ID TOP1_XYLFT Reviewed; 815 AA. AC Q87AQ6; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2003, sequence version 1. DT 07-SEP-2016, entry version 94. DE RecName: Full=DNA topoisomerase 1 {ECO:0000255|HAMAP-Rule:MF_00952}; DE EC=5.99.1.2 {ECO:0000255|HAMAP-Rule:MF_00952}; DE AltName: Full=DNA topoisomerase I {ECO:0000255|HAMAP-Rule:MF_00952}; DE AltName: Full=Omega-protein; DE AltName: Full=Relaxing enzyme; DE AltName: Full=Swivelase; DE AltName: Full=Untwisting enzyme; GN Name=topA {ECO:0000255|HAMAP-Rule:MF_00952}; GN OrderedLocusNames=PD_1767; OS Xylella fastidiosa (strain Temecula1 / ATCC 700964). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=183190; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Temecula1 / ATCC 700964; RX PubMed=12533478; DOI=10.1128/JB.185.3.1018-1026.2003; RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., RA Miyaki C.Y., Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., RA Takita M.A., Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., RA Goldman M.H.S., Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., RA Carrer H., Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., RA Coutinho L.L., Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., RA Marino C.L., Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., RA Baia G.S., Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., RA da Cunha A.F., Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., RA Leoni S.G., Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., RA de Souza A.A., Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., RA Civerolo E.L., Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., RA Kitajima J.P.; RT "Comparative analyses of the complete genome sequences of Pierce's RT disease and citrus variegated chlorosis strains of Xylella RT fastidiosa."; RL J. Bacteriol. 185:1018-1026(2003). CC -!- FUNCTION: Releases the supercoiling and torsional tension of DNA, CC which is introduced during the DNA replication and transcription, CC by transiently cleaving and rejoining one strand of the DNA CC duplex. Introduces a single-strand break via transesterification CC at a target site in duplex DNA. The scissile phosphodiester is CC attacked by the catalytic tyrosine of the enzyme, resulting in the CC formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the CC expulsion of a 3'-OH DNA strand. The free DNA strand then CC undergoes passage around the unbroken strand, thus removing DNA CC supercoils. Finally, in the religation step, the DNA 3'-OH attacks CC the covalent intermediate to expel the active-site tyrosine and CC restore the DNA phosphodiester backbone. {ECO:0000255|HAMAP- CC Rule:MF_00952}. CC -!- CATALYTIC ACTIVITY: ATP-independent breakage of single-stranded CC DNA, followed by passage and rejoining. {ECO:0000255|HAMAP- CC Rule:MF_00952}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00952}; CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00952}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00952}. CC -!- SIMILARITY: Belongs to the type IA topoisomerase family. CC {ECO:0000255|HAMAP-Rule:MF_00952}. CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000255|HAMAP- CC Rule:MF_00952}. 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; AE009442; AAO29601.1; -; Genomic_DNA. DR RefSeq; WP_004089635.1; NC_004556.1. DR ProteinModelPortal; Q87AQ6; -. DR EnsemblBacteria; AAO29601; AAO29601; PD_1767. DR KEGG; xft:PD_1767; -. DR PATRIC; 24151979; VBIXylFas71109_2289. DR KO; K03168; -. DR OMA; FGPFIKW; -. DR BioCyc; XFAS183190:GIX4-1767-MONOMER; -. DR Proteomes; UP000002516; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003917; F:DNA topoisomerase type I activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP. DR CDD; cd00186; TOP1Ac; 1. DR Gene3D; 1.10.460.10; -; 2. DR Gene3D; 2.70.20.10; -; 2. DR Gene3D; 3.40.50.140; -; 1. DR HAMAP; MF_00952; Topoisom_1_prok; 1. DR InterPro; IPR000380; Topo_IA. DR InterPro; IPR003601; Topo_IA_2. DR InterPro; IPR023406; Topo_IA_AS. DR InterPro; IPR013497; Topo_IA_cen. DR InterPro; IPR013824; Topo_IA_cen_sub1. DR InterPro; IPR013825; Topo_IA_cen_sub2. DR InterPro; IPR023405; Topo_IA_core_domain. DR InterPro; IPR003602; Topo_IA_DNA-bd_dom. DR InterPro; IPR005733; TopoI_bac-type. DR InterPro; IPR028612; Topoisom_1_IA. DR InterPro; IPR025589; Toprim_C_rpt. DR InterPro; IPR006171; Toprim_domain. DR PANTHER; PTHR11390; PTHR11390; 1. DR Pfam; PF01131; Topoisom_bac; 1. DR Pfam; PF01751; Toprim; 1. DR Pfam; PF13368; Toprim_C_rpt; 3. DR PRINTS; PR00417; PRTPISMRASEI. DR SMART; SM00437; TOP1Ac; 1. DR SMART; SM00436; TOP1Bc; 1. DR SMART; SM00493; TOPRIM; 1. DR SUPFAM; SSF56712; SSF56712; 1. DR TIGRFAMs; TIGR01051; topA_bact; 1. DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Isomerase; Magnesium; Metal-binding; KW Topoisomerase. FT CHAIN 1 815 DNA topoisomerase 1. FT /FTId=PRO_0000145173. FT DOMAIN 3 119 Toprim. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT REGION 167 172 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT ACT_SITE 308 308 O-(5'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00952}. FT METAL 9 9 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00952}. FT METAL 82 82 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00952}. FT METAL 82 82 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT METAL 84 84 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 33 33 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 143 143 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 144 144 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 147 147 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 159 159 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 310 310 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 505 505 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. SQ SEQUENCE 815 AA; 91802 MW; 2F23C4675BEA8363 CRC64; MPKHLLIVES PAKAKTINKY LGKDFTVLAS YGHVRDLVPK EGAVDPENGF AMRYDLIDKN EKHVEAITKA AKTADSIYLA TDPDREGEAI SWHISEILKE RGLLKDKPMQ RIVFTEITPR AIKEAIQKPR MIASDLVDAQ QARRALDYLV GFNLSPVLWR KVQRGLSAGR VQSPALRMIV EREEEIEAFI TREYWSIHAE CTHPAQHFSA KLIKLDGKKF EQFTITDSDT AAAAQRRIQQ AAQGRLHITD VTNKERKRRP APPFITSTLQ QEASRKLGFT TRKTMQIAQK LYEGIALGEE GSVGLITYMR TDSVNLSLDA LSEIRDIIAR DYGTNALPDK PNVYTTKSKN AQEAHEAVRP TSALRTPTQV APYLSNEEHR LYELVWKRTV ASQMIPAILN TTSVDLAAGN EHVFRATGTT VVVQGFLAVY EEGKDNKNAE DDDEGRKLPV MKTGENVPLE RILTEQHFTQ PPPRYTEAAL VKALEEYGIG RPSTYASIIQ TLLFRKYVDM EGRSFRPTDI GRAVSKFLSS HFTQYVDYDF TAHLEDELDA ISRGEEEWIP LMKKFWVPFK ELVEDKKDSL DKTDAGSVRL LGIDPTSGKE VSARIGRFGP MVQIGTVDDE EKPRFASLRP NQSIYSISLE EAIELFKMPR VLGEDQSQQV SVGIGRFGPF AKRGSTYVSL KSEDDPYTID LARATLLINE KEEIARNRII KDFENSQIQV LNGRFGPYIS DGKLNGKIPK DREPASLTLE EAQQLLINTG KPARKNFSTK KTATKNETRK QTTKKRTTDA KATKKVSDKP VKKQIKKRIA PNITQ //