ID B7LSM3_ESCF3 Unreviewed; 416 AA. AC B7LSM3; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAR-2024, entry version 81. DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|RuleBase:RU004446}; DE EC=1.1.1.42 {ECO:0000256|RuleBase:RU004446}; GN Name=icd {ECO:0000313|EMBL:CAQ89309.1}; GN OrderedLocusNames=EFER_1794 {ECO:0000313|EMBL:CAQ89309.1}; OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585054 {ECO:0000313|EMBL:CAQ89309.1, ECO:0000313|Proteomes:UP000000745}; RN [1] {ECO:0000313|Proteomes:UP000000745} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / RC JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73 RC {ECO:0000313|Proteomes:UP000000745}; RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344; RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E., RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.; RT "Organised genome dynamics in the Escherichia coli species results in RT highly diverse adaptive paths."; RL PLoS Genet. 5:E1000344-E1000344(2009). 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|ARBA:ARBA00023554}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR604439-3}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRSR:PIRSR604439-3}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. CC {ECO:0000256|PIRSR:PIRSR604439-3}; 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 --------------------------------------------------------------------------- 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; CU928158; CAQ89309.1; -; Genomic_DNA. DR RefSeq; WP_000444487.1; NC_011740.1. DR AlphaFoldDB; B7LSM3; -. DR SMR; B7LSM3; -. DR GeneID; 83576952; -. DR KEGG; efe:EFER_1794; -. DR HOGENOM; CLU_031953_7_1_6; -. DR OrthoDB; 9806254at2; -. DR Proteomes; UP000000745; 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: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; IPR019818; IsoCit/isopropylmalate_DH_CS. DR InterPro; IPR004439; Isocitrate_DH_NADP_dimer_prok. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR NCBIfam; TIGR00183; prok_nadp_idh; 1. DR PANTHER; PTHR43504; ISOCITRATE DEHYDROGENASE [NADP]; 1. DR PANTHER; PTHR43504:SF1; ISOCITRATE DEHYDROGENASE [NADP]; 1. DR Pfam; PF00180; Iso_dh; 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 Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435, KW ECO:0000256|RuleBase:RU004446}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR604439-3}; KW Manganese {ECO:0000256|PIRSR:PIRSR604439-3, ECO:0000256|RuleBase:RU004446}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|RuleBase:RU004446}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR604439-2}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000313|EMBL:CAQ89309.1}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, KW ECO:0000256|RuleBase:RU004446}. FT DOMAIN 28..412 FT /note="Isopropylmalate dehydrogenase-like" FT /evidence="ECO:0000259|SMART:SM01329" FT BINDING 104 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT BINDING 113 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 115 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 119 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 129 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 153 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 307 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-3" FT BINDING 339..345 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT BINDING 352 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT BINDING 391 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT BINDING 395 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT SITE 160 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4" FT SITE 230 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4" FT MOD_RES 100 FT /note="N6-succinyllysine" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5" FT MOD_RES 113 FT /note="Phosphoserine" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5" FT MOD_RES 142 FT /note="N6-acetyllysine" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5" FT MOD_RES 242 FT /note="N6-succinyllysine" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5" SQ SEQUENCE 416 AA; 45770 MW; 9A02EEFCB3B4FDD9 CRC64; MESKVVVPAQ GKKITLQNGK LNVPENPIIP YIEGDGIGVD VTPAMLKVVD AAVEKAYKGE RKISWMEIYT GEKSTQVYGQ DVWLPAETLD LIREYRVAIK GPLTTPVGGG IRSLNVALRQ ELDLYICLRP VRYYQGTPSP VKHPELTDMV IFRENSEDIY AGIEWKADSA DAEKVIKFLR EEMGVKKIRF PEHCGIGIKP CSEEGTKRLV RAAIEYAIAN DRDSVTLVHK GNIMKFTEGA FKDWGYQLAR EEFGGELIDG GPWLKVKNPN TGKEIVIKDV IADAFLQQIL LRPAEYDVIA CMNLNGDYIS DALAAQVGGI GIAPGANIGD ECALFEATHG TAPKYAGQDK VNPGSIILSA EMMLRHMGWT EAADLIVKGM EGAINAKTVT YDFERLMEGA KLLKCSEFGD AIIKNM //