{"metadata":{"accession":"PF02579","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR003731","hierarchy":null,"name":{"name":"Dinitrogenase iron-molybdenum cofactor","short":"Nitro_FeMo-Co"},"description":[{"text":"<p>This family contains several NIF (B, Y and X) proteins which are iron-molybdenum cofactors (FeMo-co) in the dinitrogenase enzyme which catalyses the reduction of dinitrogen to ammonium. Dinitrogenase is a hetero-tetrameric (alpha(2)beta(2)) enzyme which contains the iron-molybdenum cofactor (FeMo-co) at its active site [[cite:PUB00019929]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00019929":{"PMID":11823455,"ISBN":null,"volume":"277","issue":"16","year":2002,"title":"Cloning and mutational analysis of the gamma gene from Azotobacter vinelandii defines a new family of proteins capable of metallocluster binding and protein stabilization.","URL":null,"raw_pages":"14299-305","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Rubio LM","Rangaraj P","Homer MJ","Roberts GP","Ludden PW."],"DOI_URL":"http://dx.doi.org/10.1074/jbc.M107289200"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":44,"interactions":0,"matches":7998,"pathways":0,"proteins":7977,"proteomes":3175,"sets":0,"structural_models":{"alphafold":6020},"structures":12,"taxa":5973},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":120,"alignment:full":4784},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"2qtd","name":"Crystal structure of a putative dinitrogenase (mj0327) from methanocaldococcus jannaschii dsm at 1.70 A resolution"}}}