TCMO_STRGA
ID TCMO_STRGA Reviewed; 339 AA.
AC P39896;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Tetracenomycin polyketide synthesis 8-O-methyl transferase TcmO;
DE EC=2.1.1.-;
GN Name=tcmO;
OS Streptomyces glaucescens.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1907;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 40716 / ETH 22794 / Tue 49;
RX PubMed=1548230; DOI=10.1128/jb.174.6.1810-1820.1992;
RA Summers R.G., Wendt-Pienkowski E., Motamedi H., Hutchinson C.R.;
RT "Nucleotide sequence of the tcmII-tcmIV region of the tetracenomycin C
RT biosynthetic gene cluster of Streptomyces glaucescens and evidence that the
RT tcmN gene encodes a multifunctional cyclase-dehydratase-O-methyl
RT transferase.";
RL J. Bacteriol. 174:1810-1820(1992).
CC -!- PATHWAY: Antibiotic biosynthesis; tetracenomycin C biosynthesis.
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; M80674; AAA67519.1; -; Genomic_DNA.
DR PIR; C42276; C42276.
DR RefSeq; WP_043504920.1; NZ_CP009438.1.
DR AlphaFoldDB; P39896; -.
DR SMR; P39896; -.
DR STRING; 1907.SGLAU_26375; -.
DR eggNOG; COG2345; Bacteria.
DR OMA; NTNHGEL; -.
DR OrthoDB; 1213908at2; -.
DR BioCyc; MetaCyc:MON-18605; -.
DR UniPathway; UPA00174; -.
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; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR031725; ASMT_dimerisation.
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 PANTHER; PTHR11746; PTHR11746; 1.
DR Pfam; PF16864; Dimerisation2; 1.
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 Antibiotic biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..339
FT /note="Tetracenomycin polyketide synthesis 8-O-methyl
FT transferase TcmO"
FT /id="PRO_0000072457"
FT ACT_SITE 246
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 200
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 226..228
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 339 AA; 37035 MW; B228B66B24217F80 CRC64;
MTPHTHVRGP GDILQLTMAF YGSRALISAV ELDLFTLLAG KPLPLGELCE RAGIHPRGAR
DFLDALVALG LLEREGEDTY RNSPAADRHL DRRKPGYVGG YARLADTKLF PVWARLTEAL
RTGEKQVPSQ GGFFGGYADP EAARGFLGAM DAVNGGVGHS LAGALDWTEY SSFVDLGGAR
GNLAAHLHRA HPHLRATCFD LPEMEPFFQE HMKSLETTDQ VRFAGGDFFT DPLPRADVFI
VGHILHYFGL RQREALIARI HQALTPGGAV LVYDRMIDDD RRSAALSLLG SLNMLLTSDE
GREYTPAECV RWLSDAGFTD VRTTAVSGPD TLAIGRKPR