ID D3UGP7_HELM1 Unreviewed; 742 AA. AC D3UGP7; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 02-SEP-2026, entry version 78. DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR009407}; DE EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR009407}; DE AltName: Full=Oxalosuccinate decarboxylase {ECO:0000256|PIRNR:PIRNR009407}; GN Name=icd {ECO:0000313|EMBL:CBG39668.1}; GN OrderedLocusNames=HMU04060 {ECO:0000313|EMBL:CBG39668.1}; OS Helicobacter mustelae (strain ATCC 43772 / CCUG 25715 / CIP 103759 / LMG OS 18044 / NCTC 12198 / R85-136P) (Campylobacter mustelae). OC Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria; OC Campylobacterales; Helicobacteraceae; Helicobacter. OX NCBI_TaxID=679897 {ECO:0000313|EMBL:CBG39668.1, ECO:0000313|Proteomes:UP000001522}; RN [1] {ECO:0000313|EMBL:CBG39668.1, ECO:0000313|Proteomes:UP000001522} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43772 / LMG 18044 / NCTC 12198 / 12198 RC {ECO:0000313|Proteomes:UP000001522}; RX PubMed=20219135; DOI=10.1186/1471-2164-11-164; RA O'Toole P.W., Snelling W.J., Canchaya C., Forde B.M., Hardie K.R., RA Josenhans C., Graham R.L.J., McMullan G., Parkhill J., Belda E., RA Bentley S.D.; RT "Comparative genomics and proteomics of Helicobacter mustelae, an RT ulcerogenic and carcinogenic gastric pathogen."; RL BMC Genomics 11:164-164(2010). 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 ECO:0000256|PIRNR:PIRNR009407}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR009407-3}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRSR:PIRSR009407-3}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. CC {ECO:0000256|PIRSR:PIRSR009407-3}; CC -!- SIMILARITY: Belongs to the monomeric-type IDH family. CC {ECO:0000256|ARBA:ARBA00046318, ECO:0000256|PIRNR:PIRNR009407}. 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; FN555004; CBG39668.1; -; Genomic_DNA. DR RefSeq; WP_013022759.1; NC_013949.1. DR AlphaFoldDB; D3UGP7; -. DR STRING; 679897.HMU04060; -. DR KEGG; hms:HMU04060; -. DR eggNOG; COG2838; Bacteria. DR HOGENOM; CLU_025308_1_0_7; -. DR Proteomes; UP000001522; Chromosome. DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1. DR InterPro; IPR004436; Isocitrate_DH_NADP_mono. DR NCBIfam; TIGR00178; monomer_idh; 1. DR PANTHER; PTHR36999:SF1; ISOCITRATE DEHYDROGENASE (NADP(+)); 1. DR PANTHER; PTHR36999; ISOCITRATE DEHYDROGENASE [NADP]; 1. DR Pfam; PF03971; IDH; 1. DR PIRSF; PIRSF009407; IDH_monmr; 1. DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1. PE 3: Inferred from homology; KW Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435, KW ECO:0000256|PIRNR:PIRNR009407}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR009407-3}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR009407-3}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR009407}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR009407}; KW Reference proteome {ECO:0000313|Proteomes:UP000001522}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, KW ECO:0000256|PIRNR:PIRNR009407}. FT BINDING 129..136 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 142 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 345 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT BINDING 547 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 548 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT BINDING 552 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT SITE 252 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1" FT SITE 415 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1" SQ SEQUENCE 742 AA; 82856 MW; DAF8E1C16F4A3276 CRC64; MKITYTLTDE SPALATYSFL PIVRAFLHTA GIEVESADIS LAGRILAQFP QHLTPSQRIP NALEALGELV KHKDANLIKT PNISASIPQL KNAIAELQAK GYNVPNYPDN PKNQEEEEIK ENYQKILGSA VNPVLRQGNS DRRSTKAVKQ YAKKNPYKIA PFDSNSKTIV SYMQEGDFFS NEKAVWIKEP TEARIVFENK EGKREILKKG LKLEKEEILD ATFMDVEALD RFYVDQIALC KKQDILFSLH LKATMMKVSD PVIFGHAVRT FFAELFEEFA DELHALGVNP NNGISELLQK IQTSAKKDAI LQKYEEILHK SAKISMVNSD KGITNLHVPS DVIVDASMPA MLKNGAKLWD KEGRECDTNA VIPDRTYATI YEAVIEDLHK FGPLDPSKLG SVANVGLMAK KAQEYGSHDK TFIAKEAGSF KILDHQDRVL LEHAVQKGDI YRANQAKHDA IINWIDLGIQ RSETSHTPAI FWLDEKRPSN KIMIEMVQKR LQERGIALKS SHGANLEILP PKAACLKSLE IIRNGGDVIS ITGNVLRDYL TDLFPILELG TSAKMLSIVP MLSGGAMFET GAGGSAPKQV EQLLLENHLR WDSLGEFLAL QASLEFFAQQ NHNARAKVLA DALDVAIGKW LDNNKAPSRN AGQDDNRTSH FYLAMYFAEA LAKQKEDTAL QERFAPIASE LQAKEQKIKE EFLSKEGVSV DLGGYYKFDD EKAIKIMRPS ATFNEILHKI AQ //