ID   DNRP_STRPE              Reviewed;         298 AA.
AC   Q54809;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Rhodomycin D methylesterase DnrP;
DE            EC=3.1.1.-;
DE   AltName: Full=10-carbomethoxy-13-deoxycarminomycin esterase;
DE   AltName: Full=4-O-methylrhodomycin D methylesterase;
GN   Name=dnrP;
OS   Streptomyces peucetius.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1950;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=7601857; DOI=10.1128/jb.177.13.3879-3884.1995;
RA   Madduri K., Hutchinson C.R.;
RT   "Functional characterization and transcriptional analysis of a gene cluster
RT   governing early and late steps in daunorubicin biosynthesis in Streptomyces
RT   peucetius.";
RL   J. Bacteriol. 177:3879-3884(1995).
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 DnrK may influence the
CC       ability of DnrP to carry out the decarboxylation (Probable).
CC       {ECO:0000305|PubMed:7601857}.
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   -!- 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;
CC   -!- PATHWAY: Antibiotic biosynthesis; daunorubicin biosynthesis.
CC   -!- PATHWAY: Antibiotic biosynthesis; carminomycin biosynthesis.
CC   -!- SIMILARITY: Belongs to the methyl esterase DnrP family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L40425; AAA99002.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q54809; -.
DR   SMR; Q54809; -.
DR   ESTHER; strpe-dnrP; Aclacinomycin-methylesterase_RdmC.
DR   KEGG; ag:AAA99002; -.
DR   BioCyc; MetaCyc:MON-18174; -.
DR   UniPathway; UPA00054; -.
DR   UniPathway; UPA01040; -.
DR   GO; GO:0052689; F:carboxylic ester hydrolase 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   3: Inferred from homology;
KW   Antibiotic biosynthesis; Hydrolase.
FT   CHAIN           1..298
FT                   /note="Rhodomycin D methylesterase DnrP"
FT                   /id="PRO_0000425681"
FT   DOMAIN          25..277
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   298 AA;  32245 MW;  10F1D25E784CE6C6 CRC64;
     MPTRMITNDE VTLWSEGLGD PADAPLLLIA GGNLSAKSWP DEFVERLVAA GHFVIRYDHR
     DTGRSSRCDF ALHPYGFDEL AADALAVLDG WQVRAAHVVG MSLGNTIGQL LALDAPERLL
     TLTVMLGGAL DVDFDADLEA ALKGEPSVSG LPVPSQRFLD MMTMLQQPAE TDEELLERRV
     EKWRLLNGEG VPFDADEFRR RELLAAGHAG TFDEPIVHHM IPLPPVSRGA ELSRVTTPVL
     AIQAMCDPAA PPPHARHLAN RIPGARVVEI ENMGHALPLA VHEPLAAAIC AHTRAATV