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DNRC_STRPE
ID   DNRC_STRPE              Reviewed;         286 AA.
AC   Q54818;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Aklanonic acid methyltransferase DnrC;
DE            Short=AAMT;
DE            EC=2.1.1.288;
GN   Name=dnrC;
OS   Streptomyces peucetius.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1950;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29050 / DSM 40754 / JCM 9920 / NBRC 100596 / NCIMB 10972;
RX   PubMed=7828855; DOI=10.1016/0378-1119(94)90625-4;
RA   Grimm A., Madduri K., Ali A., Hutchinson C.R.;
RT   "Characterization of the Streptomyces peucetius ATCC 29050 genes encoding
RT   doxorubicin polyketide synthase.";
RL   Gene 151:1-10(1994).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 29050 / DSM 40754 / JCM 9920 / NBRC 100596 / NCIMB 10972;
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 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.
CC       {ECO:0000269|PubMed:7601857}.
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:7601857};
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:0000250}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. DnrC family.
CC       {ECO:0000305}.
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DR   EMBL; L35560; AAA65210.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q54818; -.
DR   SMR; Q54818; -.
DR   KEGG; ag:AAA65210; -.
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; IPR025714; Methyltranfer_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF13847; Methyltransf_31; 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..286
FT                   /note="Aklanonic acid methyltransferase DnrC"
FT                   /id="PRO_0000425670"
SQ   SEQUENCE   286 AA;  31676 MW;  AEEE0056F7B839F6 CRC64;
     MQDSSYKEQV TQAFDQSSST YDRLGVEFFT PMGRPLVEIS EPVTGERVLD IGCGRGACLF
     PAAEKVGPQG RVHGIDIAPG MIEEARKEAA ERGLRNIALD VMDAETPELP ARSFDLVMGS
     YSVIFLPDAV GALARYAGIL DHGGRIAFTS PVFRAGTFPF LPPEFTPLIP QALLEHLPEQ
     WRPEALVRRF NSWLERAEDL LRTLERCGYT SVAVTDEPVR MTALSSEAWV DWSHTQGMRL
     LWQNLPQAQR TELRARLVEG LDKLSDATGA LAIDVPVRFV TARVAH
 
 
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