ID   ELMM2_STROV             Reviewed;         390 AA.
AC   Q9AJU1;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=8-demethyl-8-(2-methoxy-alpha-L-rhamnosyl)-tetracenomycin-C 3'-O-methyltransferase {ECO:0000305};
DE            EC=2.1.1.306 {ECO:0000269|PubMed:11376004};
DE   AltName: Full=O-methyltransferase II {ECO:0000303|PubMed:11376004};
GN   Name=elmMII {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 3'-
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-(2-O-methyl-alpha-L-rhamnosyl)-tetracenomycin C +
CC         S-adenosyl-L-methionine = 8-demethyl-8-(2,3-di-O-methyl-alpha-L-
CC         rhamnosyl)-tetracenomycin C + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:41544, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:78285, ChEBI:CHEBI:78286;
CC         EC=2.1.1.306; 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; CAD57140.1; -; Genomic_DNA.
DR   EMBL; AM900040; CAP12608.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9AJU1; -.
DR   SMR; Q9AJU1; -.
DR   KEGG; ag:CAP12608; -.
DR   BioCyc; MetaCyc:MON-18590; -.
DR   BRENDA; 2.1.1.306; 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..390
FT                   /note="8-demethyl-8-(2-methoxy-alpha-L-rhamnosyl)-
FT                   tetracenomycin-C 3'-O-methyltransferase"
FT                   /id="PRO_0000430714"
FT   ACT_SITE        278
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q83WF2"
FT   BINDING         202..208
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q83WF2"
FT   BINDING         217
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q83WF2"
FT   BINDING         234
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q83WF2"
FT   BINDING         252..253
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q83WF2"
FT   BINDING         275
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q83WF2"
FT   BINDING         275
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q83WF2"
FT   BINDING         303
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q83WF2"
FT   BINDING         304
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q83WF2"
SQ   SEQUENCE   390 AA;  42836 MW;  30F4E318102882EE CRC64;
     MTTPSPTPPL AAAEVAAAAG LQQRDLLAVL DRVGLEPAVA FLVHDLTARC DTPDNPDAAR
     IGLAVEHSGH RTERVLAVRK GEPVRVDEET AGPPPVRLTF DLADLVRGVY GPPPGPGAGL
     FRVERDDAWF VKNADDAEPF RIFESYMRAV DVLVRAATSR PGDLGRLAAR HASDKWGLWH
     WFTPLYEHHF ARLRHQPVRV LELGIGGYQN PDEGGGSLKM WRSYFPQGRI FGVDYFPKHG
     LDEDRIHTLQ GSQDDAGFLR RVAEEHGPFD IVIDDGSHVA GHQQTAFRTL FPAVRNGGFY
     VIEDLWTAYC PGYGGAATAR AEGRTSIGLL KSLLDDLHYE EWTAPEPAAP GFAAPSLVGV
     HVYRNLAVLE KGRNSEGTIP FFAPREIDYV