ID   PYVH_ASPV1              Reviewed;         426 AA.
AC   A0A2V5HP22; A0A7M4B3T0;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   12-SEP-2018, sequence version 1.
DT   03-AUG-2022, entry version 16.
DE   RecName: Full=O-methyltransferase pyvH {ECO:0000303|PubMed:33117309};
DE            EC=2.1.1.- {ECO:0000305|PubMed:33117309};
DE   AltName: Full=Pyranoviolin A biosynthesis cluster protein H {ECO:0000303|PubMed:33117309};
GN   Name=pyvH {ECO:0000303|PubMed:33117309}; ORFNames=BO99DRAFT_447468;
OS   Aspergillus violaceofuscus (strain CBS 115571).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RX   PubMed=33117309; DOI=10.3389/fmicb.2020.562063;
RA   Wei X., Chen L., Tang J.W., Matsuda Y.;
RT   "Discovery of pyranoviolin A and its biosynthetic gene cluster in
RT   Aspergillus violaceofuscus.";
RL   Front. Microbiol. 11:562063-562063(2020).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115571;
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: O-methyltransferase; part of the gene cluster that mediates
CC       the biosynthesis of pyranoviolin A, a pyranonigrin analog with a C-3
CC       methoxy group (PubMed:33117309). Initially, the PKS portion of pyvA
CC       synthesizes C-10 carbon chain from 5 molecules of malonyl-CoA, which is
CC       then condensed with the thiolation (T) domain-bound glycine activated
CC       by the adenylation (A) domain (PubMed:33117309). The subsequent chain
CC       release by Dieckmann condensation (DKC) could be catalyzed by the TE
CC       domain present at the C-terminus of pyvA and/or the alpha/beta
CC       hydrolase pyvD, installing the tetramic acid moiety (Probable). The
CC       FAD-dependent monooxygenase pyvC next epoxidizes one of the olefins of
CC       the polyketide part, and the epoxide ring-opening induces the dihydro-
CC       gamma-pyrone ring formation (Probable). The cytochrome P450
CC       monooxygeanse pyvB would be responsible for the 2 consecutive
CC       reactions, in which the dihydro-gamma-pyrone is oxidized to gamma-
CC       pyrone and C-7 is hydroxylated to yield pyranonigrin F (Probable).
CC       Finally, the O-methyltransferase pyvH methylates the C-3 hydroxy group
CC       to complete the biosynthesis (Probable). {ECO:0000269|PubMed:33117309,
CC       ECO:0000305|PubMed:33117309}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:33117309}.
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; BR001648; FAA01298.1; -; Genomic_DNA.
DR   EMBL; KZ825234; PYI13687.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V5HP22; -.
DR   SMR; A0A2V5HP22; -.
DR   STRING; 1450538.A0A2V5HP22; -.
DR   Proteomes; UP000249829; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..426
FT                   /note="O-methyltransferase pyvH"
FT                   /id="PRO_0000452822"
FT   ACT_SITE        327
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         258..259
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O04385"
FT   BINDING         281
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         308..309
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O04385"
FT   BINDING         323
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O04385"
SQ   SEQUENCE   426 AA;  47949 MW;  5B90D0E2463B2381 CRC64;
     MASSRIVELA TRISENTAIV DAYLRENQLP SPSFDEDGPV DFAIQGEEVK KAHEEAIALS
     WELHRLLLGP SHFLRPVPNG LSLQAISKHD IATKVPVHGK ISYAALAQQC GLSEINTRRF
     VRYAIVHHRV FCEPQPGYVA HSAASRLLAE DPVMRDVLSH YLEECFPSFA MTLRAIDQFQ
     DNGEPNQTGW NLYHETQDAP WDYYETHPAM ARRFASTMAY ETEREGRSSN VLVEGYAWTS
     LLAETTATTT SPLVVDVGGS RGKTALEIAH AHPELTLLVQ DLPSMIEGAR DQLPAIPARE
     RVQFMAHDFF APQLVPADAY ILRHVFHNWS DRNAVRILRA LVPSLQPGAR LIVNDYIAPV
     PGVLSLAKEQ RLREMDLIML TLCNAYEREE QDWKRLFQEA DPRFHVRTMS VPKGATEGIL
     EVIWEG