ID A5W1G5_PSEP1 Unreviewed; 418 AA. AC A5W1G5; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 27-MAR-2024, entry version 94. DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|RuleBase:RU004446}; DE EC=1.1.1.42 {ECO:0000256|RuleBase:RU004446}; GN OrderedLocusNames=Pput_1822 {ECO:0000313|EMBL:ABQ77975.1}; OS Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=351746 {ECO:0000313|EMBL:ABQ77975.1}; RN [1] {ECO:0000313|EMBL:ABQ77975.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F1 {ECO:0000313|EMBL:ABQ77975.1}; 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., Parales R., Richardson P.; RT "Complete sequence of Pseudomonas putida F1."; RL Submitted (MAY-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|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; CP000712; ABQ77975.1; -; Genomic_DNA. DR AlphaFoldDB; A5W1G5; -. DR KEGG; ppf:Pput_1822; -. DR eggNOG; COG0538; Bacteria. DR HOGENOM; CLU_031953_7_1_6; -. 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:ABQ77975.1}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, KW ECO:0000256|RuleBase:RU004446}. FT DOMAIN 30..414 FT /note="Isopropylmalate dehydrogenase-like" FT /evidence="ECO:0000259|SMART:SM01329" FT BINDING 106 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT BINDING 115 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 117 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 121 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 131 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 155 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 309 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-3" FT BINDING 341..347 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT BINDING 354 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT BINDING 393 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT BINDING 397 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT SITE 162 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4" FT SITE 232 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4" FT MOD_RES 102 FT /note="N6-succinyllysine" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5" FT MOD_RES 115 FT /note="Phosphoserine" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5" FT MOD_RES 144 FT /note="N6-acetyllysine" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5" FT MOD_RES 244 FT /note="N6-succinyllysine" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5" SQ SEQUENCE 418 AA; 45705 MW; 81779C112CE46E4C CRC64; MGYQKIKVPT DGTKITVNAD HSLNVPDHPI IPYIEGDGIG VDVSPVMIKV VDAAVHKAYG GKRKIAWMEV YAGEKATQVY DQDTWLPQET LDAVRDYVVS IKGPLTTPVG GGIRSLNVAL RQQLDLYVCL RPVLWFQGVP SPVKKPGDVD MVIFRENSED IYAGIEWKAG SPEANKVIKF LKEEMGVTKI RFDQDCGIGV KPVSKEGTKR LVRKALQYVV DNDRESLTLV HKGNIMKFTE GAFKDWGYEV ARDEFGAELL DGGPWMKFKN PKTGREVIVK DAIADAMLQQ ILLRPAEYDV IATLNLNGDY LSDALAAEVG GIGIAPGANL SDTVAMFEAT HGTAPKYAGQ DKVNPGSVIL SAEMMLRHMG WTEAADLIIK GTNGAIAAKT VTYDFERLME GAKLVSSSGF GDEMIKHM //