TOP3_PASMU
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 03-AUG-2022, entry version 130.
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; Proteobacteria; 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;
CC Evidence={ECO:0000255|HAMAP-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}.
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DR EMBL; AE004439; AAK02291.1; -; Genomic_DNA.
DR RefSeq; WP_010906526.1; NC_002663.1.
DR AlphaFoldDB; Q9CP53; -.
DR SMR; Q9CP53; -.
DR STRING; 747.DR93_1859; -.
DR PRIDE; Q9CP53; -.
DR EnsemblBacteria; AAK02291; AAK02291; PM0207.
DR KEGG; pmu:PM0207; -.
DR PATRIC; fig|272843.6.peg.213; -.
DR HOGENOM; CLU_002929_5_2_6; -.
DR OMA; TYPRVDT; -.
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; 1.10.290.10; -; 1.
DR Gene3D; 1.10.460.10; -; 1.
DR Gene3D; 2.70.20.10; -; 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 PANTHER; PTHR11390; PTHR11390; 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; SSF56712; 1.
DR TIGRFAMs; TIGR01056; topB; 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..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 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|HAMAP-Rule:MF_00953"
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
