TCMI_STRGA
ID TCMI_STRGA Reviewed; 109 AA.
AC P39890;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Tetracenomycin F2 cyclase;
DE EC=4.2.1.154;
DE AltName: Full=Tetracenomycin polyketide synthesis protein TcmI;
GN Name=tcmI;
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=1592819; DOI=10.1128/jb.174.11.3651-3658.1992;
RA Guilfoile P.G., Hutchinson C.R.;
RT "Sequence and transcriptional analysis of the Streptomyces glaucescens
RT tcmAR tetracenomycin C resistance and repressor gene loci.";
RL J. Bacteriol. 174:3651-3658(1992).
RN [2]
RP PROTEIN SEQUENCE OF 2-15, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=WMH1068;
RX PubMed=8218177; DOI=10.1021/bi00092a026;
RA Shen B., Hutchinson C.R.;
RT "Tetracenomycin F2 cyclase: intramolecular aldol condensation in the
RT biosynthesis of tetracenomycin C in Streptomyces glaucescens.";
RL Biochemistry 32:11149-11154(1993).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF HIS-26;
RP ASP-27; ARG-40 AND HIS-51.
RX PubMed=15231835; DOI=10.1074/jbc.m406144200;
RA Thompson T.B., Katayama K., Watanabe K., Hutchinson C.R., Rayment I.;
RT "Structural and functional analysis of tetracenomycin F2 cyclase from
RT Streptomyces glaucescens. A type II polyketide cyclase.";
RL J. Biol. Chem. 279:37956-37963(2004).
CC -!- FUNCTION: Catalyzing the conversion of tetracenomycin F2 to
CC tetracenomycin F1. {ECO:0000269|PubMed:8218177}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + tetracenomycin F2 = H2O + tetracenomycin F1;
CC Xref=Rhea:RHEA:38851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:74931, ChEBI:CHEBI:77982; EC=4.2.1.154;
CC Evidence={ECO:0000269|PubMed:8218177};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=121 uM for tetracenomycin F2 {ECO:0000269|PubMed:8218177};
CC Vmax=704 nmol/min/mg enzyme {ECO:0000269|PubMed:8218177};
CC pH dependence:
CC Optimum pH is 6-6.5. {ECO:0000269|PubMed:8218177};
CC -!- PATHWAY: Antibiotic biosynthesis; tetracenomycin C biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15231835}.
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DR EMBL; M80674; AAA67513.1; -; Genomic_DNA.
DR PIR; B53291; B53291.
DR RefSeq; WP_043504911.1; NZ_CP009438.1.
DR PDB; 1TUW; X-ray; 1.90 A; A=1-109.
DR PDBsum; 1TUW; -.
DR AlphaFoldDB; P39890; -.
DR SMR; P39890; -.
DR STRING; 1907.SGLAU_26345; -.
DR PRIDE; P39890; -.
DR eggNOG; ENOG50332TT; Bacteria.
DR OrthoDB; 1788762at2; -.
DR BioCyc; MetaCyc:MON-18608; -.
DR BRENDA; 4.2.1.154; 6020.
DR UniPathway; UPA00174; -.
DR EvolutionaryTrace; P39890; -.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0030639; P:polyketide biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.70.1090; -; 1.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR006765; Polyketide_synth_cyclase.
DR InterPro; IPR038474; Polyketide_synth_cyclase_sf.
DR Pfam; PF04673; Cyclase_polyket; 1.
DR SUPFAM; SSF54909; SSF54909; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Direct protein sequencing; Lyase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8218177"
FT CHAIN 2..109
FT /note="Tetracenomycin F2 cyclase"
FT /id="PRO_0000072454"
FT MUTAGEN 26
FT /note="H->A: Relative activity reduced to 15% of wild-
FT type."
FT /evidence="ECO:0000269|PubMed:15231835"
FT MUTAGEN 26
FT /note="H->Q: No effect."
FT /evidence="ECO:0000269|PubMed:15231835"
FT MUTAGEN 27
FT /note="D->N: Relative activity reduced to 14% of wild-
FT type."
FT /evidence="ECO:0000269|PubMed:15231835"
FT MUTAGEN 40
FT /note="R->G: Relative activity reduced to 10% of wild-
FT type."
FT /evidence="ECO:0000269|PubMed:15231835"
FT MUTAGEN 40
FT /note="R->K: Relative activity reduced to 16% of wild-
FT type."
FT /evidence="ECO:0000269|PubMed:15231835"
FT MUTAGEN 51
FT /note="H->A: Relative activity reduced to 16% of wild-
FT type."
FT /evidence="ECO:0000269|PubMed:15231835"
FT MUTAGEN 51
FT /note="H->Q: No effect."
FT /evidence="ECO:0000269|PubMed:15231835"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:1TUW"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1TUW"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:1TUW"
FT HELIX 31..35
FT /evidence="ECO:0007829|PDB:1TUW"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:1TUW"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:1TUW"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:1TUW"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1TUW"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:1TUW"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:1TUW"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:1TUW"
SQ SEQUENCE 109 AA; 12861 MW; 1F9E3EC9E1B90593 CRC64;
MAYRALMVLR MDPADAEHVA AAFAEHDTTE LPLEIGVRRR VLFRFHDLYM HLIEADDDIM
ERLYQARSHP LFQEVNERVG QYLTPYAQDW EELKDSKAEV FYSWTAPDS
