"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"
"P62593"	"{'domain_architectures': 30140, 'entries': 13, 'isoforms': 0, 'proteomes': 0, 'sets': 1, 'structures': 78, 'taxa': 1, 'dbEntries': {'cathgene3d': 1, 'ssf': 1, 'pfam': 1, 'ncbifam': 2, 'panther': 1, 'prosite': 1, 'prints': 1, 'interpro': 5}, 'proteome': 0, 'taxonomy': 1, 'similar_proteins': 30140}"	"['TEM-type are the most prevalent beta-lactamases in enterobacteria; they hydrolyze the beta-lactam bond in susceptible beta-lactam antibiotics, thus conferring resistance to penicillins and cephalosporins. TEM-3 and TEM-4 are capable of hydrolyzing cefotaxime and ceftazidime. TEM-5 is capable of hydrolyzing ceftazidime. TEM-6 is capable of hydrolyzing ceftazidime and aztreonam. TEM-8/CAZ-2, TEM-16/CAZ-7 and TEM-24/CAZ-6 are markedly active against ceftazidime. IRT-4 shows resistance to beta-lactamase inhibitors']"	"blaT-6"	"[{'identifier': 'GO:0008800', 'name': 'beta-lactamase activity', 'category': {'code': 'F', 'name': 'molecular_function'}}, {'identifier': 'GO:0017001', 'name': 'antibiotic catabolic process', 'category': {'code': 'P', 'name': 'biological_process'}}, {'identifier': 'GO:0030655', 'name': 'beta-lactam antibiotic catabolic process', 'category': {'code': 'P', 'name': 'biological_process'}}, {'identifier': 'GO:0046677', 'name': 'response to antibiotic', 'category': {'code': 'P', 'name': 'biological_process'}}]"	"BLAT_ECOLX"	"4ab5c48e30574469cfafc0451da3679955b43a52"	True	False	False	286	"Beta-lactamase TEM"	1	""	"MSIQHFRVALIPFFAAFCLPVFAHPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRPEERFPMMSTFKVLLCGAVLSRVDAGQEQLGRRIHYSQNDLVEYSPVTEKHLTDGMTVRELCSAAITMSDNTAANLLLTTIGGPKELTAFLHNMGDHVTRLDRWEPELNEAIPNDERDTTMPAAMATTLRKLLTGELLTLASRQQLIDWMEADKVAGPLLRSALPAGWFIADKSGAGERGSRGIIAALGPDGKPSRIVVIYTTGSQATMDERNRQIAEIGASLIKHW"	"reviewed"	"{'taxId': '562', 'scientificName': 'Escherichia coli', 'fullName': 'Escherichia coli'}"