ID   PGME_ASPTE              Reviewed;         335 AA.
AC   A0A1W5SKE9;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2017, sequence version 1.
DT   03-AUG-2022, entry version 9.
DE   RecName: Full=Methyltransferase pgmE {ECO:0000303|PubMed:35351612};
DE            EC=2.1.1.- {ECO:0000305|PubMed:35351612};
DE   AltName: Full=Pigmented naphthoquinones biosynthesis cluster protein E {ECO:0000303|PubMed:35351612};
GN   Name=pgmE {ECO:0000303|PubMed:28471414};
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], IDENTIFICATION, FUNCTION, AND INDUCTION.
RC   STRAIN=MUCL38669;
RX   PubMed=28471414; DOI=10.3390/microorganisms5020022;
RA   Palonen E.K., Raina S., Brandt A., Meriluoto J., Keshavarz T., Soini J.T.;
RT   "Melanisation of Aspergillus terreus-is butyrolactone I involved in the
RT   regulation of both DOPA and DHN types of pigments in submerged culture?";
RL   Microorganisms 5:0-0(2017).
RN   [2]
RP   FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=35351612; DOI=10.1016/j.fgb.2022.103690;
RA   Tang S., Men P., Zhang W., Li H., Li Z., Huang X., Lu X.;
RT   "Identification of a polyketide biosynthesis gene cluster by
RT   transcriptional regulator activation in Aspergillus terreus.";
RL   Fungal Genet. Biol. 160:103690-103690(2022).
CC   -!- FUNCTION: Methyltransferase; part of the gene cluster that mediates the
CC       biosynthesis of pleosporalin A, ascomycone A, as well as a third
CC       cryptic naphthoquinone derived pigment, all responsible for the
CC       coloration of conidia (PubMed:28471414, PubMed:35351612). Essential for
CC       the production of pleosporalin A, but not the 2 other final products
CC       (PubMed:35351612). The pathway begins with the biosynthesis of the
CC       cyclized heptaketide 3-acetonyl-1,6,8-trihydroxy-2-naphthaldehyde by
CC       the NR-PKS pgmA. The C-6 hydroxyl group is further methylated by the O-
CC       methyltransferase pgmB to yield fusarubinaldehyde which is in turn
CC       oxidized by the cytochrome P450 monooxygenase pgmC at C-9. The C-1
CC       hydroxyl group is then methylated spontaneously. Although pgmE, pgmD
CC       and pgmH are essential for the production of pleosporalin A, it is not
CC       the case for the 2 other final products and it remains difficult to
CC       assign a specific function to each enzyme. PgmF and pgmG seem not to be
CC       involved in pigment biosynthesis although they were regulated by the
CC       cluster-specific transcription factor pgmR (PubMed:35351612)
CC       (Probable). {ECO:0000269|PubMed:28471414, ECO:0000269|PubMed:35351612,
CC       ECO:0000305|PubMed:35351612}.
CC   -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:35351612}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:35351612}.
CC   -!- INDUCTION: Expression is significantly up-regulated at the end of late
CC       growth phase, in the presence of Butyrolactone I (PubMed:28471414).
CC       Expression is positively regulated by the pgm cluster-specific
CC       transcription factor pgmR (PubMed:35351612).
CC       {ECO:0000269|PubMed:28471414, ECO:0000269|PubMed:35351612}.
CC   -!- DISRUPTION PHENOTYPE: Does not affect the methylation of the
CC       naphthoquinones derived pigments and only abolishes the production of
CC       pleosporalin A but not of the 2 other final products.
CC       {ECO:0000269|PubMed:35351612}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; KX470749; ARB51366.1; -; mRNA.
DR   VEuPathDB; FungiDB:ATEG_06208; -.
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; IPR041698; Methyltransf_25.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF13649; Methyltransf_25; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..335
FT                   /note="Methyltransferase pgmE"
FT                   /id="PRO_0000456009"
SQ   SEQUENCE   335 AA;  37741 MW;  ED13EF01DAE2C232 CRC64;
     MAETATRSDS GMFWKATTYK EQYWDGYLAA RPKYSSDFYE RIVDYYKAHN PSPPTPTVAH
     DVGTGPGQVA SELCKYFDKV IASDPNSTHL AVASARNEKS GLNHKITWTE VSAEDLNSHY
     PAGSASFLAA AECLPLLDVP RALNTFAHLL HPNGTLAAWF YGRPVFSEPT VAAKCQPILN
     DIIDLTFEKV IKGAPPAHKT TWKRSTDTLY SFLDNVTFPA ETWRDVYRFK WNPHLPLSVV
     GPNACDYPIE PSSCIDPERE KVVEAKDPHF WEEVWDISEV RRFVECLLPN IEDLKSKGVY
     DHVEVKYKEL EEAMGGDNAK KEITWPVVLI LATRV