ID   DNRS_STRPE              Reviewed;         431 AA.
AC   Q54824;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=TDP-daunosamine transferase DnrS;
DE            EC=2.4.1.-;
DE   AltName: Full=2,3,6-trideoxy-3-aminohexose transferase;
DE   Flags: Precursor;
GN   Name=dnrS; Synonyms=dnmS;
OS   Streptomyces peucetius.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1950;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 29050 / DSM 40754 / JCM 9920 / NBRC 100596 / NCIMB 10972;
RX   PubMed=7592454; DOI=10.1128/jb.177.22.6688-6692.1995;
RA   Otten S.L., Liu X., Ferguson J., Hutchinson C.R.;
RT   "Cloning and characterization of the Streptomyces peucetius dnrQS genes
RT   encoding a daunosamine biosynthesis enzyme and a glycosyl transferase
RT   involved in daunorubicin biosynthesis.";
RL   J. Bacteriol. 177:6688-6692(1995).
RN   [2]
RP   FUNCTION.
RC   STRAIN=ATCC 29050 / DSM 40754 / JCM 9920 / NBRC 100596 / NCIMB 10972;
RX   PubMed=10631513; DOI=10.1016/s1074-5521(00)80004-6;
RA   Olano C., Lomovskaya N., Fonstein L., Roll J.T., Hutchinson C.R.;
RT   "A two-plasmid system for the glycosylation of polyketide antibiotics:
RT   bioconversion of epsilon-rhodomycinone to rhodomycin D.";
RL   Chem. Biol. 6:845-855(1999).
CC   -!- FUNCTION: Involved in the biosynthesis of the anthracyclines
CC       carminomycin and daunorubicin (daunomycin) which are aromatic
CC       polyketide antibiotics that exhibit high cytotoxicity and are widely
CC       applied in the chemotherapy of a variety of cancers. Catalyzes the
CC       addition of the TDP activated glycoside, L-daunosamine-TDP (2,3,6-
CC       trideoxy-3-aminohexose-TDP) at position C-7 of epsilon-rhodomycinone to
CC       yield rhodomycin D. Glycosylation is a prerequisite for biological
CC       activity of anthracyclines and requires DnrQ which seems to act as an
CC       activator. {ECO:0000269|PubMed:10631513, ECO:0000269|PubMed:7592454}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP-beta-L-daunosamine + epsilon-rhodomycinone = dTDP + H(+)
CC         + rhodomycin D; Xref=Rhea:RHEA:45760, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58369, ChEBI:CHEBI:75291, ChEBI:CHEBI:77073,
CC         ChEBI:CHEBI:85417;
CC   -!- PATHWAY: Antibiotic biosynthesis; daunorubicin biosynthesis.
CC   -!- PATHWAY: Antibiotic biosynthesis; carminomycin biosynthesis.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC       {ECO:0000305}.
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DR   EMBL; L47164; AAD15267.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q54824; -.
DR   SMR; Q54824; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   KEGG; ag:AAD15267; -.
DR   BioCyc; MetaCyc:MON-18176; -.
DR   UniPathway; UPA00054; -.
DR   UniPathway; UPA01040; -.
DR   GO; GO:0016758; F:hexosyltransferase activity; IMP:UniProtKB.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:1901771; P:daunorubicin biosynthetic process; IMP:UniProtKB.
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   3: Inferred from homology;
KW   Antibiotic biosynthesis; Glycosyltransferase; Signal; Transferase.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..431
FT                   /note="TDP-daunosamine transferase DnrS"
FT                   /id="PRO_0000425678"
SQ   SEQUENCE   431 AA;  46555 MW;  09287C8CAEF9F647 CRC64;
     MKVLVTAFAM DAHFNGVVPL AWALRAAGHD VRVASQPALT DSITRAGLTA VPVGTDHQVQ
     AAMGAMAPGV FALHLNPDYL ENRPELLDLE FLEASTSMLT AAFYAQINND SMIDEMVDFA
     AWWRPDLVVW EPFTFGGAVA AQVTGAAQAR LLWGPDLFLR VHDRFQQVLH EVPAERRDDA
     LEEWLTWTLE RHGAAFGPEV ISGHWTIDQM PPSVRFATAR PTVPMRFVPY NGPVPAVVPP
     WLRADPGRPR VLLTQGITER STGFTGLPRA GELLASIAEL DAEVVATVKA EEREGLPPLP
     GNVRVVDSLS LHVVLPSCAA VVHHGGAGTW ATAALHGVPQ LALAWQWDDV FRAGQLEKLG
     AGIFLPPHGE GASAGRVRDR LAQVLAEPSF RQGAARIRAE MLRTPAPGAV VPTLEQLTAR
     HRAPAGQGVR H