ID   ERYBV_SACER             Reviewed;         415 AA.
AC   O33939;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Erythronolide mycarosyltransferase {ECO:0000303|PubMed:9353926};
DE            EC=2.4.1.328 {ECO:0000269|PubMed:17262863};
GN   Name=eryBV {ECO:0000303|PubMed:9353926};
OS   Saccharopolyspora erythraea (Streptomyces erythraeus).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=1836;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NRRL 2338;
RA   Summers R.G., Staver M.J., Donadio S., Wendt-Pienkowski E.,
RA   Hutchinson C.R., Katz L.;
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=NRRL 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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NRRL2338;
RX   PubMed=9393448; DOI=10.1007/s004380050566;
RA   Gaisser S., Bohm G.A., Cortes J., Leadlay P.F.;
RT   "Analysis of seven genes from the eryAI-eryK region of the erythromycin
RT   biosynthetic gene cluster in Saccharopolyspora erythraea.";
RL   Mol. Gen. Genet. 256:239-251(1997).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX   PubMed=17262863; DOI=10.1002/cbic.200600509;
RA   Zhang C., Fu Q., Albermann C., Li L., Thorson J.S.;
RT   "The in vitro characterization of the erythronolide mycarosyltransferase
RT   EryBV and its utility in macrolide diversification.";
RL   ChemBioChem 8:385-390(2007).
CC   -!- FUNCTION: Involved in the biosynthesis of the macrolide antibiotic
CC       erythromycin. Catalyzes the reversible transfer of mycarosyl from dTDP-
CC       beta-L-mycarose to erythronolide B to yield 3-alpha-L-
CC       mycarosylerythronolide B. It can also use TDP-beta-L-cladinose.
CC       {ECO:0000269|PubMed:17262863, ECO:0000303|PubMed:9353926}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP-beta-L-mycarose + erythronolide B = 3-O-alpha-L-
CC         mycarosylerythronolide B + dTDP + H(+); Xref=Rhea:RHEA:41576,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:27977, ChEBI:CHEBI:28343,
CC         ChEBI:CHEBI:58369, ChEBI:CHEBI:76814; EC=2.4.1.328;
CC         Evidence={ECO:0000269|PubMed:17262863};
CC   -!- MISCELLANEOUS: It does not require an auxiliary activator protein.
CC       {ECO:0000305|PubMed:17262863}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC       {ECO:0000305}.
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DR   EMBL; U77459; AAB84072.1; -; Genomic_DNA.
DR   EMBL; Y11199; CAA72081.1; -; Genomic_DNA.
DR   RefSeq; WP_009950885.1; NZ_CP069353.1.
DR   AlphaFoldDB; O33939; -.
DR   SMR; O33939; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   OMA; RWWKPDL; -.
DR   GO; GO:0016758; F:hexosyltransferase activity; IEA:UniProt.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   InterPro; IPR010610; DUF1205.
DR   InterPro; IPR030953; Glycosyl_450act.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   Pfam; PF06722; DUF1205; 1.
DR   TIGRFAMs; TIGR04516; glycosyl_450act; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Glycosyltransferase; Transferase.
FT   CHAIN           1..415
FT                   /note="Erythronolide mycarosyltransferase"
FT                   /id="PRO_0000430759"
SQ   SEQUENCE   415 AA;  45563 MW;  7A48FD35DD417FD8 CRC64;
     MRVLLTSFAH RTHFQGLVPL AWALRTAGHD VRVAAQPALT DAVIGAGLTA VPVGSDHRLF
     DIVPEVAAQV HRYSFYLDFY HREQELHSWE FLLGMQEATS RWVYPVVNND SFVAELVDFA
     RDWRPDLVLW EPFTFAGAVA ARACGAAHAR LLWGSDLTGY FRGRFQAQRL RRPPEDRPDP
     LGTWLTEVAG RFGVEFGEDL AVGQWSVDQL PPSFRLDTGM ETVVARTLPY NGASVVPDWL
     KKGSATRRIC ITGGFSGLGL AADADQFART LAQLARFDGE IVVTGSGPDT SAVPDNIRLV
     DFVPMGVLLQ NCAAIIHHGG AGTWATALHH GIPQISVAHE WDCMLRGQQT AELGAGIYLR
     PDEVDADSLA SALTQVVEDP TYTENAVKLR EEALSDPTPQ EIVPRLEELT RRHAG