ID I0EQ41_HELCM Unreviewed; 425 AA. AC I0EQ41; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 24-JAN-2024, entry version 49. DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|RuleBase:RU004446}; DE EC=1.1.1.42 {ECO:0000256|RuleBase:RU004446}; GN OrderedLocusNames=HCD_00140 {ECO:0000313|EMBL:AFI05060.1}; OS Helicobacter cetorum (strain ATCC BAA-540 / MIT 99-5656). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=1163745 {ECO:0000313|EMBL:AFI05060.1, ECO:0000313|Proteomes:UP000005013}; RN [1] {ECO:0000313|Proteomes:UP000005013} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-540 / MIT 99-5656 {ECO:0000313|Proteomes:UP000005013}; RA Kersulyte D., Berg D.E.; RT "Complete genome sequence of Helicobacter cetorum strain MIT 99-5656."; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AFI05060.1, ECO:0000313|Proteomes:UP000005013} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-540 / MIT 99-5656 {ECO:0000313|Proteomes:UP000005013}; RX PubMed=24358262; RA Kersulyte D., Rossi M., Berg D.E.; RT "Sequence Divergence and Conservation in Genomes ofHelicobacter cetorum RT Strains from a Dolphin and a Whale."; RL PLoS ONE 8:E83177-E83177(2013). 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; CP003481; AFI05060.1; -; Genomic_DNA. DR RefSeq; WP_014658589.1; NC_017735.1. DR AlphaFoldDB; I0EQ41; -. DR STRING; 1163745.HCD_00140; -. DR KEGG; hcm:HCD_00140; -. DR PATRIC; fig|1163745.3.peg.32; -. DR eggNOG; COG0538; Bacteria. DR HOGENOM; CLU_031953_7_1_7; -. DR OrthoDB; 9806254at2; -. DR Proteomes; UP000005013; 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; 47165 MW; 960DB6FC70A9FB7C CRC64; MAYNPKFLEK PKEGEEITIE NGKLHVPNNP IIPFIEGDGI GSDITPAMIK VVDKAVEKAY KGAKKIAWYE VFVGEKCYNK FKDHKELSPE EQWLLPDTID AINHYKVAIK GPLTTPIGEG FRSLNVALRQ KMDLYVCLRP VRWYGSPSPV KEPNKVDMVI FRENAEDIYA GVEWAEGSAE AKKLIHFLQD ELKVTKIRFP ETSGIGVKPI SKEGTERLVR KAIEYAIDND KPSVTFVHKG NIMKFTEGAF MKWGYALAQK EFGAKVIDKG PWCSIKNPKT GKEIVIKDMI ADAFLQQILL RPSEYSVIAT MNLNGDYISD ALAAMVGGIG IAPGANLNDT VGMFEATHGT APKYTGLDKV NPGSIILSAE MMLRHMGWVE AADLIVSSME KAIKSKKVTY DFARLMEGAT EVKCSEFADV MIGCM //