ID   PHM5_PYRSX              Reviewed;         366 AA.
AC   A0A2Z5XAK6;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2018, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=Methyltransferase phm5 {ECO:0000303|PubMed:29972614};
DE            EC=2.1.1.- {ECO:0000269|PubMed:29972614};
DE   AltName: Full=Phomasetin biosynthesis cluster protein 5 {ECO:0000303|PubMed:29972614};
GN   Name=phm5 {ECO:0000303|PubMed:29972614};
OS   Pyrenochaetopsis sp.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pyrenochaetopsidaceae;
OC   Pyrenochaetopsis; unclassified Pyrenochaetopsis.
OX   NCBI_TaxID=1756125;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION
RP   PHENOTYPE, AND PATHWAY.
RC   STRAIN=RK10-F058;
RX   PubMed=29972614; DOI=10.1002/anie.201805050;
RA   Kato N., Nogawa T., Takita R., Kinugasa K., Kanai M., Uchiyama M.,
RA   Osada H., Takahashi S.;
RT   "Control of the stereochemical course of [4+2] cycloaddition during trans-
RT   decalin formation by Fsa2-family enzymes.";
RL   Angew. Chem. Int. Ed. 57:9754-9758(2018).
RN   [2]
RP   FUNCTION.
RX   PubMed=34121297; DOI=10.1002/anie.202106186;
RA   Fujiyama K., Kato N., Re S., Kinugasa K., Watanabe K., Takita R.,
RA   Nogawa T., Hino T., Osada H., Sugita Y., Takahashi S., Nagano S.;
RT   "Molecular basis for two stereoselective Diels-Alderases that produce
RT   decalin skeletons*.";
RL   Angew. Chem. Int. Ed. 60:22401-22410(2021).
CC   -!- FUNCTION: Methyltransferase; part of the gene cluster that mediates the
CC       biosynthesis of the trans-fused decalin-containing tetramic acid
CC       phomasetin, the stereochemical opposite of the HIV-1 integrase
CC       inhibitor equisetin (PubMed:29972614). The PKS module of phm1 together
CC       with the enoylreductase phm4 catalyze the formation of the polyketide
CC       unit which is then conjugated to L-serine by the condensation domain of
CC       the phm1 NRPS module (PubMed:29972614). Activity of the Dieckmann
CC       cyclase domain (RED) of phm1 results in release of the Dieckmann
CC       product intermediate (PubMed:29972614). The Diels-Alderase phm7 then
CC       uses the Dieckmann product of phm1 as substrate and catalyzes the
CC       Diels-Alder cycloaddition to form the decalin ring of N-
CC       desmethylphomasetin (PubMed:29972614, PubMed:34121297). N-
CC       desmethylphomasetin is further methylated to phomasetin by the
CC       methyltransferase phm5 (PubMed:29972614). {ECO:0000269|PubMed:29972614,
CC       ECO:0000269|PubMed:34121297}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:29972614}.
CC   -!- DISRUPTION PHENOTYPE: Impairs the production of phomasetin but
CC       accumulates N-desmethylphomasetin. {ECO:0000269|PubMed:29972614}.
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; LC361337; BBC43188.1; -; Genomic_DNA.
DR   SMR; A0A2Z5XAK6; -.
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   PIRSF; PIRSF005739; O-mtase; 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..366
FT                   /note="Methyltransferase phm5"
FT                   /id="PRO_0000453344"
FT   BINDING         204..205
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O04385"
FT   BINDING         230
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         255..256
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O04385"
FT   BINDING         273
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O04385"
FT   BINDING         274
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   366 AA;  40640 MW;  2C7E952F7EBA0B52 CRC64;
     MAVKSSTVDV RAALQSAGAH YMNLIEFGIL KVFIDHQIFD HIPAEGSISV TDLATRTKAE
     VSLLQRFSDY LVASEVLASP APHELAHTTR SLSYRSEEIA AGFVSHVYHF FLRPMATWTA
     YFEENGLREP KDAKTIPLGL ATGHPEEDLY GVLDKEPRLA YMFNVAQARS AAIFPMKGLY
     DFAWLREALE DHIGAESPAI VDIGGSHGLA LKELLAENPF IPSKRCAVLD FPQTVEQAQQ
     NLDEDLRDIH FIGGSMLEPL PVALHAAGIY QFRRVLSDFV DKDIILALEQ VRRVCAPYSR
     VLIIEELVKA SRDKFAIAQD ISVLNFGGKR RSEADWHQLA SQAGLQVRHV FEQTETAFAV
     VELGLA