ID E1Q3R6_HELPP Unreviewed; 425 AA. AC E1Q3R6; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAR-2024, entry version 66. DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|RuleBase:RU004446}; DE EC=1.1.1.42 {ECO:0000256|RuleBase:RU004446}; GN OrderedLocusNames=HPPC_00125 {ECO:0000313|EMBL:ADO06288.1}; OS Helicobacter pylori (strain PeCan4). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=765963 {ECO:0000313|EMBL:ADO06288.1, ECO:0000313|Proteomes:UP000006863}; RN [1] {ECO:0000313|Proteomes:UP000006863} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PeCan4 {ECO:0000313|Proteomes:UP000006863}; RA Kersulyte D., Vasquez J., Gilman R.H., Berg D.E.; RT "Complete genome sequence of Helicobacter pylori strain PeCan4."; RL Submitted (JUN-2010) 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; CP002074; ADO06288.1; -; Genomic_DNA. DR RefSeq; WP_000323979.1; NC_014555.1. DR AlphaFoldDB; E1Q3R6; -. DR KEGG; hpc:HPPC_00125; -. DR HOGENOM; CLU_031953_7_1_7; -. DR Proteomes; UP000006863; 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 Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, KW ECO:0000256|RuleBase:RU004446}. FT DOMAIN 31..421 FT /note="Isopropylmalate dehydrogenase-like" FT /evidence="ECO:0000259|SMART:SM01329" FT BINDING 114 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT BINDING 123 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 125 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 139 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 162 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 316 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-3" FT BINDING 348..354 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT BINDING 361 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT BINDING 400 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT BINDING 404 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT SITE 169 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4" FT SITE 239 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4" FT MOD_RES 110 FT /note="N6-succinyllysine" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5" FT MOD_RES 123 FT /note="Phosphoserine" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5" FT MOD_RES 151 FT /note="N6-acetyllysine" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5" SQ SEQUENCE 425 AA; 47522 MW; C7EE417A1CCF10EB CRC64; MAYNPKILQK PKEGEEITIK DNKLHVPNHP IIPFIEGDGI GSDITPAMIK VVDSAVQKAY KGEKKIAWYE VFVGEKCYQK FKDHKELSPE EQWLLPDTIE AINHYKVSIK GPLTTPIGEG FRSLNVALRQ KMDLYVCLRP VRWYGSPSPV KEPQKVDMVI FRENSEDIYA GIEWQEGSTE AKKLIHFLQN ELKVKKIRFP ESSGIGVKPI SKEGTERLVR KAIEYAIDND KPSVTFVHKG NIMKYTEGAF MKWGYALAQK EFNAQVIDKG PWCSLKNPKT GKEIIIKDMI ADAFLQQILL RPSEYSVIAT MNLNGDYISD ALAAMVGGIG IAPGANLNDT VGMFEATHGT APKYAGLDKV NPGSIILSAE MMLRHMGWVE AADLIVSAME KAIKSKKVTY DFARLMDGAK EVKCSEFASV MIENM //