ID   ELMM1_STROV             Reviewed;         378 AA.
AC   Q9AJU2;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=8-demethyl-8-alpha-L-rhamnosyl tetracenomycin-C 2'-O-methyltransferase {ECO:0000305};
DE            EC=2.1.1.305 {ECO:0000269|PubMed:11376004};
DE   AltName: Full=O-methyltransferase I {ECO:0000303|PubMed:11376004};
GN   Name=elmMI {ECO:0000303|PubMed:11376004};
OS   Streptomyces olivaceus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=47716;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=Tu 2353;
RX   PubMed=11376004; DOI=10.1074/jbc.m101225200;
RA   Patallo E.P., Blanco G., Fischer C., Brana A.F., Rohr J., Mendez C.,
RA   Salas J.A.;
RT   "Deoxysugar methylation during biosynthesis of the antitumor polyketide
RT   elloramycin by Streptomyces olivaceus. Characterization of three
RT   methyltransferase genes.";
RL   J. Biol. Chem. 276:18765-18774(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Tu 2353;
RX   PubMed=18310024; DOI=10.1099/mic.0.2007/014035-0;
RA   Ramos A., Lombo F., Brana A.F., Rohr J., Mendez C., Salas J.A.;
RT   "Biosynthesis of elloramycin in Streptomyces olivaceus requires
RT   glycosylation by enzymes encoded outside the aglycon cluster.";
RL   Microbiology 154:781-788(2008).
CC   -!- FUNCTION: O-methyltransferase involved in the biosynthesis of the
CC       permethylated L-rhamnose moiety of elloramycin, an antitumor
CC       polyketide. Mediates the methylation of the hydroxy groups at the 2'-
CC       position after the sugar moiety has been attached to the aglycon.
CC       {ECO:0000269|PubMed:11376004}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=8-demethyl-8-alpha-L-rhamnosyl-tetracenomycin C + S-adenosyl-
CC         L-methionine = 8-demethyl-8-(2-O-methyl-alpha-L-rhamnosyl)-
CC         tetracenomycin C + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:41540, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:78283, ChEBI:CHEBI:78285;
CC         EC=2.1.1.305; Evidence={ECO:0000269|PubMed:11376004};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q83WF2};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the methyltransferase OleY/MycE family.
CC       {ECO:0000305}.
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DR   EMBL; AJ300305; CAD57139.1; -; Genomic_DNA.
DR   EMBL; AM900040; CAP12606.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9AJU2; -.
DR   SMR; Q9AJU2; -.
DR   KEGG; ag:CAP12606; -.
DR   BioCyc; MetaCyc:MON-18589; -.
DR   BRENDA; 2.1.1.305; 6068.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0032259; P:methylation; IDA:UniProtKB.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR040800; MycE_N.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF17843; MycE_N; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Magnesium; Metal-binding; Methyltransferase;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..378
FT                   /note="8-demethyl-8-alpha-L-rhamnosyl tetracenomycin-C 2'-
FT                   O-methyltransferase"
FT                   /id="PRO_0000430713"
FT   ACT_SITE        271
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q83WF2"
FT   BINDING         195..201
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q83WF2"
FT   BINDING         210
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q83WF2"
FT   BINDING         227
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q83WF2"
FT   BINDING         245..246
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q83WF2"
FT   BINDING         268
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q83WF2"
FT   BINDING         268
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q83WF2"
FT   BINDING         296
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q83WF2"
FT   BINDING         297
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q83WF2"
SQ   SEQUENCE   378 AA;  41180 MW;  9D9D4EA7E446A0E3 CRC64;
     MDSPQVARTL VDSAGGTAAH TREAIRQIGV PETAAFLADE LAGRTETVTI RHAAEVQFVF
     DDRYAPDAAD PVPWTFRVGP EGVTHRAGAL PDPGAVVTQD LTELARSLYG PAADRSDATR
     TVWWRDHDDP RVYFDPPPVF PAVERLLAAA DGRDVPGLAG LALRHGSDKW GIHTYTAAYE
     QHFAPFRDRA VTVVEIGVGG YDDPAAGGGS LRMWKRYFRR GLVYGVDIAD KSRHREPRVH
     TVVADQSDPA SLRDLADAIG PIDIVIDDGS HISAHVVTAF STLFPRLNPG GLYVVEDLQT
     SYWPAFQGAY DDDTRTSVGF LKRLVDGLHH AEYPSRAGRP AQPTDRTVGS LHFHPNLAFV
     EKRANSGHGG ISRLREAT