ID   SFMM3_STRLA             Reviewed;         334 AA.
AC   B0CN39;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=O-methyltransferase SfmM3 {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000305};
GN   Name=sfmM3 {ECO:0000303|PubMed:17981978};
OS   Streptomyces lavendulae.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1914 {ECO:0000312|EMBL:ABI22145.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NRRL 11002 {ECO:0000312|EMBL:ABI22145.1};
RX   PubMed=17981978; DOI=10.1128/jb.00826-07;
RA   Li L., Deng W., Song J., Ding W., Zhao Q.F., Peng C., Song W.W., Tang G.L.,
RA   Liu W.;
RT   "Characterization of the saframycin A gene cluster from Streptomyces
RT   lavendulae NRRL 11002 revealing a nonribosomal peptide synthetase system
RT   for assembling the unusual tetrapeptidyl skeleton in an iterative manner.";
RL   J. Bacteriol. 190:251-263(2008).
RN   [2]
RP   PATHWAY.
RX   PubMed=19494690; DOI=10.4014/jmb.0808.484;
RA   Fu C.Y., Tang M.C., Peng C., Li L., He Y.L., Liu W., Tang G.L.;
RT   "Biosynthesis of 3-hydroxy-5-methyl-o-methyltyrosine in the saframycin/
RT   safracin biosynthetic pathway.";
RL   J. Microbiol. Biotechnol. 19:439-446(2009).
RN   [3]
RP   IDENTIFICATION.
RX   PubMed=22187429; DOI=10.1074/jbc.m111.306316;
RA   Tang M.C., Fu C.Y., Tang G.L.;
RT   "Characterization of SfmD as a heme peroxidase that catalyzes the
RT   regioselective hydroxylation of 3-methyltyrosine to 3-hydroxy-5-
RT   methyltyrosine in saframycin A biosynthesis.";
RL   J. Biol. Chem. 287:5112-5121(2012).
CC   -!- FUNCTION: O-methyltransferase that mediates the methylation of 3-
CC       hydroxy-5-methyl-L-tyrosine (3-OH-5-Me-Tyr) into 3-hydroxy-5-methyl-O-
CC       methyltyrosine (3-OH-5-Me-OMe-Tyr), a core structure of saframycin A, a
CC       potent antitumor antibiotic that belongs to the tetrahydroisoquinoline
CC       family. {ECO:0000305|PubMed:22187429}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-hydroxy-3-methyl-L-tyrosine + S-adenosyl-L-methionine = 5-
CC         hydroxy-3-methyl-O-methyl-L-tyrosine + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:47752, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:78241,
CC         ChEBI:CHEBI:87846; Evidence={ECO:0000305|PubMed:22187429};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:19494690}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family. COMT
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR   EMBL; DQ838002; ABI22145.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0CN39; -.
DR   SMR; B0CN39; -.
DR   BioCyc; MetaCyc:MON-19338; -.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Antibiotic biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..334
FT                   /note="O-methyltransferase SfmM3"
FT                   /id="PRO_0000430697"
FT   ACT_SITE        236
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         190
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         216..218
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   334 AA;  35860 MW;  8452C0C476143D1E CRC64;
     MRRMLYAQLP SRALVVVAQL GIADILAEGP ADISTLAERT STDAVALARL LRGLAVFGVF
     EEGAEQVYSL TPLGEALTSG HPASALPSAT LVAGQFGAAW GDLLETVRTG QSPFERSRGV
     SLFTHMEQDE ELRAVFDDSQ GRGLALELDE ILRAIDFSAY PTVVDVGGSD GTFLRRILSA
     HPDISGIVFD LPGSTSLQAE RPTADPLEGR YSVATGDFFD SLPEGGDLYL LSHILHDWDD
     DRAVQILRTC RAAMSDDATL MVVDLIAANR GQRDERLHTA ALMDLYMLSL FGGNGGQERT
     AAQVEVLLSK AGFRITRVDS LPSGMNVIRA VRAA