ID Q8EDW2_SHEON Unreviewed; 741 AA. AC Q8EDW2; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 119. 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 Name=icd {ECO:0000313|EMBL:AAN55658.1}; GN OrderedLocusNames=SO_2629 {ECO:0000313|EMBL:AAN55658.1}; OS Shewanella oneidensis (strain MR-1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=211586 {ECO:0000313|EMBL:AAN55658.1, ECO:0000313|Proteomes:UP000008186}; RN [1] {ECO:0000313|EMBL:AAN55658.1, ECO:0000313|Proteomes:UP000008186} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MR-1 {ECO:0000313|EMBL:AAN55658.1, RC ECO:0000313|Proteomes:UP000008186}; RX PubMed=12368813; DOI=10.1038/nbt749; RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C., RA Read T.D., Eisen J.A., Seshadri R., Ward N., Methe B., Clayton R.A., RA Meyer T., Tsapin A., Scott J., Beanan M., Brinkac L., Daugherty S., RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R., RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J., Weidman J., RA Impraim M., Lee K., Berry K., Lee C., Mueller J., Khouri H., Gill J., RA Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C., RA Nealson K.H., Fraser C.M.; RT "Genome sequence of the dissimilatory metal ion-reducing bacterium RT Shewanella oneidensis."; RL Nat. Biotechnol. 20:1118-1123(2002). 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; AE014299; AAN55658.1; -; Genomic_DNA. DR RefSeq; NP_718214.1; NC_004347.2. DR RefSeq; WP_011072577.1; NZ_CP053946.1. DR AlphaFoldDB; Q8EDW2; -. DR STRING; 211586.SO_2629; -. DR PaxDb; 211586-SO_2629; -. DR KEGG; son:SO_2629; -. DR PATRIC; fig|211586.12.peg.2532; -. DR eggNOG; COG2838; Bacteria. DR HOGENOM; CLU_025308_1_0_6; -. DR OrthoDB; 9807643at2; -. DR PhylomeDB; Q8EDW2; -. DR BioCyc; SONE211586:G1GMP-2415-MONOMER; -. DR Proteomes; UP000008186; 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:AAN55658.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008186}; 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 741 AA; 80501 MW; A9F17C40A617ECE7 CRC64; MKDNSPTIIY TETDEAPALA TLSLLPIIKT FTNAADVAVE TRDISLSGRV IANFPEKLTD AQKIGDHLAE LGDLANQPEA NIIKLPNISA SIPQLKACIL ELQQKGYDIP NYPDEPKTDE EKSIKARYDK IKGSAVNPVL REGNSDRRAP LSVKNFAKKN PHSMGKWVKD SKSHVAHMSE GDFYGSELSV TLSNADTVNI VLAQKDGQEV VLKSGLKLLA GEIIDASVMS KKALVSFFER EIANAKAENV LLSLHLKATM MKVSDPIMFG HAVKVFFKPV FDKHAALFAE LGVDVNNGFG DVYAKIASLP TDVRSQIEAD IAAVYAEGPA LAMVDSDKGI TNLHVPSDII IDASMPAAIR SSGQMWGPDG KLHDTKALIP DRCYAGVYQE TIAFCKEHGA FDPSTMGSVP NVGLMAQKAE EYGSHDKTFE IPADGVVNVI DASGKVLMSH NVEAGDIWRM CQVKDAPIRD WVKLAVRRAR LSNTPAVFWL DANRAHDAQL IVKVKQYLPE HDTSGLDISI MSPEEATRFS LARIKEGKDT ISVTGNVLRD YLTDLFPILE LGTSAKMLSI VPLMNGGGLF ETGAGGSAPK HVQQVEKEGH LRWDSLGEFL ALAASLEHLS QTVGNPKAQV LADTLDQAIG QFLDSNKSPS RRVGELDNRG SHFYLAMYWA QALAVQTKDE QLQAHFIPLA HALSANEQVI VAELNNAQGA PVDLGGYYRL DAVKAEKAMR PSETLNKLLI A //