ID   DNRC_STRS5              Reviewed;         220 AA.
AC   Q55214; Q55227;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Aklanonic acid methyltransferase DauC;
DE            Short=AAMT;
DE            EC=2.1.1.288;
GN   Name=dauC;
OS   Streptomyces sp. (strain C5).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=45212;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   SUBUNIT.
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, AND DISRUPTION PHENOTYPE.
RC   STRAIN=C5;
RA   Bartel P.L., Connors N.C., William R.S.;
RT   "Biosynthesis of anthracyclines: analysis of mutants of Streptomyces sp.
RT   strain C5 blocked in daunomycin biosynthesis.";
RL   J. Gen. Microbiol. 136:1877-1886(1990).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=C5;
RA   Connors N.C., Bartel P.L., William R.S.;
RT   "Biosynthesis of anthracyclines: enzymic conversion of aklanonic acid to
RT   aklavinone and epsilon-rhodomycinone by anthracycline-producing
RT   streptomycetes.";
RL   J. Gen. Microbiol. 136:1887-1894(1990).
CC   -!- FUNCTION: Involved in the biosynthesis of aklavinone which is an
CC       important precursor common to the formation of the clinically
CC       significant anthracyclines such as carminomycin, daunorubicin
CC       (daunomycin), rhodomycin, aclacinomycin T (aklavin) and aclacinomycin A
CC       (aclarubicin). These compounds are aromatic polyketide antibiotics that
CC       exhibit high cytotoxicity and are widely applied in the chemotherapy of
CC       a variety of cancers. Catalyzes the methyl esterification of aklanonic
CC       acid to yield aklanonic acid methyl ester. {ECO:0000269|PubMed:7836284,
CC       ECO:0000269|Ref.2, ECO:0000269|Ref.3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aklanonate + S-adenosyl-L-methionine = methyl aklanonate + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:37875, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:77987, ChEBI:CHEBI:77988;
CC         EC=2.1.1.288; Evidence={ECO:0000269|PubMed:7836284};
CC   -!- PATHWAY: Antibiotic biosynthesis; daunorubicin biosynthesis.
CC   -!- PATHWAY: Antibiotic biosynthesis; carminomycin biosynthesis.
CC   -!- PATHWAY: Antibiotic biosynthesis; rhodomycin biosynthesis.
CC   -!- PATHWAY: Antibiotic biosynthesis; aclacinomycin biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:7836284}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate aklanonate.
CC       {ECO:0000269|Ref.2, ECO:0000269|Ref.3}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. DnrC family.
CC       {ECO:0000305}.
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DR   EMBL; L35154; AAB16936.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q55214; -.
DR   SMR; Q55214; -.
DR   PRIDE; Q55214; -.
DR   KEGG; ag:AAB16936; -.
DR   BioCyc; MetaCyc:MON-18181; -.
DR   BRENDA; 2.1.1.288; 1284.
DR   UniPathway; UPA00054; -.
DR   UniPathway; UPA01040; -.
DR   UniPathway; UPA01042; -.
DR   UniPathway; UPA01043; -.
DR   GO; GO:0008168; F:methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR   GO; GO:1901771; P:daunorubicin biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0044598; P:doxorubicin metabolic process; IDA:UniProtKB.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR041698; Methyltransf_25.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF13649; Methyltransf_25; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..220
FT                   /note="Aklanonic acid methyltransferase DauC"
FT                   /id="PRO_0000425669"
SQ   SEQUENCE   220 AA;  24320 MW;  BD3FC5735886EACD CRC64;
     MQDSSYKKQV TQAFDQSSST YDRLGVEFFT PMGRRLVDIS EPVTGERVLD IGCGRGACLF
     PAAEKVGSQG CVHGIDIAPG MIEEARKEAT ERGLRNISLM VMDAETPGFP ARSFDLVMGS
     YSVIFLPDAV GALARYADIL DHGGRIAFTS PVFRAGTFPF LPPEFTPLIP QALLEHLPEQ
     WRPEALVRRF NSWLERAEDL VRTLEGCGYA RLRQSTSRCG