OLEY_STRAT
ID OLEY_STRAT Reviewed; 386 AA.
AC O87833;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=L-olivosyl-oleandolide 3-O-methyltransferase;
DE EC=2.1.1.239 {ECO:0000269|PubMed:11514520};
DE AltName: Full=Oleandomycin biosynthesis protein Y {ECO:0000305};
GN Name=oleY;
OS Streptomyces antibioticus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1890;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC STRAIN=ATCC 11891 / DSM 40868 / BCRC 11580 / NCIMB 11506 / PSA 205;
RX PubMed=9749673; DOI=10.1007/s004380050816;
RA Olano C., Rodriguez A.M., Michel J.M., Mendez C., Raynal M.C., Salas J.A.;
RT "Analysis of a Streptomyces antibioticus chromosomal region involved in
RT oleandomycin biosynthesis, which encodes two glycosyltransferases
RT responsible for glycosylation of the macrolactone ring.";
RL Mol. Gen. Genet. 259:299-308(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 11891 / DSM 40868 / BCRC 11580 / NCIMB 11506 / PSA 205;
RX PubMed=11514520; DOI=10.1128/jb.183.18.5358-5363.2001;
RA Rodriguez L., Rodriguez D., Olano C., Brana A.F., Mendez C., Salas J.A.;
RT "Functional analysis of OleY L-oleandrosyl 3-O-methyltransferase of the
RT oleandomycin biosynthetic pathway in Streptomyces antibioticus.";
RL J. Bacteriol. 183:5358-5363(2001).
CC -!- FUNCTION: 3-O-methyltransferase involved in the synthesis of L-
CC oleandrose, a sugar attached to oleandomycin, a macrolide antibiotic.
CC Acts on monoglycosylated macrolactones and mediates the conversion of
CC L-olivosyl-erythronolide B into its 3-O-methylated derivative, L-
CC oleandrosyl-erythronolide B. Also able to methylate other
CC monoglycosylated derivatives, such as L-rhamnosyl- and L-mycarosyl-
CC erythronolide B. {ECO:0000269|PubMed:11514520}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-olivosyl-oleandolide + S-adenosyl-L-methionine = H(+) + L-
CC oleandrosyl-oleandolide + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:31623, ChEBI:CHEBI:15378, ChEBI:CHEBI:29613,
CC ChEBI:CHEBI:29614, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789;
CC EC=2.1.1.239; Evidence={ECO:0000269|PubMed:11514520};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q83WF2};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.2-7.6. {ECO:0000269|PubMed:11514520};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:9749673}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11514520}.
CC -!- SIMILARITY: Belongs to the methyltransferase OleY/MycE family.
CC {ECO:0000305}.
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DR EMBL; AJ002638; CAA05644.1; -; Genomic_DNA.
DR AlphaFoldDB; O87833; -.
DR SMR; O87833; -.
DR KEGG; ag:CAA05644; -.
DR BioCyc; MetaCyc:MON-17057; -.
DR BRENDA; 2.1.1.239; 5974.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent 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..386
FT /note="L-olivosyl-oleandolide 3-O-methyltransferase"
FT /id="PRO_0000418458"
FT REGION 364..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 271
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q83WF2"
FT BINDING 166
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
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 386 AA; 42439 MW; E29C473CC15760B0 CRC64;
MSYDDHAVLE AILRCAGGDE RFLLNTVEEW GAAEITAALV DELLFRCEIP QVGGEAFIGL
DVLHGADRIS HVLQVTDGKP VTSAEPAGQE LGGRTWSSRS ATLLRELFGP PSGRTAGGFG
VSFLPDLRGP RTMEGAALAA RATNVVLHAT TNETPPLDRL ALRYESDKWG GVHWFTGHYD
RHLRAVRDQA VRILEIGIGG YDDLLPSGAS LKMWKRYFPR GLVFGVDIFD SRRATSRVSR
RSAARQDDPE FMRRVAEEHG PFDVIIDDGS HINAHMRTSF SVMFPHLRNG GFYVIEDTFT
SYWPGYGGPS GARCPSGTTA LEMVKGLIDS VHYEERPDGA ATADYIARNL VGLHAYQTTS
SSSRRAINKE GGIPHTVPRE PFWNDN
