PGME_ASPTN
ID PGME_ASPTN Reviewed; 335 AA.
AC Q0CJC6;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 59.
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}; ORFNames=ATEG_06208;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP 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 [3]
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; CH476601; EAU33969.1; -; Genomic_DNA.
DR RefSeq; XP_001215386.1; XM_001215386.1.
DR STRING; 33178.CADATEAP00002977; -.
DR EnsemblFungi; EAU33969; EAU33969; ATEG_06208.
DR GeneID; 4321477; -.
DR VEuPathDB; FungiDB:ATEG_06208; -.
DR eggNOG; KOG3010; Eukaryota.
DR HOGENOM; CLU_049344_0_0_1; -.
DR OMA; WHSVERW; -.
DR OrthoDB; 899118at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
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; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..335
FT /note="Methyltransferase pgmE"
FT /id="PRO_0000456008"
SQ SEQUENCE 335 AA; 37771 MW; 1813FDE98552CD98 CRC64;
MAETATRSDS GMFWKATTYK EQYWDGYLAA RPKYSSDFYE RIVDYYKAHN PSPPTPTVAH
DVGTGPGQVA SELCKYFDKV IASDPNSTHL AVASARNEKS GLNHKITWTE VSAEDLNSHY
PAGSASFLAA AECLPLLDVP RALNTFAHLL HPNGTLAAWF YGRPVFSEPT VAAKCQPILN
DIIDLTFEKV IKGAPPAHKT TWKRSTDTLY SFLDNVAFPT ETWRDVYRFK WNPHLPLSVV
GPNACDYPIE PSSCIDPERE KVVEAKDPHF WEEVWDIFEV RRFVECLLPN IEELKSKGVY
DHVEVKYKEL EEAMGGANAK KEITWPVVLI LATRV
