ID   PGMB_ASPTE              Reviewed;         442 AA.
AC   A0A1W5SMT6;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2017, sequence version 1.
DT   03-AUG-2022, entry version 15.
DE   RecName: Full=O-methyltransferase pgmB {ECO:0000303|PubMed:35351612};
DE            EC=2.1.1.- {ECO:0000269|PubMed:35351612};
DE   AltName: Full=Pigmented naphthoquinones biosynthesis cluster protein B {ECO:0000303|PubMed:35351612};
GN   Name=pgmB {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, CATALYTIC ACTIVITY, 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: O-methyltransferase; part of the gene cluster that mediates
CC       the 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). Specifically
CC       methylates position C-6 of the pgmA product 3-acetonyl-1,6,8-
CC       trihydroxy-2-naphthaldehyde to yield fusarubinaldehyde
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: Abolished completely the production of the
CC       naphthoquinones derived pigments and leads to the accumulation of four
CC       new compounds which lack the O-methyl group, including 6-O-demethyl-5-
CC       deoxyanhydrofusarubin and 6-O-demethyl-5-deoxyfusarubin.
CC       {ECO:0000269|PubMed:35351612}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; KX470747; ARB51364.1; -; mRNA.
DR   VEuPathDB; FungiDB:ATEG_06203; -.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR016461; COMT-like.
DR   InterPro; IPR001077; O_MeTrfase_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00891; Methyltransf_2; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51683; SAM_OMT_II; 1.
PE   1: Evidence at protein level;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..442
FT                   /note="O-methyltransferase pgmB"
FT                   /id="PRO_0000456003"
FT   ACT_SITE        341
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         291
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   442 AA;  48316 MW;  E8A191D70D8975E6 CRC64;
     MTPYSSAADL GSTVSPLEGL SSVITKNTSI VSQYLQANNL PQPSPEANGP VVVLPSDAPQ
     DVQQARQQLI AASLEIFQLA IGPSEFLPHL ATNFQYISCL TWLAHYDIFH LVPRDKNISY
     ADLARATGVP EQRLKSILRM AMTSSLFREH PNGTDVGHSA VSALLASDDD AYSYATYMCS
     KTAPMAMSMT EAHKRWGAST RTNETAYNVA FNTELPLFDD LAQNKARMGE FARYMRSVRS
     SETVALKHLV SGVDWESIPA GGMLVDVGGS TGGAAIALAQ AYPHIRFTIQ DLPENVETGE
     KAAAASLPAD IASRLTFQAH DFTLPQPVRA ADAYLLRMIL HDWPDEQAVK ILRNIVTAME
     ETKSRLFIMD TVLPKPGSVP VSVERIARAR DLTMIQSFNS KERELDEWKE LITAADPRLQ
     LIAVTQPLGS AMSILEIQLS AK