ELMM3_STROV
ID ELMM3_STROV Reviewed; 261 AA.
AC Q9AJU0;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=8-demethyl-8-(2,3-dimethoxy-alpha-L-rhamnosyl)-tetracenomycin-C 4'-O-methyltransferase {ECO:0000305};
DE EC=2.1.1.307 {ECO:0000269|PubMed:11376004};
DE AltName: Full=O-methyltransferase III {ECO:0000303|PubMed:11376004};
GN Name=elmMIII {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 4'-
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-(2,3-di-O-methyl-alpha-L-rhamnosyl)-
CC tetracenomycin C + S-adenosyl-L-methionine = 8-demethyl-8-(2,3,4-tri-
CC O-methyl-alpha-L-rhamnosyl)-tetracenomycin C + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:41548, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:78286,
CC ChEBI:CHEBI:78287; EC=2.1.1.307;
CC Evidence={ECO:0000269|PubMed:11376004};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the methyltransferase TylF/MycF family.
CC {ECO:0000305}.
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DR EMBL; AJ300305; CAD57141.1; -; Genomic_DNA.
DR EMBL; AM900040; CAP12609.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9AJU0; -.
DR SMR; Q9AJU0; -.
DR KEGG; ag:CAP12609; -.
DR BioCyc; MetaCyc:MON-18591; -.
DR BRENDA; 2.1.1.307; 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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR008884; TylF_MeTrfase.
DR PANTHER; PTHR40036; PTHR40036; 1.
DR Pfam; PF05711; TylF; 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..261
FT /note="8-demethyl-8-(2,3-dimethoxy-alpha-L-rhamnosyl)-
FT tetracenomycin-C 4'-O-methyltransferase"
FT /id="PRO_0000430715"
FT BINDING 53..54
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9L9F2"
FT BINDING 81..85
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9L9F2"
FT BINDING 111..115
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9L9F2"
FT BINDING 167
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9L9F2"
FT BINDING 185..186
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9L9F2"
FT BINDING 185
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 191
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9L9F2"
FT BINDING 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
SQ SEQUENCE 261 AA; 29044 MW; 7DEC0B29EBD72CA6 CRC64;
MTEDARDLYL DLMKKVLTNL IYRDAPIQTF VYDGEPDADP RLLGRDWPSV AHTMVGLKRL
DNLQYCVETV LADGVPGDLV ETGVWRGGSS IFMRAVLRAH GDTARRVWVA DSFEGMPEVG
ADSHAVDREM RLHEHNGVLA VPLEQVRANF ERYGLLDDQV RFLPGWFKDT LPGAPTGRLA
VIRLDGDLYE STTDALENLM PRLSPGGFVI IDDYAIDACR DAVHDYRGRY GISDPISEID
GTGVFWRHTA ASARSLQPAT V
