{"metadata":{"accession":"IPR023467","entry_id":null,"type":"family","go_terms":[{"identifier":"GO:0008168","name":"methyltransferase activity","category":{"code":"F","name":"molecular_function"}},{"identifier":"GO:0006730","name":"one-carbon metabolic process","category":{"code":"P","name":"biological_process"}}],"source_database":"interpro","member_databases":{"pirsf":{"PIRSF004960":"N5-methyltetrahydromethanopterin--coenzyme M methyltransferase, subunit H/methyltransferase Mtx, subunit H"},"pfam":{"PF02007":"Tetrahydromethanopterin S-methyltransferase MtrH subunit"}},"integrated":null,"hierarchy":{"accession":"IPR023467","name":"Tetrahydromethanopterin S-methyltransferase, subunit H/Methyltransferase Mtx, subunit H","type":"Family","children":[{"accession":"IPR028342","name":"Tetrahydromethanopterin S-methyltransferase subunit H","type":"Family","children":[]}]},"name":{"name":"Tetrahydromethanopterin S-methyltransferase, subunit H/Methyltransferase Mtx, subunit H","short":"MeTrfase_MtrH/MtxH"},"description":[{"text":"<p>In archaea the enzyme tetrahydromethanopterin S-methyltransferase is composed of eight subunits, MtrA-H. The enzyme is a membrane- associated enzyme complex which catalyzes an energy-conserving, sodium-ion-translocating step in methanogenesis from hydrogen and carbon dioxide [[cite:PUB00005738]]. Subunit MtrH catalyzes the methylation reaction and was shown to exhibit methyltetrahydromethanopterin:cob(I)alamin methyltransferase activity [[cite:PUB00006446]].</p>\r\n<reaction>CH3-H4MPT + cob(I)alamin -->H4MPT + CH3-cob(III)alamin (H4MPT = tetrahydromethanopterin)</reaction>","llm":false,"checked":false,"updated":false},{"text":"<p>Methyltransferase MtxH from the archaea Methanosarcina may be part of a complex composed of 3 subunits; MtxA, MtxH and MtxX [[cite:PUB00027982]].</p>\n\n<p>This entry also includes methylcorrinoid:tetrahydrofolate methyltransferase (also known as [methyl-Co(III) glycine betaine-specific corrinoid protein]--tetrahydrofolate methyltransferase) from Desulfitobacterium hafniense, which in vitro catalyses the transfer of a methyl group from methylcobalamin to tetrahydrofolate.  In vivo this may permit anaerobic methylotrophic growth using glycine betaine [[cite:PUB00086416]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00027982":{"PMID":9461302,"ISBN":null,"volume":"250","issue":"3","year":1997,"title":"Identification of the active site histidine in the corrinoid protein MtrA of the energy-conserving methyltransferase complex from Methanobacterium thermoautotrophicum.","URL":null,"raw_pages":"783-8","medline_journal":"Eur J Biochem","ISO_journal":"Eur. J. Biochem.","authors":["Harms U","Thauer RK."],"DOI_URL":"http://dx.doi.org/10.1111/j.1432-1033.1997.00783.x"},"PUB00005738":{"PMID":7737157,"ISBN":null,"volume":"228","issue":"3","year":1995,"title":"The energy conserving N5-methyltetrahydromethanopterin:coenzyme M methyltransferase complex from Methanobacterium thermoautotrophicum is composed of eight different subunits.","URL":null,"raw_pages":"640-8","medline_journal":"Eur J Biochem","ISO_journal":"Eur. J. Biochem.","authors":["Harms U","Weiss DS","Gartner P","Linder D","Thauer RK."],"DOI_URL":"http://dx.doi.org/10.1111/j.1432-1033.1995.0640m.x"},"PUB00006446":{"PMID":10338124,"ISBN":null,"volume":"449","issue":"2-3","year":1999,"title":"The energy conserving methyltetrahydromethanopterin:coenzyme M methyltransferase complex from methanogenic archaea: function of the subunit MtrH.","URL":null,"raw_pages":"165-8","medline_journal":"FEBS Lett","ISO_journal":"FEBS Lett.","authors":["Hippler B","Thauer RK."],"DOI_URL":"http://dx.doi.org/10.1016/S0014-5793(99)00429-9"},"PUB00086416":{"PMID":25313086,"ISBN":null,"volume":"111","issue":"43","year":2014,"title":"A nonpyrrolysine member of the widely distributed trimethylamine methyltransferase family is a glycine betaine methyltransferase.","URL":null,"raw_pages":"E4668-76","medline_journal":"Proc Natl Acad Sci U S A","ISO_journal":"Proc. Natl. Acad. Sci. U.S.A.","authors":["Ticak T","Kountz DJ","Girosky KE","Krzycki JA","Ferguson DJ Jr."],"DOI_URL":"https://doi.org/10.1073/pnas.1409642111"}},"set_info":null,"overlaps_with":[{"accession":"IPR011005","name":"Dihydropteroate synthase-like superfamily","type":"homologous_superfamily"}],"counters":{"subfamilies":0,"domain_architectures":4,"interactions":0,"matches":502,"pathways":0,"proteins":502,"proteomes":224,"sets":0,"structural_models":{"alphafold":466,"bfvd":0},"structures":9,"taxa":623},"entry_annotations":{"alignment:seed":5,"alignment:full":148},"cross_references":{"gp":{"displayName":"Genome Properties","description":"Genome properties is an annotation system whereby functional attributes can be assigned to a genome, based on the presence of a defined set of protein signatures within that genome.","rank":45,"accessions":[{"accession":"GenProp0288","url":"https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp0288"},{"accession":"GenProp0722","url":"https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp0722"}]},"ec":{"displayName":"ENZYME","description":"ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.","rank":19,"accessions":[{"accession":"7.2.1.4","url":"https://enzyme.expasy.org/EC/7.2.1.4"}]}},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"6sj8","name":"Methyltransferase MtgA from Desulfitobacterium hafniense in complex with tetrahydrofolate"}}}