ID   SFMM2_STRLA             Reviewed;         366 AA.
AC   B0CN31;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=L-tyrosine C(3)-methyltransferase {ECO:0000305};
DE            EC=2.1.1.304 {ECO:0000303|PubMed:22187429};
GN   Name=sfmM2 {ECO:0000303|PubMed:17981978};
OS   Streptomyces lavendulae.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1914 {ECO:0000312|EMBL:ABI22137.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NRRL 11002 {ECO:0000312|EMBL:ABI22137.1};
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   FUNCTION, AND 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   FUNCTION, PATHWAY, AND CATALYTIC ACTIVITY.
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: C-methyltransferase that mediates the methylation of tyrosine
CC       into 3-methyl-L-tyrosine (3-Me-Tyr) in biosynthesis of saframycin A, a
CC       potent antitumor antibiotic that belongs to the tetrahydroisoquinoline
CC       family. Involved in biosynthesis of 3-hydroxy-5-methyl-O-methyltyrosine
CC       (3-OH-5-Me-OMe-Tyr), a core structure of saframycin A.
CC       {ECO:0000269|PubMed:19494690, ECO:0000269|PubMed:22187429}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tyrosine + S-adenosyl-L-methionine = 3-methyl-L-tyrosine +
CC         H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:41428,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58315,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:78239; EC=2.1.1.304;
CC         Evidence={ECO:0000303|PubMed:22187429};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:19494690,
CC       ECO:0000269|PubMed:22187429}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01020}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQ838002; ABI22137.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0CN31; -.
DR   SMR; B0CN31; -.
DR   KEGG; ag:ABI22137; -.
DR   BioCyc; MetaCyc:MON-19336; -.
DR   BRENDA; 2.1.1.304; 133.
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   Pfam; PF00891; Methyltransf_2; 1.
DR   PIRSF; PIRSF005739; O-mtase; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51683; SAM_OMT_II; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..366
FT                   /note="L-tyrosine C(3)-methyltransferase"
FT                   /id="PRO_0000430696"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         223
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   366 AA;  39990 MW;  679AECDCB65B8E81 CRC64;
     MTISLENTTV GQNPAGGPPT GKAPLDMEGL AWILFGASAF QYLNAACELN LFELLENKPG
     LTKPQIGAEL GLADRANDIL LLGATATGML TVEDGRYQLA TVLAELLKTD DWQRFKDTVG
     FEQYVCYEGQ IDFTESLRSN SNVGLRRVRG SGRDLYHRLH ENPQMEQAFY KYMRSWSELA
     NQHLVEVLDL SGTSKLLDCG GGDAVNSIAL AQANPHIEAG ILEIPPTAPL TEKKIAEAGL
     SDRITVKPGD MHTDEFPTGY DTVMFAHQLV IWTPEENTAL LRKAYNALPE GGRVIIFNSM
     SNDEGDGPVV AALDSVYFAA LPAEGGMIYS WATYEESLTK AGFNPETFQR IDFPGWTPHG
     VIIATK