ID   DNRQ_STRPE              Reviewed;         438 AA.
AC   Q54823;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Anthracycline biosynthesis protein DnrQ;
GN   Name=dnrQ;
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. DnrQ is required
CC       for the glycosylation of epsilon-rhodomycinone by DnrS to yield
CC       rhodomycin D. {ECO:0000269|PubMed:10631513,
CC       ECO:0000269|PubMed:7592454}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   -!- CAUTION: Although DnrQ shows significant similarity to cytochrome P450
CC       family, it lacks the heme-binding sites. The conservation of amino acid
CC       sequence is confined primarily to the C-terminal half of the protein.
CC       {ECO:0000305}.
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DR   EMBL; L47164; AAD15266.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q54823; -.
DR   SMR; Q54823; -.
DR   KEGG; ag:AAD15266; -.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002397; Cyt_P450_B.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   InterPro; IPR030958; P450-rel_GT_act.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00359; BP450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   TIGRFAMs; TIGR04515; P450_rel_GT_act; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis.
FT   CHAIN           1..438
FT                   /note="Anthracycline biosynthesis protein DnrQ"
FT                   /id="PRO_0000425679"
SQ   SEQUENCE   438 AA;  46317 MW;  A535F0E3611663B8 CRC64;
     MPTPTSAPPA APTDSELGRH LLTVRGFHFV FGALGDPYAR RLRGEADHLS LGELVRDRGP
     LHGSALGTWV TADGGISARL LDDPLLGPRH PASEGPQEHV LENVWETWRT CHVTPLGEDL
     LTPAAADSDR LAALLGPVLG PRTCTAWQVD AGRAVHRVLD GLPPHFDVVS DLARPAIAGS
     LAAVLGLPDE ARAELPDLLA ACGPVLDSAL CPPRLPVARA MTQALRRVRE LMAAAVANHL
     TAPADGAVSA LLAVDPGGGR DPGDTVTAAV LSTVVGAETA ITTVANAVMA LLKHDEQWSL
     LRADPGRAAD AVEETLRWAP PVTLRSLITQ GEVQIGGETL EADQHVVVLV DAAQRDPALY
     EDPDRFRLDR PRSPGFTHMA LAGRDHLGLV APLVRVQCTA VLRALAERLP GLRAEGEPLR
     RGRSPVVRAP LSLRLAQK