ID   MDMC_STRMY              Reviewed;         221 AA.
AC   Q00719;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=O-methyltransferase MdmC;
DE            EC=2.1.1.-;
GN   Name=mdmC;
OS   Streptomyces mycarofaciens.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1949;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 21454 / JCM 4939 / NBRC 13792;
RX   PubMed=1629172; DOI=10.1128/jb.174.15.5141-5144.1992;
RA   Hara O., Hutchinson C.R.;
RT   "A macrolide 3-O-acyltransferase gene from the midecamycin-producing
RT   species Streptomyces mycarofaciens.";
RL   J. Bacteriol. 174:5141-5144(1992).
CC   -!- FUNCTION: 4-O-methyltransferase for the lactone ring of midecamycin and
CC       other macrolide antibiotics.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-dependent O-methyltransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01019}.
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DR   EMBL; M93958; AAA26782.1; -; Genomic_DNA.
DR   PIR; B42719; B42719.
DR   AlphaFoldDB; Q00719; -.
DR   SMR; Q00719; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002935; SAM_O-MeTrfase.
DR   Pfam; PF01596; Methyltransf_3; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51682; SAM_OMT_I; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Metal-binding; Methyltransferase;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..221
FT                   /note="O-methyltransferase MdmC"
FT                   /id="PRO_0000096334"
FT   BINDING         44
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         66
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         68..69
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         74
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         92
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         93
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         121
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         143
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         145
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         169
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         170
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
SQ   SEQUENCE   221 AA;  24052 MW;  EE22BD193E297ACB CRC64;
     MADQTTLSPA LLDYARSVAL REDGLLRELH DMTAQLPGGR AMQIMPEEAQ FLGLLIRLVG
     ARRVLEIGTF TGYSTLCMAR ALPAGGRIVT CDISDKWPGI GAPFWQRAGV DGLIDLRIGD
     AARTLAELRE RDGDGAFDLV FVDADKAGYL HYYEQALALV RPGGLVAIDN TLFFGRVADP
     AADDPDTVAV RTLNDLLRDD ERVDIALLTV ADGITLARRR E