{"metadata":{"accession":"PF01977","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR048304","hierarchy":null,"name":{"name":"3-octaprenyl-4-hydroxybenzoate carboxy-lyase Rift-related domain","short":"UbiD"},"description":[{"text":"<p>This family has been characterised as 3-octaprenyl-4- hydroxybenzoate carboxy-lyase enzymes [[cite:PUB00020511]]. This enzyme catalyses the third reaction in ubiquinone biosynthesis. For optimal activity the carboxy-lase was shown to require Mn2+ [[cite:PUB00020511]]. This entry represents the central RIFT-related domain.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":[{"title":"UbiD_protein_domain","extract":"<p>In molecular biology this protein domain, refers to UbiD, which is found in prokaryotes, archaea and fungi, with two members in <i>Archaeoglobus fulgidus</i>. They are related to UbiD, a 3-octaprenyl-4-hydroxybenzoate carboxy-lyase from <i>Escherichia coli</i> that is involved in ubiquinone biosynthesis. The member from <i>Helicobacter pylori</i> has a C-terminal extension of just over 100 residues that is shared, in part, by the <i>Aquifex aeolicus</i> homologue.</p>","thumbnail":null}],"literature":{"PUB00152178":{"PMID":28857436,"ISBN":null,"volume":"56","issue":"44","year":2017,"title":"Regioselective para-Carboxylation of Catechols with a Prenylated Flavin Dependent Decarboxylase.","URL":null,"raw_pages":"13893-13897","medline_journal":"Angew Chem Int Ed Engl","ISO_journal":"Angew Chem Int Ed Engl","authors":["Payer SE","Marshall SA","Barland N","Sheng X","Reiter T","Dordic A","Steinkellner G","Wuensch C","Kaltwasser S","Fisher K","Rigby SEJ","Macheroux P","Vonck J","Gruber K","Faber K","Himo F","Leys D","Pavkov-Keller T","Glueck SM."],"DOI_URL":"https://doi.org/10.1002/anie.201708091"},"PUB00152176":{"PMID":23671667,"ISBN":null,"volume":"8","issue":"5","year":2013,"title":"Structural insights into the UbiD protein family from the crystal structure of PA0254 from Pseudomonas aeruginosa.","URL":null,"raw_pages":"e63161","medline_journal":"PLoS One","ISO_journal":"PLoS One","authors":["Jacewicz A","Izumi A","Brunner K","Schnell R","Schneider G."],"DOI_URL":"https://doi.org/10.1371/journal.pone.0063161"},"PUB00152175":{"PMID":26083754,"ISBN":null,"volume":"522","issue":"7557","year":2015,"title":"New cofactor supports α,β-unsaturated acid decarboxylation via 1,3-dipolar cycloaddition.","URL":null,"raw_pages":"497-501","medline_journal":"Nature","ISO_journal":"Nature","authors":["Payne KA","White MD","Fisher K","Khara B","Bailey SS","Parker D","Rattray NJ","Trivedi DK","Goodacre R","Beveridge R","Barran P","Rigby SE","Scrutton NS","Hay S","Leys D."],"DOI_URL":"https://doi.org/10.1038/nature14560"},"PUB00020511":{"PMID":782527,"ISBN":null,"volume":"436","issue":"4","year":1976,"title":"Membrane-associated reactions in ubiquinone biosynthesis in Escherichia coli. 3-Octaprenyl-4-hydroxybenzoate carboxy-lyase.","URL":null,"raw_pages":"800-10","medline_journal":"Biochim Biophys Acta","ISO_journal":"Biochim. Biophys. Acta","authors":["Leppik RA","Young IG","Gibson F."],"DOI_URL":"http://dx.doi.org/10.1016/0005-2736(76)90407-7"},"PUB00152177":{"PMID":25862228,"ISBN":null,"volume":"81","issue":"12","year":2015,"title":"Structure and Mechanism of Ferulic Acid Decarboxylase (FDC1) from Saccharomyces cerevisiae.","URL":null,"raw_pages":"4216-23","medline_journal":"Appl Environ Microbiol","ISO_journal":"Appl Environ Microbiol","authors":["Bhuiya MW","Lee SG","Jez JM","Yu O."],"DOI_URL":"https://doi.org/10.1128/AEM.00762-15"},"PUB00152179":{"PMID":28057757,"ISBN":null,"volume":"292","issue":"11","year":2017,"title":"Oxidative Maturation and Structural Characterization of Prenylated FMN Binding by UbiD, a Decarboxylase Involved in Bacterial Ubiquinone Biosynthesis.","URL":null,"raw_pages":"4623-4637","medline_journal":"J Biol Chem","ISO_journal":"J Biol Chem","authors":["Marshall SA","Fisher K","Ni Cheallaigh A","White MD","Payne KA","Parker DA","Rigby SE","Leys D."],"DOI_URL":"https://doi.org/10.1074/jbc.M116.762732"}},"set_info":{"accession":"CL0336","name":"FMN-binding"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":34,"interactions":0,"matches":11748,"pathways":0,"proteins":11717,"proteomes":9103,"sets":1,"structural_models":{"alphafold":7643},"structures":83,"taxa":13944},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":289,"alignment:full":5966},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}