ID   OMT_ASPNA               Reviewed;         195 AA.
AC   G3XNF3;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=O-methyltransferase {ECO:0000303|PubMed:32159958};
DE            Short=OMT {ECO:0000303|PubMed:32159958};
DE            EC=2.1.1.- {ECO:0000269|PubMed:32159958};
DE   AltName: Full=Pyrophen biosynthesis cluster protein OMT {ECO:0000303|PubMed:32159958};
GN   Name=OMT {ECO:0000303|PubMed:32159958}; ORFNames=ASPNIDRAFT_41845;
OS   Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS   NCTC 3858a / NRRL 328 / USDA 3528.7).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=380704;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL
RC   328 / USDA 3528.7;
RX   PubMed=21543515; DOI=10.1101/gr.112169.110;
RA   Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.I.,
RA   Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA   Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA   van Dijck P.W.M., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA   Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.J.,
RA   Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA   Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA   Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA   Martinez D., van Peij N.N.M.E., Roubos J.A., Nielsen J., Baker S.E.;
RT   "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT   versus enzyme-producing CBS 513.88.";
RL   Genome Res. 21:885-897(2011).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=32159958; DOI=10.1021/acs.jnatprod.9b00989;
RA   Hai Y., Huang A., Tang Y.;
RT   "Biosynthesis of Amino Acid Derived alpha-Pyrones by an NRPS-NRPKS Hybrid
RT   Megasynthetase in Fungi.";
RL   J. Nat. Prod. 83:593-600(2020).
CC   -!- FUNCTION: O-methyltransferase; part of the gene cluster that mediates
CC       the biosynthesis of pyrophen and campyrone B, which represent a class
CC       of fungal amino acid-derived alpha-pyrone natural products
CC       (PubMed:32159958). The first step of pyrophen biosynthesis is catalyzed
CC       by the PKS-NRPS hybrid synthetase ATPKS that uptakes and condensates L-
CC       phenylalanine and malonyl-CoA in order to produce
CC       desmethyldesacetylpyrophen (PubMed:32159958). Although the A domain
CC       does not discriminate between 2 enantiomeric phenylalanines, the
CC       downstream KS domain must play a gate keeping role to stereoselectively
CC       accept the L-phenylalanyl-S-phosphopantetheine (Ppant)-T domain
CC       intermediate for chain elongation (PubMed:32159958). The resulting
CC       amino acid derived diketide is off-loaded through lactonization to
CC       yield the alpha-pyrone intermediate desmethyldesacetylpyrophen
CC       (PubMed:32159958). The cluster-specific O-methyltransferase (OMT) then
CC       methylates desmethyldesacetylpyrophen to desacetylpyrophen, which is
CC       further acetylated to pyrophen by an endogenous yet unidentified N-
CC       acetyltransferase (PubMed:32159958). ATPKS has relaxed substrate
CC       specificity to activate and extend branched-chain amino acid L-leucine
CC       to produce small amounts of campyrone B (PubMed:32159958).
CC       {ECO:0000269|PubMed:32159958}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:32159958}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000255}.
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DR   EMBL; ACJE01000002; EHA27897.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3XNF3; -.
DR   SMR; G3XNF3; -.
DR   EnsemblFungi; EHA27897; EHA27897; ASPNIDRAFT_41845.
DR   HOGENOM; CLU_046029_0_0_1; -.
DR   Proteomes; UP000009038; Unassembled WGS sequence.
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; IPR013217; Methyltransf_12.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF08242; Methyltransf_12; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   Methyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..195
FT                   /note="O-methyltransferase"
FT                   /id="PRO_0000452990"
SQ   SEQUENCE   195 AA;  21666 MW;  0F35F16954A2C35E CRC64;
     MGQSHLDIGV GTGYYPAKSL KAGAKCTEIT LLDLSPNSLQ ATEQRILETV GREAVRVNTV
     VASALEPLPF DKAKKFNSIS VFFLLHCMPG TPEEKCKLFD VVRPHLAEDG VLVGTTVLGQ
     GVPINWLGQK MMNSYNNNTK SFHNSEDNKA QFDEGLRRNF EEVDSWIMGQ VMLFKARKPR
     QQDAITNVVP KDNLD