"accession"	"counters"	"description"	"gene"	"go_terms"	"id"	"ida_accession"	"in_alphafold"	"in_bfvd"	"is_fragment"	"length"	"name"	"protein_evidence"	"proteome"	"sequence"	"source_database"	"source_organism"
"A5U079"	"{'domain_architectures': 23973, 'entries': 28, 'isoforms': 0, 'proteomes': 1, 'sets': 3, 'structures': 0, 'taxa': 1, 'dbEntries': {'cathgene3d': 1, 'profile': 1, 'ssf': 1, 'smart': 1, 'cdd': 2, 'pfam': 2, 'ncbifam': 2, 'sfld': 6, 'panther': 1, 'pirsf': 1, 'interpro': 10}, 'proteome': 1, 'taxonomy': 1, 'similar_proteins': 23973}"	"['Radical S-adenosylmethionine (SAM) enzyme responsible for the first step of the biosynthesis of the enzyme cofactor mycofactocin (MFT). Catalyzes two reactions at the C-terminus of the mycofactocin precursor (the MftA peptide). The first one is the oxidative decarboxylation of the C-terminal L-tyrosine of MftA, forming an unsaturated tyramine moiety. The second reaction is the cross-linking of the tyramine with the penultimate L-valine residue, forming a five-membered lactam ring. Its activity requires the presence of the MftB chaperone']"	"pqqE"	"[{'identifier': 'GO:0003824', 'name': 'catalytic activity', 'category': {'code': 'F', 'name': 'molecular_function'}}, {'identifier': 'GO:0051536', 'name': 'iron-sulfur cluster binding', 'category': {'code': 'F', 'name': 'molecular_function'}}]"	"A5U079_MYCTA"	"425f8febc6863d4a5a464e3e542f22b69146c258"	True	False	False	391	"Mycofactocin maturase MftC"	4	"UP000001988"	"MTSPVPRLIEQFERGLDAPICLTWELTYACNLACVHCLSSSGKRDPGELSTRQCKDIIDELERMQVFYVNIGGGEPTVRPDFWELVDYATAHHVGVKFSTNGVRITPEVATRLAATDYVDVQISLDGATAEVNDAIRGTGSFDMAVRALQNLAAAGFAGVKISVVITRRNVAQLDEFATLASRYGATLRITRLRPSGRGTDVWADLHPTADQQVQLYDWLVSKGERVLTGDSFFHLAPLGQSGALAGLNMCGAGRVVCLIDPVGDVYACPFAIHDHFLAGNVLSDGGFQNVWKNSSLFRELREPQSAGACGSCGHYDSCRGGCMAAKFFTGLPLDGPDPECVQGHSEPALARERHLPRPRADHSRGRRVSKPVPLTLSMRPPKRPCNESPV"	"unreviewed"	"{'taxId': '419947', 'scientificName': 'Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)', 'fullName': 'Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)'}"