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 19-JAN-2010, entry version 53.
DE RecName: Full=Multifunctional cyclase-dehydratase-3-O-methyl transferase tcmN;
GN Name=tcmN;
OS Streptomyces glaucescens.
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Streptomycineae; Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1907;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 40716 / ETH 22794 / GLA.0;
RX MEDLINE=92193265; PubMed=1548230;
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
RT that the tcmN gene encodes a multifunctional cyclase-dehydratase-O-
RT methyl transferase.";
RL J. Bacteriol. 174:1810-1820(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
RC STRAIN=DSM 40716 / ETH 22794 / GLA.0;
RX MEDLINE=90060035; PubMed=2684656;
RA Bibb M.J., Biro S., Motamedi H., Collins J.F., Hutchinson C.R.;
RT "Analysis of the nucleotide sequence of the Streptomyces glaucescens
RT tcmI 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
CC early, partially cyclized intermediate, while the C-terminal
CC domain catalyzes the 3-O-methylation of one or more later
CC intermediates in the biosynthetic pathway. Catalyzes the
CC methylation of tetracenomycin D3 (Tcm D3) to yield Tcm B3.
CC Catalyzes as well the following side reactions: methylation of 8-
CC O-methyl-Tcm D3 to yield Tcm E; and of 9-carboxymethyl-Tcm B3 to
CC yield Tcm A2.
CC -!- PATHWAY: Antibiotic biosynthesis; tetracenomycin C biosynthesis.
CC -!- DOMAIN: This multifunction enzyme is comprised of two structurally
CC and functionally independent domains.
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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 PDBsum; 2RER; -.
DR PDBsum; 2RES; -.
DR PDBsum; 2REZ; -.
DR SMR; P16559; 160-483.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR001077; O_MeTrfase_2.
DR InterPro; IPR005031; Polyket_cyc.
DR Pfam; PF00891; Methyltransf_2; 1.
DR Pfam; PF03364; Polyketide_cyc; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Methyltransferase;
KW Multifunctional enzyme; Transferase.
FT CHAIN 1 494 Multifunctional cyclase-dehydratase-3-O-
FT methyl transferase tcmN.
FT /FTId=PRO_0000072456.
FT STRAND 3 13
FT HELIX 15 22
FT HELIX 25 27
FT HELIX 28 31
FT STRAND 33 42
FT STRAND 48 54
FT STRAND 64 72
FT TURN 73 76
FT STRAND 77 84
FT STRAND 88 100
FT STRAND 103 114
FT HELIX 122 150
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
//
