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 13-SEP-2023, entry version 93. 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; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 eggNOG; ENOG50332TT; Bacteria. DR OrthoDB; 4147507at2; -. DR BioCyc; MetaCyc:MONOMER-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; Dimeric alpha+beta barrel; 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; Dimeric alpha+beta barrel; 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 FT wild-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 FT wild-type." FT /evidence="ECO:0000269|PubMed:15231835" FT MUTAGEN 40 FT /note="R->G: Relative activity reduced to 10% of FT wild-type." FT /evidence="ECO:0000269|PubMed:15231835" FT MUTAGEN 40 FT /note="R->K: Relative activity reduced to 16% of FT wild-type." FT /evidence="ECO:0000269|PubMed:15231835" FT MUTAGEN 51 FT /note="H->A: Relative activity reduced to 16% of FT wild-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 //