TCMN_STRGA
ID TCMN_STRGA Reviewed; 494 AA.
AC P16559;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Multifunctional cyclase-dehydratase-3-O-methyl transferase TcmN;
DE EC=2.1.1.-;
GN Name=tcmN;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
RC STRAIN=DSM 40716 / ETH 22794 / Tue 49;
RX PubMed=2684656; DOI=10.1002/j.1460-2075.1989.tb08414.x;
RA Bibb M.J., Biro S., Motamedi H., Collins J.F., Hutchinson C.R.;
RT "Analysis of the nucleotide sequence of the Streptomyces glaucescens tcmI
RT genes provides key information about the enzymology of polyketide
RT antibiotic biosynthesis.";
RL EMBO J. 8:2727-2736(1989).
CC -!- FUNCTION: The N-terminal domain enhances the formation of an early,
CC partially cyclized intermediate, while the C-terminal domain catalyzes
CC the 3-O-methylation of one or more later intermediates in the
CC biosynthetic pathway. Catalyzes the methylation of tetracenomycin D3
CC (Tcm D3) to yield Tcm B3. Catalyzes as well the following side
CC reactions: methylation of 8-O-methyl-Tcm D3 to yield Tcm E; and of 9-
CC carboxymethyl-Tcm B3 to yield Tcm A2.
CC -!- PATHWAY: Antibiotic biosynthesis; tetracenomycin C biosynthesis.
CC -!- DOMAIN: This multifunction enzyme is comprised of two structurally and
CC functionally independent domains.
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; AAA67518.1; -; Genomic_DNA.
DR EMBL; X15312; CAB38457.1; -; Genomic_DNA.
DR PIR; B42276; S27696.
DR PDB; 2RER; X-ray; 1.90 A; A=1-170.
DR PDB; 2RES; X-ray; 2.20 A; A=1-170.
DR PDB; 2REZ; X-ray; 1.95 A; A=1-154.
DR PDB; 3TVQ; X-ray; 1.67 A; A=1-169.
DR PDBsum; 2RER; -.
DR PDBsum; 2RES; -.
DR PDBsum; 2REZ; -.
DR PDBsum; 3TVQ; -.
DR AlphaFoldDB; P16559; -.
DR SMR; P16559; -.
DR STRING; 1907.SGLAU_26370; -.
DR eggNOG; COG2226; Bacteria.
DR eggNOG; COG2867; Bacteria.
DR OMA; CELWDLA; -.
DR BioCyc; MetaCyc:MON-18604; -.
DR BRENDA; 2.3.1.235; 6020.
DR UniPathway; UPA00174; -.
DR EvolutionaryTrace; P16559; -.
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; 3.30.530.20; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR005031; COQ10_START.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR023393; START-like_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00891; Methyltransf_2; 1.
DR Pfam; PF03364; Polyketide_cyc; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Methyltransferase;
KW Multifunctional enzyme; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..494
FT /note="Multifunctional cyclase-dehydratase-3-O-methyl
FT transferase TcmN"
FT /id="PRO_0000072456"
FT ACT_SITE 405
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 358
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 384..386
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT STRAND 3..13
FT /evidence="ECO:0007829|PDB:3TVQ"
FT HELIX 15..22
FT /evidence="ECO:0007829|PDB:3TVQ"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:3TVQ"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:3TVQ"
FT STRAND 35..44
FT /evidence="ECO:0007829|PDB:3TVQ"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:3TVQ"
FT STRAND 64..72
FT /evidence="ECO:0007829|PDB:3TVQ"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:3TVQ"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:3TVQ"
FT STRAND 88..100
FT /evidence="ECO:0007829|PDB:3TVQ"
FT STRAND 103..114
FT /evidence="ECO:0007829|PDB:3TVQ"
FT HELIX 122..151
FT /evidence="ECO:0007829|PDB:3TVQ"
SQ SEQUENCE 494 AA; 55930 MW; 6E153D32782F66B5 CRC64;
MAARTDNSIV VNAPFELVWD VTNDIEAWPE LFSEYAEAEI LRQDGDGFDF RLKTRPDANG
RVWEWVSHRV PDKGSRTVRA HRVETGPFAY MNLHWTYRAV AGGTEMRWVQ EFDMKPGAPF
DNAHMTAHLN TTTRANMERI KKIIEDRHRE GQRTPASVLP TELHAQQLLL LAASGRLARI
VHVLTELRIA DLLADGPRHV AELAKETDTH ELSLYRVLRS AASVGVFAEG PVRTFSATPL
SDGLRTGNPD GVLPLVKYNN MELTRRPYDE IMHSVRTGEP AFRRVFGSSF FEHLEANPEA
GEFFERFMAH WSRRLVLDGL ADQGMERFSR IADLGGGDGW FLAQILRRHP HATGLLMDLP
RVAASAGPVL EEAKVADRVT VLPGDFFTDP VPTGYDAYLF KGVLHNWSDE RAVTVLRRVR
EAIGDDDARL LIFDQVMAPE NEWDHAKLLD IDMLVLFGGR ERVLAEWRQL LLEADFDIVN
TPSHTWTTLE CRPV
