"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"
"Q4WF29"	"{'domain_architectures': 63653, 'entries': 7, 'isoforms': 0, 'proteomes': 1, 'sets': 1, 'structures': 5, 'taxa': 1, 'dbEntries': {'ssf': 1, 'cathgene3d': 1, 'pfam': 1, 'panther': 1, 'interpro': 3}, 'proteome': 1, 'taxonomy': 1, 'similar_proteins': 63653}"	"['Displays specific triacetylfusarinine C (TAFC) esterase activity but does not hydrolyze fusarinine C, which has the same core structure as TAFC (PubMed:17586718, PubMed:30070018). Hydrolysis optimizes but is not essential for TAFC-mediated iron uptake (PubMed:17586718). Both extra- and intracellular siderophores have been shown to be crucial for the virulence (PubMed:17586718). Subsequent to chelation of iron and uptake, FsC and TAFC are hydrolyzed and the iron is transferred to the metabolism or to the intracellular siderophore ferricrocin (FC) for transport and storage of iron (PubMed:17586718). Hydrolyzes both TAFC and DF-TAFC with equal efficiencies, suggesting that its function might not be restricted to the release of iron from the siderophore but might also include the degradation of the iron-free chelator to protect cells (PubMed:17586718)']"	"estB"	""	"ESTB_ASPFU"	"9db87eed00e5bc39adf7846218077296416adf32"	True	False	False	292	"Siderophore triacetylfusarinine C esterase"	1	"UP000002530"	"MGDRPTPVPLPNSEQFYLENDRGEPYLIQVSWPLHWEDKQTGRGPLPIIYIVDGNALFLTATEAAWRRAAASHFAGGGIIVAIGYPLKGKLYDARRRSFDLTPPTACAPVGYGGADVFLDFIENSVRPAVQARFPQVSLAREALYGHSYGGLLALHALFTRPQSFDCYIASSPSIWWNSLCILHEAKAFVETKKVSHDQSPSLMVSWGSWEQHPPRWADELLDHYEARKRTAAELRMADNALDLCAMLHGCSRLHALIKTEYEGEDHTSVMSCSVSRGLTMFFEDWPFHQSG"	"reviewed"	"{'taxId': '330879', 'scientificName': 'Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)', 'fullName': 'Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)'}"