ERYG_SACEN
ID ERYG_SACEN Reviewed; 306 AA.
AC A4F7P5; Q54095; Q54098;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Erythromycin 3''-O-methyltransferase;
DE EC=2.1.1.254;
DE AltName: Full=Erythromycin biosynthesis protein G;
GN Name=eryG; OrderedLocusNames=SACE_0728;
OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Saccharopolyspora.
OX NCBI_TaxID=405948;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC 2338;
RX PubMed=1840640; DOI=10.1007/bf00290659;
RA Haydock S.F., Dowson J.A., Dhillon N., Roberts G.A., Cortes J.,
RA Leadlay P.F.;
RT "Cloning and sequence analysis of genes involved in erythromycin
RT biosynthesis in Saccharopolyspora erythraea: sequence similarities between
RT EryG and a family of S-adenosylmethionine-dependent methyltransferases.";
RL Mol. Gen. Genet. 230:120-128(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC 2338;
RX PubMed=17369815; DOI=10.1038/nbt1297;
RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA Haydock S.F., Leadlay P.F.;
RT "Complete genome sequence of the erythromycin-producing bacterium
RT Saccharopolyspora erythraea NRRL23338.";
RL Nat. Biotechnol. 25:447-453(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 257-306, AND PATHWAY.
RX PubMed=2011746; DOI=10.1126/science.2011746;
RA Weber J.M., Leung J.O., Swanson S.J., Idler K.B., McAlpine J.B.;
RT "An erythromycin derivative produced by targeted gene disruption in
RT Saccharopolyspora erythraea.";
RL Science 252:114-117(1991).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC 2338;
RX PubMed=2185226; DOI=10.1128/jb.172.5.2541-2546.1990;
RA Paulus T.J., Tuan J.S., Luebke V.E., Maine G.T., DeWitt J.P., Katz L.;
RT "Mutation and cloning of eryG, the structural gene for erythromycin O-
RT methyltransferase from Saccharopolyspora erythraea, and expression of eryG
RT in Escherichia coli.";
RL J. Bacteriol. 172:2541-2546(1990).
RN [5]
RP PATHWAY.
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC 2338;
RX PubMed=9353926; DOI=10.1099/00221287-143-10-3251;
RA Summers R.G., Donadio S., Staver M.J., Wendt-Pienkowski E.,
RA Hutchinson C.R., Katz L.;
RT "Sequencing and mutagenesis of genes from the erythromycin biosynthetic
RT gene cluster of Saccharopolyspora erythraea that are involved in L-mycarose
RT and D-desosamine production.";
RL Microbiology 143:3251-3262(1997).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent O-methyltransferase that
CC catalyzes the last step in the erythromycin biosynthesis pathway.
CC Methylates the position 3 of the mycarosyl moiety of erythromycin C,
CC forming the most active form of the antibiotic, erythromycin A. Can
CC also methylate the precursor erythromycin D, forming erythromycin B.
CC {ECO:0000269|PubMed:1840640, ECO:0000269|PubMed:2185226}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=erythromycin C + S-adenosyl-L-methionine = erythromycin A +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32647,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:64258, ChEBI:CHEBI:64268; EC=2.1.1.254;
CC Evidence={ECO:0000269|PubMed:2185226};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=erythromycin D + S-adenosyl-L-methionine = erythromycin B +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32651,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:63677, ChEBI:CHEBI:64279; EC=2.1.1.254;
CC Evidence={ECO:0000269|PubMed:2185226};
CC -!- PATHWAY: Antibiotic biosynthesis; erythromycin biosynthesis.
CC {ECO:0000269|PubMed:1840640, ECO:0000269|PubMed:2011746,
CC ECO:0000269|PubMed:2185226, ECO:0000269|PubMed:9353926}.
CC -!- DISRUPTION PHENOTYPE: Cells accumulate erythromycin C and its precursor
CC erythromycin D, with little or no production of erythromycin A or
CC erythromycin B. {ECO:0000269|PubMed:2185226}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
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DR EMBL; X60379; CAA42929.1; -; Genomic_DNA.
DR EMBL; AM420293; CAM00069.1; -; Genomic_DNA.
DR EMBL; M54983; AAA26498.1; -; Genomic_DNA.
DR PIR; S18533; S18533.
DR RefSeq; WP_009950399.1; NZ_PDBV01000001.1.
DR AlphaFoldDB; A4F7P5; -.
DR SMR; A4F7P5; -.
DR STRING; 405948.SACE_0728; -.
DR EnsemblBacteria; CAM00069; CAM00069; SACE_0728.
DR KEGG; sen:SACE_0728; -.
DR eggNOG; COG2230; Bacteria.
DR HOGENOM; CLU_039068_6_0_11; -.
DR OrthoDB; 1518440at2; -.
DR BioCyc; MetaCyc:MON-17061; -.
DR BRENDA; 2.1.1.254; 5518.
DR UniPathway; UPA00240; -.
DR Proteomes; UP000006728; Chromosome.
DR GO; GO:0102307; F:erythromycin C 3''-o-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102308; F:erythromycin D 3''-o-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IMP:UniProtKB.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IMP:UniProtKB.
DR GO; GO:0032259; P:methylation; IMP:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..306
FT /note="Erythromycin 3''-O-methyltransferase"
FT /id="PRO_0000418462"
FT BINDING 157
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT CONFLICT 35
FT /note="E -> A (in Ref. 1; CAA42929)"
FT /evidence="ECO:0000305"
FT CONFLICT 257..259
FT /note="LRK -> ARC (in Ref. 3; AAA26498)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 306 AA; 33990 MW; DA58E5266C72FCC3 CRC64;
MSVKQKSALQ DLVDFAKWHV WTRVRPSSRA RLAYELFADD HEATTEGAYI NLGYWKPGCA
GLEEANQELA NQLAEAAGIS EGDEVLDVGF GLGAQDFFWL ETRKPARIVG VDLTPSHVRI
ASERAERENV QDRLQFKEGS ATDLPFGAET FDRVTSLESA LHYEPRTDFF KGAFEVLKPG
GVLAIGDIIP LDLREPGSDG PPKLAPQRSG SLSGGIPVEN WVPRETYAKQ LREAGFVDVE
VKSVRDNVME PWLDYWLRKL QDESFKKSVS RLFYSQVKRS LTSDSGMKGE LPALDFVIAS
ARKPGA
