ID I3TJN7_TISMK Unreviewed; 415 AA. AC I3TJN7; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 27-MAR-2024, entry version 56. DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108}; DE EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108}; GN OrderedLocusNames=TMO_1136 {ECO:0000313|EMBL:AFK52975.1}; OS Tistrella mobilis (strain KA081020-065). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales; OC Geminicoccaceae; Tistrella. OX NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK52975.1, ECO:0000313|Proteomes:UP000005258}; RN [1] {ECO:0000313|EMBL:AFK52975.1, ECO:0000313|Proteomes:UP000005258} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK52975.1, RC ECO:0000313|Proteomes:UP000005258}; RX PubMed=22458477; DOI=10.1021/ja301735a; RA Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H., RA Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.; RT "Bacterial biosynthesis and maturation of the didemnin anti-cancer RT agents."; RL J. Am. Chem. Soc. 134:8625-8632(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:PIRNR000108}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRNR:PIRNR000108, CC ECO:0000256|PIRSR:PIRSR000108-3}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRNR:PIRNR000108, CC ECO:0000256|PIRSR:PIRSR000108-3}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. CC {ECO:0000256|PIRNR:PIRNR000108, ECO:0000256|PIRSR:PIRSR000108-3}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00001936}; CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769, CC ECO:0000256|PIRNR:PIRNR000108}. 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; CP003236; AFK52975.1; -; Genomic_DNA. DR AlphaFoldDB; I3TJN7; -. DR STRING; 1110502.TMO_1136; -. DR KEGG; tmo:TMO_1136; -. DR PATRIC; fig|1110502.3.peg.1170; -. DR eggNOG; COG0538; Bacteria. DR HOGENOM; CLU_023296_1_1_5; -. DR Proteomes; UP000005258; Chromosome. DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0006102; P:isocitrate metabolic process; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1. DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS. DR InterPro; IPR004790; Isocitrate_DH_NADP. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR NCBIfam; TIGR00127; nadp_idh_euk; 1. DR PANTHER; PTHR11822:SF21; ISOCITRATE DEHYDROGENASE [NADP], MITOCHONDRIAL; 1. DR PANTHER; PTHR11822; NADP-SPECIFIC ISOCITRATE DEHYDROGENASE; 1. DR Pfam; PF00180; Iso_dh; 1. DR PIRSF; PIRSF000108; IDH_NADP; 1. DR SMART; SM01329; Iso_dh; 1. DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1. DR PROSITE; PS00470; IDH_IMDH; 1. PE 3: Inferred from homology; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000108}; KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRNR:PIRNR000108}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRNR:PIRNR000108}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000108}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR000108}; KW Reference proteome {ECO:0000313|Proteomes:UP000005258}; KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}. FT DOMAIN 19..405 FT /note="Isopropylmalate dehydrogenase-like" FT /evidence="ECO:0000259|SMART:SM01329" FT BINDING 85..87 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4" FT BINDING 87 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2" FT BINDING 92 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4" FT BINDING 104..110 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2" FT BINDING 119 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2" FT BINDING 142 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2" FT BINDING 261 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-3" FT BINDING 269 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4" FT BINDING 284 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-3" FT BINDING 319..324 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4" FT BINDING 337 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4" FT SITE 149 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-1" FT SITE 221 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-1" SQ SEQUENCE 415 AA; 46329 MW; BA26676BD26AD356 CRC64; MPRIAEEIVR MTKIKVANPV VELDGDEMTR IIWRFIKDKL ILPYLDVDLL YYDLGVEHRD ATNDKVTVDA AEAIAKHGVG VKCATITPDE ARVEEFKLKQ MWKSPNGTIR NILGGTVFRE PIICRNVPRL VPGWTQPIVI GRHAFGDQYR ATDFKVPGKG TLTVRFQPED GGEAIEYEVF KFPGSGVAMA MYNLDESIRG FARACMNYGL QRGYPVYLST KNTILKAYDG RFKDLFQEVF DAEFADQFKA AGIVYEHRLI DDMVASALKW DGGFVWACKN YDGDVQSDTV AQGFGSLGLM TSVLMTPDGK TVEAEAAHGT VTRHFREHQK GRETSTNPIA SIFAWTRGLG YRGKFDGNDA LIGFAETLER VCVETVEAGH MTKDLAILVG KDQAWLNTNA FLDKIDENLK KAMAS //