ID TOP3_PASMU Reviewed; 650 AA. AC Q9CP53; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 138. DE RecName: Full=DNA topoisomerase 3 {ECO:0000255|HAMAP-Rule:MF_00953}; DE EC=5.6.2.1 {ECO:0000255|HAMAP-Rule:MF_00953}; DE AltName: Full=DNA topoisomerase III {ECO:0000255|HAMAP-Rule:MF_00953}; GN Name=topB {ECO:0000255|HAMAP-Rule:MF_00953}; OrderedLocusNames=PM0207; 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_00953}. 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_00953}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00953}; CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP-Rule:MF_00953}; CC -!- SIMILARITY: Belongs to the type IA topoisomerase family. CC {ECO:0000255|HAMAP-Rule:MF_00953, ECO:0000255|PROSITE- CC ProRule:PRU01383}. 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; AAK02291.1; -; Genomic_DNA. DR RefSeq; WP_010906526.1; NC_002663.1. DR AlphaFoldDB; Q9CP53; -. DR SMR; Q9CP53; -. DR STRING; 272843.PM0207; -. DR EnsemblBacteria; AAK02291; AAK02291; PM0207. DR KEGG; pmu:PM0207; -. DR PATRIC; fig|272843.6.peg.213; -. DR HOGENOM; CLU_002929_5_2_6; -. DR OrthoDB; 9803554at2; -. DR Proteomes; UP000000809; 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule. DR CDD; cd00186; TOP1Ac; 1. DR CDD; cd03362; TOPRIM_TopoIA_TopoIII; 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_00953; Topoisom_3_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; IPR005738; TopoIII. DR InterPro; IPR006171; TOPRIM_domain. DR InterPro; IPR034144; TOPRIM_TopoIII. DR NCBIfam; TIGR01056; topB; 1. DR PANTHER; PTHR11390:SF21; DNA TOPOISOMERASE 3-ALPHA; 1. DR PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1. DR Pfam; PF01131; Topoisom_bac; 1. DR Pfam; PF01751; Toprim; 1. 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 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 Topoisomerase. FT CHAIN 1..650 FT /note="DNA topoisomerase 3" FT /id="PRO_0000145188" FT DOMAIN 1..134 FT /note="Toprim" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" FT DOMAIN 155..617 FT /note="Topo IA-type catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01383" FT REGION 194..199 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" FT ACT_SITE 342 FT /note="O-(5'-phospho-DNA)-tyrosine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01383" FT BINDING 7 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_00953" FT BINDING 103 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_00953" FT BINDING 103 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" FT BINDING 105 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" FT SITE 61 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" FT SITE 170 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" FT SITE 178 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" FT SITE 185 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" FT SITE 344 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" SQ SEQUENCE 650 AA; 74196 MW; AE779A388CC7D166 CRC64; MRLFIAEKPS LARAIADVLP KPHQRGDGFI KCGADDYVTW CIGHLLEQAE PDAYDPKFKQ WRLEHLPIIP EKWQLIPRKD VHKQLTIVEK LIHQADILIN AGDPDREGQL LVDEVFSYAN LSVDKLNQIQ RCLISDLNPS AVEKAVNKLQ SNRNFIPLAT SALARARADW LYGINMTRAY TLRGRQAGYQ GVLSVGRVQT PVLGLIVRRD LEIENFKPQD FFEVLAHIQA ETPEKITALS AQEKANIPQF KALWQPSKAC EDYQDEEGRV LSLGLVENVV KRIAQQPAEV VEYVDKREHE SAPLPYSLSA LQIDAAKRYG LSAQEVLDIC QRLYETHRLI TYPRSDCRYL PEEHFGERTK VFQAISRHIS DYQPLPDILN PEQKNRCWND KKVEAHHAII PTAKNTPVNL NQREWQIYHL IARQYLMQFC PDAEYRKSKI TLNIAGGTFI AQARNLQVAG WKQLLGKEDS DEQQEPLLPV VKKGQILFCE KGEIVSKKTQ PPKPFTDATL LSAMTGIARF VQDKELKKIL RETDGLGTEA TRAGIIELLF KRGFLYKKGR NIHSTETGRI LIQALPDVAT QPDMTAHWES QLTSISQKEM SYQQFMSTLT NFLPELMRYV NFAALRQLSQ VEKPQSFSKK MSAKSKKRPT //