An L-tyrosine:2-oxoglutarate aminotransferase (probably invD) and atromentin synthetase invA1 catalyze consecutive steps to turn over L-tyrosine into atromentin, which represents the generic precursor molecule for the entire terphenylquinone and pulvinic acid family of pigments, which are widely distributed secondary metabolites in homobasidiomycetes. The first step catalyzed by the aminotransferase converts L-tyrosine in to 4-hydroxyphenylpyruvate (4-HPP). Adenylation of two 4-HPP monomers by the invA1 adenylation (A) domain, covalent tethering of the monomers as a thioester and oxoester onto the invA1 thiolation (T) and thioesterase (TE) domains, respectively, and symmetric C-C-bond formation between two monomers catalyzed by the invA1 TE domain leads to atromentin.

Belongs to the ATP-dependent AMP-binding enzyme family.

959 amino acids

MSPVATTTSVTPDVISSLKTSFSAGQTSYIPSTLFDVLSYAAERYPSHELGFITSSAHDSSIQTKTFSLFNAQVRNLGRALLDLNKPAGSIIVVYLTEHEDNMAAVWACLLAGYVPCLQPALSAQQAHKEGHVAHIKNLFGSATWLTNEAGAEQVSSIAGLEIHLLSELKIAAEGYSVSADWTARTVQPDDEAILFLTSGSTGFSKAVVHTHRTILAACYAKGEAYGLTSESNILNWVGFDHVAGSLEMHIAPLLYGASQLHVHASAILSDPLRFLQLIDEKSINVAFAPNFLLAKLTRDLEKKTELFGSFDLSSVTRINSGGEAVVSKTAKAFVATLKNLSRDPSKVSFVISPGFGMTETCAGCIYNPADVSTSEPNYEFLELGTPITGCEMRIVNPEDGVTPRVDGESGELQVRGPMVFSRYYNNAEATASSFVEGGWYRTGDVGIVENGVMRLSGRIKETVIVHGVSYGIPELETYLQTVEGVTHSFLAAAPYRAPGQETEGFIIFYAPTFDLYGEDASSKLFATHRALRDISVKMITLPPQHIVPIPVNQMEKTTLGKLSRARLTGLFKQGELAKHIARAEELLSEARGASFVTPQTETEQTLAAIYAGIFNLEVADVSATDNFFELGGTSIDVIRLKREGEAAFDLPEIPTIQILKHPVVSSLANYIVALKTKGVNAEEYDPIVPLQLTGKKTPIFMVHPGVGEVLIFVNLAKYFQNERPFYALRARGFEPGQPFFTSMDEMVSCYAAAVKRTQAHGPYAIAGYSYGGVVAFEVAKRLEAMGEEVKFTGLINIPPHIADRMHEIDWTGGMLNLSYFLGLVSKQDANDLAPSMRPLTRKEQLEIVWKLSPPERLVELQLTPEKLDHWVDIAGSLIECGKEYNPGGSVSALDVFYAIPLRGSKEDWLNKQLKPWEEFSRGATSYTDVPGQHYTLMDFDHVPGFQKIFRSRLEARGL

104.9 kDa

(Note: Representative image - actual molecular weight may vary depending on tag type and expression method)

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