{"metadata":{"accession":"PF06155","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR010376","hierarchy":null,"name":{"name":"Gamma-butyrobetaine hydroxylase-like, N-terminal","short":"GBBH-like_N"},"description":[{"text":"<p>This domain is found in several proteins including gamma-butyrobetaine dioxygenase, Fe-S cluster assembly factor HCF101  and trimethyllysine dioxygenase proteins. Gamma-butyrobetaine  hydroxylase (GBBH) is a alpha-ketoglutarate-dependent dioxygenase  that catalyzes the biosynthesis of L-carnitine by hydroxylation of gamma-butyrobetaine (GBB). GBBH is a dimeric enzyme. The monomer consists of a catalytic double-stranded beta-helix domain and a smaller N-terminal domain. The N-terminal domain has a bound Zn ion,  which is coordinated by three cysteines and one histidine. The  N-terminal domain could facilitate dimer formation, but its precise  function is not known [[cite:PUB00075680]]. Other family members have been suggested  to be involved in FeS cluster maintenance (see Supplementary note 5  in [[cite:PUB00093610]].)</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00093610":{"PMID":29769716,"ISBN":null,"volume":"557","issue":"7706","year":2018,"title":"Mutant phenotypes for thousands of bacterial genes of unknown function.","URL":null,"raw_pages":"503-509","medline_journal":"Nature","ISO_journal":"Nature","authors":["Price MN","Wetmore KM","Waters RJ","Callaghan M","Ray J","Liu H","Kuehl JV","Melnyk RA","Lamson JS","Suh Y","Carlson HK","Esquivel Z","Sadeeshkumar H","Chakraborty R","Zane GM","Rubin BE","Wall JD","Visel A","Bristow J","Blow MJ","Arkin AP","Deutschbauer AM."],"DOI_URL":null},"PUB00075680":{"PMID":20599753,"ISBN":null,"volume":"398","issue":"4","year":2010,"title":"Crystal structure of human gamma-butyrobetaine hydroxylase.","URL":null,"raw_pages":"634-9","medline_journal":"Biochem Biophys Res Commun","ISO_journal":"Biochem. Biophys. Res. Commun.","authors":["Tars K","Rumnieks J","Zeltins A","Kazaks A","Kotelovica S","Leonciks A","Sharipo J","Viksna A","Kuka J","Liepinsh E","Dambrova M."],"DOI_URL":"http://dx.doi.org/10.1016/j.bbrc.2010.06.121"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":122,"interactions":0,"matches":11424,"pathways":0,"proteins":11413,"proteomes":7190,"sets":0,"structural_models":{"alphafold":8604},"structures":19,"taxa":14088},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":130,"alignment:full":7259},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"3luu","name":"Crystal structure of Protein with unknown function which belongs to Pfam DUF971 family (AFE_2189) from Acidithiobacillus ferrooxidans ATCC 23270 at 1.93 A resolution"}}}