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 03-MAY-2023, entry version 122. DE RecName: Full=DNA topoisomerase 1 {ECO:0000255|HAMAP-Rule:MF_00952}; DE EC=5.6.2.1 {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}; OrderedLocusNames=PD_1767; OS Xylella fastidiosa (strain Temecula1 / ATCC 700964). OC Bacteria; Pseudomonadota; 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., Miyaki C.Y., RA Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A., RA Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S., RA Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H., RA Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L., RA Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L., RA Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S., RA Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F., RA Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G., RA Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A., RA Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L., RA Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.; RT "Comparative analyses of the complete genome sequences of Pierce's disease RT and citrus variegated chlorosis strains of Xylella fastidiosa."; RL J. Bacteriol. 185:1018-1026(2003). CC -!- FUNCTION: Releases the supercoiling and torsional tension of DNA, which CC is introduced during the DNA replication and transcription, by CC transiently cleaving and rejoining one strand of the DNA duplex. CC Introduces a single-strand break via transesterification at a target CC site in duplex DNA. The scissile phosphodiester is attacked by the CC catalytic tyrosine of the enzyme, resulting in the formation of a DNA- CC (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH CC DNA strand. The free DNA strand then undergoes passage around the CC unbroken strand, thus removing DNA supercoils. Finally, in the CC religation step, the DNA 3'-OH attacks the covalent intermediate to CC expel the active-site tyrosine and restore the DNA phosphodiester CC backbone. {ECO:0000255|HAMAP-Rule:MF_00952}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP-independent breakage of single-stranded DNA, followed by CC passage and rejoining.; EC=5.6.2.1; Evidence={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-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 --------------------------------------------------------------------------- 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 AlphaFoldDB; Q87AQ6; -. DR SMR; Q87AQ6; -. DR EnsemblBacteria; AAO29601; AAO29601; PD_1767. DR GeneID; 58017292; -. DR KEGG; xft:PD_1767; -. DR HOGENOM; CLU_002929_0_2_6; -. DR OMA; PECKYTR; -. DR Proteomes; UP000002516; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule. DR CDD; cd00186; TOP1Ac; 1. DR CDD; cd03363; TOPRIM_TopoIA_TopoI; 1. DR Gene3D; 3.40.50.140; -; 1. DR Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1. DR Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1. DR Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 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; IPR013826; Topo_IA_cen_sub3. 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 InterPro; IPR034149; TOPRIM_TopoI. DR PANTHER; PTHR42785; DNA TOPOISOMERASE, TYPE IA, CORE; 1. DR PANTHER; PTHR42785:SF1; OMEGA-PROTEIN; 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; Prokaryotic type I DNA topoisomerase; 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 DNA-binding; Isomerase; Magnesium; Metal-binding; Reference proteome; KW Topoisomerase. FT CHAIN 1..815 FT /note="DNA topoisomerase 1" FT /id="PRO_0000145173" FT DOMAIN 3..119 FT /note="Toprim" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT REGION 167..172 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT REGION 759..815 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 770..805 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 308 FT /note="O-(5'-phospho-DNA)-tyrosine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT BINDING 9 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT BINDING 82 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT BINDING 82 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT BINDING 84 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT SITE 33 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT SITE 143 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT SITE 144 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT SITE 147 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT SITE 159 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT SITE 310 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT SITE 505 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-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 //