRARA TGAPAIFWLD SSRAHDAQLI EKVGTYLKEH DTAGLDIRIM NPVEAMQFSL GRLRAGQDTI SVTGNVLRDY LTDLFPIIEL GTSAKMLSVV PLMNGGGLFE TGAGGSAPKH VQQFEKEGYL RWDSLGEFSA LAASFEYLAS AFSNEKAAVL AETLDQAIGK FLDNRKSPAR KVGQIDNRGS HFYLALYWAE ALAAQSGDGE LKSRFADVAA KLAAAETAIN EELIAAQGKP VAMGGYYHVD EALVSAAMRP SATFNAIIDT L //