ID   DNRP_STRS5              Reviewed;         298 AA.
AC   Q55217;
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=Rhodomycin D methylesterase DauP;
DE            EC=3.1.1.-;
DE   AltName: Full=10-carbomethoxy-13-deoxycarminomycin esterase;
DE   AltName: Full=4-O-methylrhodomycin D methylesterase;
GN   Name=dauP;
OS   Streptomyces sp. (strain C5).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=45212;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C5;
RX   PubMed=7836284; DOI=10.1128/jb.177.3.536-543.1995;
RA   Dickens M.L., Ye J., Strohl W.R.;
RT   "Analysis of clustered genes encoding both early and late steps in
RT   daunomycin biosynthesis by Streptomyces sp. strain C5.";
RL   J. Bacteriol. 177:536-543(1995).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=C5;
RX   PubMed=9098063; DOI=10.1128/jb.179.8.2641-2650.1997;
RA   Dickens M.L., Priestley N.D., Strohl W.R.;
RT   "In vivo and in vitro bioconversion of epsilon-rhodomycinone glycoside to
RT   doxorubicin: functions of DauP, DauK, and DoxA.";
RL   J. Bacteriol. 179:2641-2650(1997).
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       removal of methyl group from the carbomethoxy group of rhodomycin D
CC       (10-carbomethoxy-13-deoxycarminomycin) and 4-O-methylrhodomycin D to
CC       yield 10-carboxy-13-deoxycarminomycin and 10-carboxy-13-
CC       deoxydaunorubicin, respectively. Could be also involved in the
CC       decarboxylation of 10-carboxy-13-deoxycarminomycin and 10-carboxy-13-
CC       deoxydaunorubicin to yield 13-deoxycarminomycin and 13-
CC       deoxydaunorubicin, respectively. It seems that DauK may influence the
CC       ability of DauP to carry out the decarboxylation.
CC       {ECO:0000269|PubMed:9098063}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + rhodomycin D = 10-carboxy-13-deoxycarminomycin + H(+) +
CC         methanol; Xref=Rhea:RHEA:40247, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17790, ChEBI:CHEBI:77073, ChEBI:CHEBI:77077;
CC         Evidence={ECO:0000269|PubMed:9098063};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-O-methylrhodomycin D + H2O = 10-carboxy-13-deoxydaunorubicin
CC         + H(+) + methanol; Xref=Rhea:RHEA:40251, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:77074,
CC         ChEBI:CHEBI:77076; Evidence={ECO:0000269|PubMed:9098063};
CC   -!- PATHWAY: Antibiotic biosynthesis; daunorubicin biosynthesis.
CC   -!- PATHWAY: Antibiotic biosynthesis; carminomycin biosynthesis.
CC   -!- SIMILARITY: Belongs to the methyl esterase DnrP family. {ECO:0000305}.
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DR   EMBL; L35154; AAB16939.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q55217; -.
DR   SMR; Q55217; -.
DR   ESTHER; strsp-dauP; Aclacinomycin-methylesterase_RdmC.
DR   KEGG; ag:AAB16939; -.
DR   BioCyc; MetaCyc:MON-18183; -.
DR   UniPathway; UPA00054; -.
DR   UniPathway; UPA01040; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016872; F:intramolecular lyase activity; IDA:UniProtKB.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IMP:UniProtKB.
DR   GO; GO:1901771; P:daunorubicin biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0044598; P:doxorubicin metabolic process; IMP:UniProtKB.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Hydrolase.
FT   CHAIN           1..298
FT                   /note="Rhodomycin D methylesterase DauP"
FT                   /id="PRO_0000425680"
FT   DOMAIN          25..277
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   298 AA;  32361 MW;  AF69F32D64D5FB20 CRC64;
     MPTRMITKDE VTLWSEGIGD PADAPLLLIA GGNLSARSWP DEFVERLAAA GHFVIRYDHR
     DTGRSSRYDF ALHPYGFDEL ATDALAVLDA WQVRAAHVVG MSLGNTIGQL LALDAPERLL
     TLTVMLGGAL DVDFDADLEA ALKGEPSVSG LPVPSRRFLD MMMLLQQPAG TDEELLERRV
     EKWRLLNGEG VPFDSDEFRR RELLAAGHAG TFDEPIVHHM IPQPPVSRGA ELARITTPVL
     AIQAMCDPAA PPPHARHLAD RIPGARVVEI ENMGHALPLA VHEPLAAAIC AHTRAATV