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Database: UniProt
Entry: A0A343JAM5_9CLOT
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Original site: A0A343JAM5_9CLOT 
ID   A0A343JAM5_9CLOT        Unreviewed;       728 AA.
AC   A0A343JAM5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=DNA topoisomerase 3 {ECO:0000256|HAMAP-Rule:MF_00953};
DE            EC=5.6.2.1 {ECO:0000256|HAMAP-Rule:MF_00953};
DE   AltName: Full=DNA topoisomerase III {ECO:0000256|HAMAP-Rule:MF_00953};
GN   Name=topB {ECO:0000256|HAMAP-Rule:MF_00953};
GN   ORFNames=BEN51_03555 {ECO:0000313|EMBL:ASW42583.1};
OS   Clostridium isatidis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=182773 {ECO:0000313|EMBL:ASW42583.1, ECO:0000313|Proteomes:UP000264883};
RN   [1] {ECO:0000313|EMBL:ASW42583.1, ECO:0000313|Proteomes:UP000264883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15098 {ECO:0000313|EMBL:ASW42583.1,
RC   ECO:0000313|Proteomes:UP000264883};
RA   Little G.T., Minton N.P.;
RT   "Complete Genome Sequence Of The Indigo Reducing Clostridium isatidis
RT   DSM15098.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000213, ECO:0000256|HAMAP-
CC         Rule:MF_00953};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00953};
CC   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000256|ARBA:ARBA00009446, ECO:0000256|HAMAP-Rule:MF_00953}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00953}.
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DR   EMBL; CP016786; ASW42583.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A343JAM5; -.
DR   KEGG; cia:BEN51_03555; -.
DR   OrthoDB; 9803554at2; -.
DR   Proteomes; UP000264883; 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; TOPOISOMERASE_I_PROK; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00953};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00953};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00953};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00953};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264883};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW   Rule:MF_00953}.
FT   DOMAIN          3..138
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          188..193
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT   ACT_SITE        310
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT   BINDING         105
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT   SITE            61
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT   SITE            169
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT   SITE            177
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT   SITE            312
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
SQ   SEQUENCE   728 AA;  82989 MW;  BF303BAA443F6AE8 CRC64;
     MGKSLVLAEK PSVGRDLAKV LKCNQNKRTY IEGNKYIVTW ALGHLVGLQD PEAYDDKYKS
     WSMETLPMLP KNMKLTVLKK TSKQFYEVKK LLNRNDVDEI IIATDAGREG ELVARWIIEK
     AGVKKKPIKR LWISSQTNKA ILEGFKKLKD GREYNNLYKA AVCRAEADWI VGLNATRALT
     CKYNAQLSAG RVQSPTLAMI VDREEEIKNF KPEDYYTLNV KGNNFTLNWV NNKGNSSIFN
     KEFADSLAAK VKGHDGEVVD ITKSNKKKYS PALYDLTELQ RDANKFWGYS AKQTLNIMQR
     LYENHKLLTY PRTDSRYISS DIVPTIPERL KAIGIGEYRI YAEKLLKEGV KANKNFVDNS
     KVSDHHAIIP TEERGNTANL SSEERHIYDL VVKRFLSVML PPYEYEQTNL KVLVNGETFT
     AKGNITKNKG WKKLYEKDNL NEVENSQELP TLNKGDKIKI LQVNLVKKQT TPPARFDEAT
     LLSAMENPNK YIAVSKDAAK TLNETGGLGT VATRADIIEK LFNSFVIEKR GKEIVPTSKG
     KQLIELVPAE LKSPLLTAKW ENKLDKISKG KEDPSTFIKE MRNYAIALVE AIKQENSKFI
     HDNQTGRKCP NCSKYLLEVK GKNSRMLVCQ DRECGYKENL ARFTNVRCPE CKKKLELRGE
     GEAKIYVCVG ATCNFREKAS QFEKRFDKND KVNKKEVNKI IRKIKKEAEE FNNNPFASLL
     GNLNLEDK
//
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