ID   TYLM2_STRFR             Reviewed;         452 AA.
AC   P95747;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 3.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Tylactone mycaminosyltransferase {ECO:0000303|PubMed:15612702};
DE            EC=2.4.1.316 {ECO:0000269|PubMed:15612702};
GN   Name=tylMII {ECO:0000303|PubMed:9031628};
OS   Streptomyces fradiae (Streptomyces roseoflavus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=T59235;
RX   PubMed=9031628; DOI=10.1016/s0378-1119(96)00595-1;
RA   Gandecha A.R., Large S.L., Cundliffe E.;
RT   "Analysis of four tylosin biosynthetic genes from the tylLM region of
RT   Streptomyces fradiae.";
RL   Gene 184:197-203(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=T59235;
RA   Gandecha A.R.;
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBSTRATE
RP   SPECIFICITY.
RX   PubMed=15612702; DOI=10.1021/ja043900e;
RA   Melancon C.E. III, Takahashi H., Liu H.W.;
RT   "Characterization of tylM3/tylM2 and mydC/mycB pairs required for efficient
RT   glycosyltransfer in macrolide antibiotic biosynthesis.";
RL   J. Am. Chem. Soc. 126:16726-16727(2004).
CC   -!- FUNCTION: Involved in the biosynthesis of the macrolide antibiotic
CC       tylosin derived from the polyketide lactone tylactone. Catalyzes the
CC       transfer of alpha-D-mycaminosyl from dTDP-alpha-D-mycaminose to the 5-
CC       hydroxyl group of tylactone to yield 5-O-mycaminosytylactone. It can
CC       also accept 16-membered tylactone and 12-membered ring macrolide.
CC       {ECO:0000269|PubMed:15612702, ECO:0000303|PubMed:9031628}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP-alpha-D-mycaminose + tylactone = 5-O-beta-D-
CC         mycaminosyltylactone + dTDP + H(+); Xref=Rhea:RHEA:21468,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29700, ChEBI:CHEBI:58369,
CC         ChEBI:CHEBI:63268, ChEBI:CHEBI:76802; EC=2.4.1.316;
CC         Evidence={ECO:0000269|PubMed:15612702};
CC   -!- ACTIVITY REGULATION: The activity of TylM2 is substantially increased
CC       by the addition of the accessory protein TylM3.
CC       {ECO:0000269|PubMed:15612702}.
CC   -!- PATHWAY: Antibiotic biosynthesis; tylosin biosynthesis.
CC       {ECO:0000303|PubMed:9031628}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC       {ECO:0000305}.
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DR   EMBL; X81885; CAA57472.2; -; Genomic_DNA.
DR   AlphaFoldDB; P95747; -.
DR   SMR; P95747; -.
DR   STRING; 1906.SFRA_32295; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   PRIDE; P95747; -.
DR   KEGG; ag:CAA57472; -.
DR   eggNOG; COG1819; Bacteria.
DR   BioCyc; MetaCyc:MON-18380; -.
DR   BRENDA; 2.4.1.316; 5932.
DR   UniPathway; UPA01018; -.
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..452
FT                   /note="Tylactone mycaminosyltransferase"
FT                   /id="PRO_0000430767"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   452 AA;  48660 MW;  5D0468BF8653DDB4 CRC64;
     MRRALDDRRR GPHGPEGKPP MRVLLTCIAH NTHYYNLVPV AWALRAAGHE VRVAAQPALT
     DTITASGLTA VPVGGNESVL EFVTEIGGDP GPYQRGMDFA ETCGEPLSYE HALGQQTAMS
     ALCFAPFNCD STIDDMVALA RSWRPDLVLW EPFTYAGPIA AHACGAAHAR LLWGPDVILN
     ARAQFRRLAA GQPEERREDP VAEWLGWTLE RHGLTAERET VEELIGGQWT LDPTAESLRL
     PAAGRVVPFR FVPYNGRSVL PDWLLRKPGR PRVCFTLGVS ARETYGRDAV PFHELLAGLG
     DLDAEIVATL DPGQLSGAGE VPRNVRAVDF VPMDALLPTC SAVVHHGGAG TCFTATLNGL
     PQIVVAALWD APLKGAQLAE AGAGVSIAPE KLDAATLRAG VVRALEDEDM RRSAGLLRAE
     MLAEPTPAGL VPQLERLTAL HRNGRSRSAP ER