STTC_ASPTE
ID STTC_ASPTE Reviewed; 299 AA.
AC P9WEV4;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 12-AUG-2020, sequence version 1.
DT 25-MAY-2022, entry version 4.
DE RecName: Full=Ophiobolin family sesterterpenoid biosynthesis cluster acetyltransferase {ECO:0000303|PubMed:28604695};
DE EC=2.3.1.- {ECO:0000305|PubMed:28604695};
DE Flags: Precursor;
OS Aspergillus terreus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=33178;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 20542 / MF4845;
RX PubMed=28604695; DOI=10.1038/nchembio.2408;
RA Clevenger K.D., Bok J.W., Ye R., Miley G.P., Verdan M.H., Velk T., Chen C.,
RA Yang K., Robey M.T., Gao P., Lamprecht M., Thomas P.M., Islam M.N.,
RA Palmer J.M., Wu C.C., Keller N.P., Kelleher N.L.;
RT "A scalable platform to identify fungal secondary metabolites and their
RT gene clusters.";
RL Nat. Chem. Biol. 13:895-901(2017).
CC -!- FUNCTION: Acetyltransferase; part of the gene cluster that mediates the
CC biosynthesis of an ophiobolin family sesterterpenoid.
CC {ECO:0000269|PubMed:28604695}.
CC -!- FUNCTION: Sesterterpenoid synthase; part of the gene cluster that
CC mediates the biosynthesis of an ophiobolin family sesterterpenoid.
CC {ECO:0000269|PubMed:28604695}.
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|PubMed:28604695}.
CC -!- SIMILARITY: Belongs to the bfoA family. {ECO:0000305}.
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DR EMBL; KX449366; AQM58280.1; -; Genomic_DNA.
DR AlphaFoldDB; P9WEV4; -.
DR VEuPathDB; FungiDB:ATEG_03569; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
PE 3: Inferred from homology;
KW Acyltransferase; Glycoprotein; Signal; Transferase.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..299
FT /note="Ophiobolin family sesterterpenoid biosynthesis
FT cluster acetyltransferase"
FT /id="PRO_0000450610"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 299 AA; 33650 MW; 5FC7C13C5F4EFC3B CRC64;
MYFFRALLSP VVLWPALVSG KSNSNTANYT VEELWDLEVT FWDNFLYPAN VKQVEAINST
LFTTEVQGRV DITRVFNGSE LNTEYIFGLF SDPNHLSLVG VPIAYSITQF IAERNIASAT
TVVTFNATSF GNLLLPVTID TWIMWDANGR IMQYDATFRW FGFLLDTLVE ALATSINGTA
SQATAALTQL LATTVCDTHD KYCTGENQQY DNSTACYDFL TTAIPLGKDY ELGRDTLLCR
EVHEHMVQYD PKMHCPHIGP TGGDYCVNDQ TYEQKVLQKY FNVSWIVGVP WTGNIWLGD