ID   DMPM_STRAD              Reviewed;         376 AA.
AC   P42712;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=O-demethylpuromycin-O-methyltransferase;
DE            EC=2.1.1.38;
GN   Name=dmpM;
OS   Streptomyces alboniger.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces aurantiacus group.
OX   NCBI_TaxID=132473;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 12461 / DSM 40043 / JCM 4309 / NBRC 12738 / NCIMB 13007 / NRRL
RC   B-2403;
RX   PubMed=1756982; DOI=10.1016/0378-1119(91)90588-3;
RA   Lacalle R.A., Ruiz D., Jimenez A.;
RT   "Molecular analysis of the dmpM gene encoding an O-demethyl puromycin O-
RT   methyltransferase from Streptomyces alboniger.";
RL   Gene 109:55-61(1991).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-demethylpuromycin + S-adenosyl-L-methionine = H(+) +
CC         puromycin + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:22280,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58037,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:60255; EC=2.1.1.38;
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR   EMBL; M74560; AAB00531.1; -; Genomic_DNA.
DR   AlphaFoldDB; P42712; -.
DR   SMR; P42712; -.
DR   KEGG; ag:AAB00531; -.
DR   BioCyc; MetaCyc:MON-13985; -.
DR   GO; GO:0030739; F:O-demethylpuromycin O-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR016461; COMT-like.
DR   InterPro; IPR001077; O_MeTrfase_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00891; Methyltransf_2; 1.
DR   PIRSF; PIRSF005739; O-mtase; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51683; SAM_OMT_II; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..376
FT                   /note="O-demethylpuromycin-O-methyltransferase"
FT                   /id="PRO_0000079944"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        281
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         235
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         261..263
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   376 AA;  40328 MW;  6B7AADA2D56BE7FC CRC64;
     MAPTEATRGG PADPAPAPEA HRGGHTEHAD PAEHAAQFGA QERILTLVWG YISSEILDLA
     TRLDLPDLMG TEERAAAELA ASLDTDPVAT LRLLRAFAAL GLAEETGAGR FRLTPAGHRL
     RTDVPDSLHA FVRQGMGVFR QAWSHFDHSI RTGEPAFDQV FGTDFFSYLS ERPELSGTFT
     SSMREATRTM STALAKEEEY DFSSYGTVVD IGGADGSLLA AVLSAHPGVE GVVFDSPEGA
     RDAAATLDAA GVGERGRVET GDFFTRVPGG GDLYVLKSIL HDWSDARSAD ILRTVRAAMP
     AHARLLVVEV LLPDTVDSSA HPLGYLSDLY MLVNMGGRER SERDLRSLLS DTGFRTTRVR
     TPPGLTPFSL IEAAPV