ID TOP1_PASMU Reviewed; 868 AA. AC Q9CN30; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 20-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 146. 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=PM0615; OS Pasteurella multocida (strain Pm70). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Pasteurella. OX NCBI_TaxID=272843; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pm70; RX PubMed=11248100; DOI=10.1073/pnas.051634598; RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.; RT "Complete genomic sequence of Pasteurella multocida Pm70."; RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001). 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; Evidence={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 --------------------------------------------------------------------------- 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; AE004439; AAK02699.1; -; Genomic_DNA. DR RefSeq; WP_010906754.1; NC_002663.1. DR AlphaFoldDB; Q9CN30; -. DR SMR; Q9CN30; -. DR STRING; 272843.PM0615; -. DR EnsemblBacteria; AAK02699; AAK02699; PM0615. DR KEGG; pmu:PM0615; -. DR HOGENOM; CLU_002929_4_1_6; -. DR OrthoDB; 9804262at2; -. DR Proteomes; UP000000809; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. 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; 2.20.25.10; -; 1. DR Gene3D; 3.40.50.140; -; 1. DR Gene3D; 3.30.65.10; Bacterial Topoisomerase I, domain 1; 3. 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; IPR049330; TOP1_Znf. 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; IPR013498; Topo_IA_Znf. DR InterPro; IPR005733; TopoI_bac-type. DR InterPro; IPR013263; TopoI_Znr_bac. DR InterPro; IPR028612; Topoisom_1_IA. DR InterPro; IPR006171; TOPRIM_domain. DR InterPro; IPR034149; TOPRIM_TopoI. DR NCBIfam; TIGR01051; topA_bact; 1. DR PANTHER; PTHR42785:SF1; DNA TOPOISOMERASE; 1. DR PANTHER; PTHR42785; DNA TOPOISOMERASE, TYPE IA, CORE; 1. DR Pfam; PF21372; TOP1_ZnF; 1. DR Pfam; PF08272; Topo_Zn_Ribbon; 2. DR Pfam; PF01131; Topoisom_bac; 1. DR Pfam; PF01751; Toprim; 1. DR Pfam; PF01396; zf-C4_Topoisom; 2. 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 SUPFAM; SSF57783; Zinc beta-ribbon; 3. DR PROSITE; PS00396; TOPO_IA_1; 1. DR PROSITE; PS52039; TOPO_IA_2; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW DNA-binding; Isomerase; Magnesium; Metal-binding; Reference proteome; KW Repeat; Topoisomerase; Zinc; Zinc-finger. FT CHAIN 1..868 FT /note="DNA topoisomerase 1" FT /id="PRO_0000145160" FT DOMAIN 3..148 FT /note="Toprim" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT DOMAIN 164..581 FT /note="Topo IA-type catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01383" FT ZN_FING 605..636 FT /note="C4-type 1" FT ZN_FING 667..694 FT /note="C4-type 2" FT ZN_FING 716..739 FT /note="C4-type 3" FT REGION 198..203 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT ACT_SITE 325 FT /note="O-(5'-phospho-DNA)-tyrosine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01383" FT BINDING 9 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT BINDING 117 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" 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 174 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT SITE 175 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT SITE 178 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT SITE 190 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT SITE 327 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT SITE 513 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" SQ SEQUENCE 868 AA; 98048 MW; E63DF724C4B4ED8D CRC64; MSKSLVIVES PAKAKTINKY LGSNYVVKSS VGHIRDLPTV GSSNGEKAKA ISTKGLSAEE KSAIKQEKDR NALVKRMGID PYHQWKANYQ ILPGKEKVVA ELKSLAKKAD HIYLATDLDR EGEAIAWHLR EVIGGDDARF SRVVFNEITK NAIQQAFEKP EQLNLDRVNA QQTRRFLDRV VGFMVSPLLW KKVARGLSAG RVQSVAVKLV VEREREIKAF QPEEYWEIDV LTQTQAKQAL RLAVTQFKGK KFEPKNATQA QSAVDFLQHA DYVVSDLETK PTHSRAKAPF ITSTLQQTAS TRLGFGVKKT MMLAQRLYEA GYITYMRTDS TNLSQDALKM VRGYIQSHYG ESYLPSKPVF YSSKENAQEA HEAIRPSDVN TLAEQLTGMD KDAVRLYDLI WRQFVACQMP AAQYDSTTVT VRAGEYELKA KGRILRFDGW TKVLPTMSKN AEDQVLPDVQ LNEKLHLEHV LPEQLFTKPP ARFSEAALVK ELEKRGIGRP STYAAIISTI QERGYVRVEN RRFYAEKMGE IVTDRLNQSF TALMNYDFTA NMENILDQIA NGEKNWKTEL NQFFKDFSQQ LSQAELDELE GGMKPNSLVP TDINCPTCGR KMAIRTASTG VFLGCSGYAL PPKERCKTTM NLIPEAELLN VLDEASETKA LMERKRCPKC GTAMDSYLID PERKIHICGH NPNCDGYVLE QGSFKIKGYD GPIVECDKCG ADMHLKLGRF GKYMGCTSCD NTRKILKSGE VAPPKEEPTH FPELKCEKSD AYFVLRDGAS GVFMSAHNFP KSRETRAPKV AELALYRDRL PEKLRYLADA PQHDPEGNDA IVRFSRKEKR QYVTSEKNGK ATKWIVDYLG NQWVERKK //