ID   SOL2_ALTSO              Reviewed;         427 AA.
AC   D7UQ43;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=O-methyltransferase sol2 {ECO:0000303|PubMed:20486243};
DE            EC=2.1.1.- {ECO:0000255|PROSITE-ProRule:PRU01020};
DE   AltName: Full=Solanapyrone biosynthesis protein 2 {ECO:0000303|PubMed:20486243};
GN   Name=sol2;
OS   Alternaria solani.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Porri.
OX   NCBI_TaxID=48100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=20486243; DOI=10.1002/cbic.201000173;
RA   Kasahara K., Miyamoto T., Fujimoto T., Oguri H., Tokiwano T., Oikawa H.,
RA   Ebizuka Y., Fujii I.;
RT   "Solanapyrone synthase, a possible Diels-Alderase and iterative type I
RT   polyketide synthase encoded in a biosynthetic gene cluster from Alternaria
RT   solani.";
RL   ChemBioChem 11:1245-1252(2010).
RN   [2]
RP   FUNCTION.
RX   PubMed=9659400; DOI=10.1016/s0167-4838(98)00040-5;
RA   Katayama K., Kobayashi T., Oikawa H., Honma M., Ichihara A.;
RT   "Enzymatic activity and partial purification of solanapyrone synthase:
RT   first enzyme catalyzing Diels-Alder reaction.";
RL   Biochim. Biophys. Acta 1384:387-395(1998).
RN   [3]
RP   FUNCTION.
RX   PubMed=18256508; DOI=10.1271/bbb.70600;
RA   Katayama K., Kobayashi T., Chijimatsu M., Ichihara A., Oikawa H.;
RT   "Purification and N-terminal amino acid sequence of solanapyrone synthase,
RT   a natural Diels-Alderase from Alternaria solani.";
RL   Biosci. Biotechnol. Biochem. 72:604-607(2008).
CC   -!- FUNCTION: O-methyltransferase; part of the gene cluster that mediates
CC       the biosynthesis of the phytotoxin solanapyrone, a causal agent of
CC       early blight disease of potato and tomato (PubMed:20486243). The
CC       prosolanapyrone synthase sol1 is a polyketide synthase that produces
CC       the octaketide desmethylprosolanapyrone I via sequential condensations
CC       of 7 malonyl-CoA units with one acetyl-CoA unit, and one methylation
CC       step (PubMed:20486243). The octaketide backbone is further methylated
CC       by the sol2 O-methyltransferase to yield prosolanapyrone I
CC       (PubMed:20486243). Prosolanapyrone I is hydroxylated to prosolanapyrone
CC       II by the cytochrome P450 monooxygenase sol6 (PubMed:20486243). The
CC       solanapyrone synthase sol5 then catalyzes the oxidation of
CC       prosolanapyrone II and the subsequent Diels Alder cycloisomerization of
CC       the product prosolanapyrone III to solanapyrones A and D
CC       (PubMed:9659400, PubMed:18256508). Solanapyrones A and D are then
CC       converted into solanapyrones B and E, respectively, by the sol3
CC       dehydrogenase (PubMed:20486243). {ECO:0000269|PubMed:18256508,
CC       ECO:0000269|PubMed:20486243, ECO:0000269|PubMed:9659400}.
CC   -!- PATHWAY: Phytotoxin biosynthesis. {ECO:0000305|PubMed:20486243}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family. COMT
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AB514562; BAJ09788.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7UQ43; -.
DR   SMR; D7UQ43; -.
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; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..427
FT                   /note="O-methyltransferase sol2"
FT                   /id="PRO_0000438552"
FT   ACT_SITE        327
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         281
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   427 AA;  46803 MW;  E7D7313CFAC1A07F CRC64;
     MALKSTNGTH AGPTASAASL ASLAANISEK AASLSTYLES QGHAQPSFLP GCADPPETEE
     YLALHTSLTS SLEDLQRLVD GPRRSLRPFI MIGNDLAALQ VAFDFGFFQL IPPEGSMDVE
     TLAHKVGIDA DRTARVLRML ATHRIFVEPK PGFFAHTAAS AVFHDDEELR CAGHYMLDEC
     FKAATACSDC IKASPNDSDS THSPFNTYFG VPMFSYYEQN PQFAARFAKA MAVDRQIAEL
     RDCFPWGDIK GTVVDVGGGS GHISMALARN FPKLDFIVQD DSEKMLAQGR ARNLSDIEGR
     ISFMKHSFFH PQPIGGAGAF FIRQCTHNWC DRDVVKILKS FVPGLENSAP GTPLLINDTV
     LPVPGSKPLH EERALRQMDM LMFVVLGAKQ RTAKEFEALL KEADARYEIR RVHADGSMGL
     VEVHLNI