ID   TYLCV_STRFR             Reviewed;         461 AA.
AC   Q9XC67;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Demethyllactenocin mycarosyltransferase {ECO:0000303|PubMed:10658660};
DE            EC=2.4.1.318 {ECO:0000269|PubMed:10658660};
GN   Name=tylCV;
OS   Streptomyces fradiae (Streptomyces roseoflavus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=T59235;
RX   PubMed=10658660; DOI=10.1099/00221287-146-1-139;
RA   Bate N., Butler A.R., Smith I.P., Cundliffe E.;
RT   "The mycarose-biosynthetic genes of Streptomyces fradiae, producer of
RT   tylosin.";
RL   Microbiology 146:139-146(2000).
CC   -!- FUNCTION: Involved in the biosynthesis of mycarose which is a 6-
CC       deoxyhexose sugar required during production of the macrolide
CC       antibiotic tylosin. Catalyzes the transfer of L-mycarosyl from dTDP-
CC       beta-L-mycarose to demethyllactenocin to yield demethylmacrocin.
CC       {ECO:0000269|PubMed:10658660}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=demethyllactenocin + dTDP-beta-L-mycarose = demethylmacrocin +
CC         dTDP + H(+); Xref=Rhea:RHEA:14649, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58369, ChEBI:CHEBI:76810, ChEBI:CHEBI:76814,
CC         ChEBI:CHEBI:76819; EC=2.4.1.318;
CC         Evidence={ECO:0000269|PubMed:10658660};
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate desmycosin
CC       (tylosin B). {ECO:0000269|PubMed:10658660}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AF147704; AAD41824.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9XC67; -.
DR   SMR; Q9XC67; -.
DR   STRING; 1906.SFRA_26370; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   KEGG; ag:AAD41824; -.
DR   eggNOG; COG1819; Bacteria.
DR   BioCyc; MetaCyc:MON-18391; -.
DR   BRENDA; 2.4.1.318; 5932.
DR   GO; GO:0016758; F:hexosyltransferase activity; IEA:InterPro.
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; IPR002213; UDP_glucos_trans.
DR   InterPro; IPR006326; UDPGT_MGT-like.
DR   Pfam; PF00201; UDPGT; 1.
DR   TIGRFAMs; TIGR01426; MGT; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Transferase.
FT   CHAIN           1..461
FT                   /note="Demethyllactenocin mycarosyltransferase"
FT                   /id="PRO_0000430730"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   461 AA;  50120 MW;  4A61AFE1F06A2F59 CRC64;
     MAGLRPGAGV PPGTPWPISP GKHCVRSAIS RRARLPYHAP GTPLGRFRRA PDEGSCRMAH
     IAFFILPAAG HVNPTLGVAE ELAARGHRVT YALPEDMADR AVRVGARAVT YPLDRERFRA
     DMVPKEESDE YTDEGEFLKV LEWLLDTTAD TLPLLESAFA EDRPDVVAND PSTFWTGLLL
     AGKWDIPVIR STPSYASNEH WALHPPFEPG AAQVDPALIE LTARAEKLLK EHGTTSDPVA
     FAATVQSGPG LFYMPRYFQY AGETFDDRHH FVGPCAPRAS FHGTWQRPED GRPLVMVSLG
     TIYNERPGIF RACVEAFRDR PWNILLVLGG GLGAGDLGPL PENVLVRDFV PLGDVLPHTD
     LLVNHGGTST AMEALAHGVP IVAMPEMPEP RATARRIAEL DLGDWLLPGE VTAEKLSGIA
     QRVLTDDRIR KGLDRMRGEI RRAGGPAVAA DVIEGLLSPA A