ID Q31GM7_HYDCU Unreviewed; 739 AA. AC Q31GM7; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 1. DT 27-MAR-2024, entry version 109. 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=Tcr_1101 {ECO:0000313|EMBL:ABB41696.1}; OS Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira OS crunogena). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Hydrogenovibrio. OX NCBI_TaxID=317025 {ECO:0000313|EMBL:ABB41696.1}; RN [1] {ECO:0000313|EMBL:ABB41696.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=XCL-2 {ECO:0000313|EMBL:ABB41696.1}; 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., Dalin E., Tice H., Pitluck S., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Lykidis A., Scott K.M., Sievert S., Kerfeld C., RA Freyermuth S., Dobrinski K., Boller A., Fitzpatrick K., Thoma P., Moore J., RA Richardson P.; RT "Complete sequence of Thiomicrospira crunogena XCL-2."; RL Submitted (JUL-2006) 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; CP000109; ABB41696.1; -; Genomic_DNA. DR AlphaFoldDB; Q31GM7; -. DR STRING; 317025.Tcr_1101; -. DR KEGG; tcx:Tcr_1101; -. DR eggNOG; COG2838; Bacteria. DR HOGENOM; CLU_025308_1_0_6; -. 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; 2. 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:ABB41696.1}; KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}. FT BINDING 81..86 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 131..138 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 134 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 144 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 349 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT BINDING 546 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 547 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT BINDING 551 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT BINDING 583..584 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 588 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 599..601 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 648 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT SITE 254 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1" FT SITE 419 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1" SQ SEQUENCE 739 AA; 80615 MW; E52ED0373D36817D CRC64; MTAKIIYTLT DEAPALATYS LLPIVEAFTK AAGVSVETRD ISLAGRILAN VPDKLSEAQK VGDALTELGN LAKTPEANII KLPNISASVP QLNAAIKELQ SQGYDIPDYP ATPQNAEEEK IKAAYAKVLG SAVNPVLREG NSDRRAPTSV KNFAKKHPHS MGAWSEDSKS KVAHMTEGDF YGSEKSMTLP EATEFKIEFV SESGDIKELK GTAPLQAGEV IDAAVMSQKA LRDFLAKAVA EAKEQGILFS IHLKATMMKV SDPIIFGQAV SVFFEDVFKK YADEFKKLGV NPNNGLGDVY SKIESLPADK QAEIEASIAK TIEDKADVAM VDSDKGITNL HVPSDVIVDA SMPAMIRTSG KMWNKDGQQQ DALAVIPDRC YAGVYQETIN FCKHHGAFDP TTMGTVPNVG LMAQKAEEYG SHDKTFQMDN AGTVRVVEPN GNVLLEQTVE AGDIFRMCQV KDAPIQDWVK LAVNRARATN TPAVFWLDTN RAHDHQLIEK VNHYLLDHDT TGLEIHIMSP EEATRFTLRH VKEGKDVISV TGNVLRDYLT DLFPILELGT SAKMLSIVPL MNGGGLFETG AGGSAPKHVQ QFMSENHLRW DSLGEFLALA VSLEHLATHF NNPKAQVLAD TLDKATGRFL ENNKSPSRKV GEIDNRGSHF YLAMYWAQEL AAQKADAELK ARFEKVADAL TQNEDTIMSE LNGSQGKSVD IGGYYKFNGE LASQAMRPSA TLNTLIDAV //