{"metadata":{"accession":"PF12225","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR022026","hierarchy":null,"name":{"name":"Methylene-tetrahydrofolate reductase C terminal","short":"DUF5981"},"description":[{"text":"<p>This family is found in bacteria and archaea, and is approximately 100 amino acids in length. There is a conserved NGPCGG sequence motif. This family is the C terminal of methylene-tetrahydrofolate reductase. This protein reduces FAD using the reducing equivalents from reduced FAD, subsequently reduces tetrahydrofolate. The C terminal of MTHFR contains the FAD binding site and is the catalytic portion of the enzyme.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00052921":{"PMID":19610625,"ISBN":null,"volume":"48","issue":"32","year":2009,"title":"Functional role for the conformationally mobile phenylalanine 223 in the reaction of methylenetetrahydrofolate reductase from Escherichia coli.","URL":null,"raw_pages":"7673-85","medline_journal":"Biochemistry","ISO_journal":"Biochemistry","authors":["Lee MN","Takawira D","Nikolova AP","Ballou DP","Furtado VC","Phung NL","Still BR","Thorstad MK","Tanner JJ","Trimmer EE."],"DOI_URL":"http://dx.doi.org/10.1021/bi9007325"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":9,"interactions":0,"matches":1276,"pathways":0,"proteins":1276,"proteomes":1049,"sets":0,"structural_models":{"alphafold":864},"structures":0,"taxa":1917},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":75,"alignment:full":713},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}