ID A0A1M5YNC7_9FIRM Unreviewed; 728 AA.
AC A0A1M5YNC7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=SAMN02745180_02321 {ECO:0000313|EMBL:SHI13419.1};
OS Sporanaerobacter acetigenes DSM 13106.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Sporanaerobacteraceae;
OC Sporanaerobacter.
OX NCBI_TaxID=1123281 {ECO:0000313|EMBL:SHI13419.1, ECO:0000313|Proteomes:UP000184389};
RN [1] {ECO:0000313|EMBL:SHI13419.1, ECO:0000313|Proteomes:UP000184389}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13106 {ECO:0000313|EMBL:SHI13419.1,
RC ECO:0000313|Proteomes:UP000184389};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQXR01000013; SHI13419.1; -; Genomic_DNA.
DR RefSeq; WP_072744962.1; NZ_FQXR01000013.1.
DR AlphaFoldDB; A0A1M5YNC7; -.
DR STRING; 1123281.SAMN02745180_02321; -.
DR OrthoDB; 9803554at2; -.
DR Proteomes; UP000184389; Unassembled WGS sequence.
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:UP000184389};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00953}.
FT DOMAIN 3..136
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 187..192
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 168
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT SITE 176
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; 83486 MW; AF415DFD8997A18A CRC64;
MNKILVLAEK PSVGRDIARV LKCNKKGNGY LEGDKYIVTW ALGHLVTLAD PEEYNKSYKS
WRIEDLPILP SHMKLVVIKQ TQKQFYIVKE QMNRKDVSQI VIATDAGREG ELVARWIIEK
ANIRKPIKRL WISSVTDKAI RDGFNKLRDG KEYENLYASA VARAEADWIV GINATRALTC
KYNAQLSCGR VQTPTLFMVA KREEEIKNFK EKEFYGIVAT TKDLKLVWQD NHTKDIRTFD
EKKCDKILAS IEKKDAQVYD VEKTYKKSYS PRLYDLTELQ RDANKIFGYS AKETLSVMQR
LYETHKILTY PRTDSRYLTS DIVDTLGERI KACGIGPYQS MASRILKKPI VANKSFVDDS
KVSDHHAIIP TEERVPLSKL NERERKIYDL VVKRFMAVLY PPFEFEQTTI KAKIGDENFF
AKGKRVLAQG WKEVYANNYE DDDVQEDTPE QLLPNINKGD VLKVNSIIKT KGHTKPPAPF
TEGTLLSAME NPSKYMANES KDLIKIIGET GGIGTVATRA DIIEKLFNNF LIEKRGKDIY
ITGKGKQLLG LVPEDLKSPA LTAEWEQKLE AIAKGKLRKN TFIEEMEIYS KDITNEIKNS
DETFRHDNIS RVKCPQCGKY MLEVKGKKGK MLVCQDRECG YRKNISKVTN ARCPNCHKKL
ELRGEGEGQI FVCSCGYREK LSSFNERRKK EKNSVSKKEV SKYLKEQNKF KNEAINTDLA
DALKKLKF
//
