ID   COUO_STRRH              Reviewed;         230 AA.
AC   Q9F8T9;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=C-methyltransferase CouO;
DE            EC=2.1.1.-;
DE   AltName: Full=Coumermycin biosynthesis protein O;
GN   Name=couO;
OS   Streptomyces rishiriensis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=68264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 14812 / DSM 40489 / JCM 4821 / NBRC 13407 / NRRL B-3239 /
RC   404Y3;
RX   PubMed=11036020; DOI=10.1128/aac.44.11.3040-3048.2000;
RA   Wang Z.X., Li S.M., Heide L.;
RT   "Identification of the coumermycin A(1) biosynthetic gene cluster of
RT   Streptomyces rishiriensis DSM 40489.";
RL   Antimicrob. Agents Chemother. 44:3040-3048(2000).
RN   [2]
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 14812 / DSM 40489 / JCM 4821 / NBRC 13407 / NRRL B-3239 /
RC   404Y3;
RX   PubMed=16274243; DOI=10.1021/bi051599o;
RA   Pacholec M., Tao J., Walsh C.T.;
RT   "CouO and NovO: C-methyltransferases for tailoring the aminocoumarin
RT   scaffold in coumermycin and novobiocin antibiotic biosynthesis.";
RL   Biochemistry 44:14969-14976(2005).
CC   -!- FUNCTION: Mediates C-methylation at the 8-position of the aminocoumarin
CC       moieties in coumermycin A1 in the biosynthetic pathway of coumermycin
CC       antibiotic. Active on both mono- and bis-amides for mono- and di-C-
CC       methylation adjacent to the phenolic hydroxyl before it is glycosylated
CC       by CouM. {ECO:0000269|PubMed:16274243}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=52.0 uM for desmethyl-monoamide {ECO:0000269|PubMed:16274243};
CC         KM=63.4 uM for monomethyl-diamide {ECO:0000269|PubMed:16274243};
CC         KM=63.8 uM for monomethyl-diamide {ECO:0000269|PubMed:16274243};
CC         KM=108.5 uM for desmethyl-novobiocic acid
CC         {ECO:0000269|PubMed:16274243};
CC         Note=kcat is 2.2 min(-1) with desmethyl-monoamide as substrate. kcat
CC         is 1.23 min(-1) with monomethyl-diamide as substrate. kcat is 1.38
CC         min(-1) with monomethyl-diamide as substrate. kcat is 1.71 min(-1)
CC         with desmethyl-diamide as substrate. kcat is 0.23 min(-1) with
CC         desmethyl-novobiocic acid as substrate.;
CC   -!- PATHWAY: Antibiotic biosynthesis.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF235050; AAG29793.1; -; Genomic_DNA.
DR   PDB; 5M58; X-ray; 2.05 A; A/B=1-230.
DR   PDBsum; 5M58; -.
DR   AlphaFoldDB; Q9F8T9; -.
DR   SMR; Q9F8T9; -.
DR   KEGG; ag:AAG29793; -.
DR   GO; GO:0008168; F:methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0032259; P:methylation; IDA:UniProtKB.
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   3D-structure; Antibiotic biosynthesis; Methyltransferase;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..230
FT                   /note="C-methyltransferase CouO"
FT                   /id="PRO_0000424003"
FT   HELIX           8..19
FT                   /evidence="ECO:0007829|PDB:5M58"
FT   HELIX           22..25
FT                   /evidence="ECO:0007829|PDB:5M58"
FT   HELIX           26..35
FT                   /evidence="ECO:0007829|PDB:5M58"
FT   STRAND          42..46
FT                   /evidence="ECO:0007829|PDB:5M58"
FT   HELIX           52..60
FT                   /evidence="ECO:0007829|PDB:5M58"
FT   STRAND          65..71
FT                   /evidence="ECO:0007829|PDB:5M58"
FT   HELIX           73..85
FT                   /evidence="ECO:0007829|PDB:5M58"
FT   STRAND          91..94
FT                   /evidence="ECO:0007829|PDB:5M58"
FT   HELIX           104..106
FT                   /evidence="ECO:0007829|PDB:5M58"
FT   TURN            107..109
FT                   /evidence="ECO:0007829|PDB:5M58"
FT   STRAND          110..117
FT                   /evidence="ECO:0007829|PDB:5M58"
FT   HELIX           119..121
FT                   /evidence="ECO:0007829|PDB:5M58"
FT   HELIX           125..135
FT                   /evidence="ECO:0007829|PDB:5M58"
FT   STRAND          136..147
FT                   /evidence="ECO:0007829|PDB:5M58"
FT   HELIX           150..152
FT                   /evidence="ECO:0007829|PDB:5M58"
FT   HELIX           155..166
FT                   /evidence="ECO:0007829|PDB:5M58"
FT   HELIX           172..183
FT                   /evidence="ECO:0007829|PDB:5M58"
FT   HELIX           188..201
FT                   /evidence="ECO:0007829|PDB:5M58"
FT   STRAND          204..212
FT                   /evidence="ECO:0007829|PDB:5M58"
FT   STRAND          214..218
FT                   /evidence="ECO:0007829|PDB:5M58"
FT   STRAND          220..227
FT                   /evidence="ECO:0007829|PDB:5M58"
SQ   SEQUENCE   230 AA;  25649 MW;  EB941000D64B2E57 CRC64;
     MKIEPITGSE AEAFHRMGSR AFERYNEFVD LLVGAGIADG QTVVDLCCGS GELEIILTSR
     FPSLNLVGVD LSEDMVRIAR DYAAEQGKEL EFRHGDAQSP AGMEDLLGKA DLVVSRHAFH
     RLTRLPAGFD TMLRLVKPGG AILNVSFLHL SDFDEPGFRT WVRFLKERPW DAEMQVAWAL
     AHYYAPRLQD YRDALAQAAD ETPVSEQRIW VDDQGYGVAT VKCFARRAAA