ID   PYTC_ASPTE              Reviewed;         324 AA.
AC   P9WEZ3; A0A5M3YT69;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   12-AUG-2020, sequence version 1.
DT   03-AUG-2022, entry version 7.
DE   RecName: Full=Methyltransferase pytC {ECO:0000303|PubMed:32077283};
DE            EC=2.1.1.- {ECO:0000305|PubMed:32077283};
DE   AltName: Full=Pyranterreones biosynthesis cluster protein C {ECO:0000303|PubMed:32077283};
GN   Name=pytC {ECO:0000303|PubMed:32077283};
GN   ORFNames=ATEG_00912, ATETN484_0003083300;
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].
RC   STRAIN=TN-484;
RA   Kanamasa S., Takahashi H.;
RT   "Aspergillus terreus TN-484 whole genome shotgun sequence.";
RL   Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, FUNCTION, DISRUPTION
RP   PHENOTYPE, AND PATHWAY.
RC   STRAIN=MEFC01;
RX   PubMed=32077283; DOI=10.1021/acs.jnatprod.9b01140;
RA   Tang S., Zhang W., Li Z., Li H., Geng C., Huang X., Lu X.;
RT   "Discovery and characterization of a PKS-NRPS hybrid in Aspergillus terreus
RT   by genome mining.";
RL   J. Nat. Prod. 83:473-480(2020).
CC   -!- FUNCTION: Methyltransferase; part of the gene cluster that mediates the
CC       biosynthesis of pyranterreones, a family of antioxidative compounds
CC       (PubMed:32077283). The first step of pyranonigrins biosynthesis is
CC       performed by the hybrid PKS-NRPS synthetase pytA that condenses 4
CC       malonyl-CoA units ato the acetyl starter unit by the modular PKS of
CC       pytA (PubMed:32077283). The acyl chain is then connected to an L-serine
CC       through the amide bond by the modular NRPS of pytA (PubMed:32077283). A
CC       tetramic acid is formed and released from the PKS-NRPS pytA to give
CC       pyranterreone 5 with the help of the thioesterase pytI
CC       (PubMed:32077283). Pyranterreone 5 could be methylated by pytC to
CC       afford pyranterreone 6 (Probable). Both pyranterreones 5 and 6 are
CC       subsequently oxidized by the FAD-linked oxidoreductase pytB and the
CC       cytochrome P450 monooxygenase pytD to form the fused gamma-pyrone core,
CC       resulting in pyranterreones 7 and 11, respectively (PubMed:32077283).
CC       The hydroxy group at C-8 of pyranterreones 7 and 11 are dehydrated by
CC       the aspartyl protease pytH to form a delta-7 double bond to give
CC       pyranterreones 3 and 1, 2 accordingly (PubMed:32077283). The exo-
CC       methylene of pyranterreone 3 could be reduced into a pendant methyl by
CC       reductase pytE to provide pyranterreone 4, also known as cordylactam
CC       (Probable). Pyranterreone 4 can be reconverted to pyranterreone 3
CC       through pytB-catalyzed dehydrogenation or further oxidized to
CC       pyranterreones 9 and 10 (Probable). {ECO:0000269|PubMed:32077283,
CC       ECO:0000305|PubMed:32077283}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:32077283}.
CC   -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC       transcription factor pytR. {ECO:0000269|PubMed:32077283}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes the production of most pyranterreones,
CC       but accumulates pyranterreone 5. {ECO:0000269|PubMed:32077283}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. LaeA
CC       methyltransferase family. {ECO:0000305}.
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DR   EMBL; BKZM02000003; GES59607.1; -; Genomic_DNA.
DR   EMBL; MN699962; QIH14020.1; -; Genomic_DNA.
DR   AlphaFoldDB; P9WEZ3; -.
DR   SMR; P9WEZ3; -.
DR   VEuPathDB; FungiDB:ATEG_00912; -.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..324
FT                   /note="Methyltransferase pytC"
FT                   /id="PRO_0000450468"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   324 AA;  36850 MW;  6BEFDE06550AF082 CRC64;
     MTVRTAAEPP NRIEVDMDAP SLDTDSSCTS LSSSVQRYEY KHGRRYHGYH AGSYPFPNDK
     REQDRLDMIH HLYTRILNDR LFLAPLDPRG KAILDIGTGT GIWALHMGDA HPAARLIVGN
     DLSPIQPSWA PANVRFVVDD VEKDWVDRHP YDFIHCRYMA GSIKDWPRLI RQCYAHLRPG
     GWLELQESVN VMYSEDGTLP PDSFMARMMH GLIVACEKIG RTMDPAPSME KWVQEAGFDP
     ITKHRFKIPV GSWPKDPRLK ECGSLMRVNF VEGVEAFTAS LFTEVLGWTP EEVAVLNTGV
     REEAMRNDIH AIFDFVVIVA QKPY