(data stored in SCRATCH9089 zone)

SWISSPROT: 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   11-DEC-2019, entry version 124.
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}.
DR   EMBL; AE004439; AAK02291.1; -; Genomic_DNA.
DR   RefSeq; WP_010906526.1; NC_002663.1.
DR   SMR; Q9CP53; -.
DR   PRIDE; Q9CP53; -.
DR   EnsemblBacteria; AAK02291; AAK02291; PM0207.
DR   KEGG; pmu:PM0207; -.
DR   PATRIC; fig|272843.6.peg.213; -.
DR   eggNOG; ENOG4108IYH; Bacteria.
DR   eggNOG; COG0550; LUCA.
DR   HOGENOM; HOG000086848; -.
DR   KO; K03169; -.
DR   OMA; TYPRVDT; -.
DR   BioCyc; PMUL272843:G1FZ8-215-MONOMER; -.
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;
DR   PRODOM; Q9CP53.
DR   SWISS-2DPAGE; Q9CP53.
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   METAL           7
FT                   /note="Magnesium 1; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00953"
FT   METAL           103
FT                   /note="Magnesium 1; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00953"
FT   METAL           103
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00953"
FT   METAL           105
FT                   /note="Magnesium 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
//

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