ID A0A1Q9K1T8_9FIRM Unreviewed; 697 AA.
AC A0A1Q9K1T8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=BHF69_07305 {ECO:0000313|EMBL:OLR62505.1};
OS Anaerostipes sp. 992a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerostipes.
OX NCBI_TaxID=1261637 {ECO:0000313|EMBL:OLR62505.1, ECO:0000313|Proteomes:UP000187371};
RN [1] {ECO:0000313|EMBL:OLR62505.1, ECO:0000313|Proteomes:UP000187371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=992a {ECO:0000313|EMBL:OLR62505.1,
RC ECO:0000313|Proteomes:UP000187371};
RX PubMed=27613689;
RA Trachsel J., Bayles D.O., Looft T., Levine U.Y., Allen H.K.;
RT "Function and Phylogeny of Bacterial Butyryl Coenzyme A:Acetate
RT Transferases and Their Diversity in the Proximal Colon of Swine.";
RL Appl. Environ. Microbiol. 82:6788-6798(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLR62505.1}.
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DR EMBL; MJIG01000004; OLR62505.1; -; Genomic_DNA.
DR RefSeq; WP_075670398.1; NZ_MJIG01000004.1.
DR AlphaFoldDB; A0A1Q9K1T8; -.
DR STRING; 1261637.BHF69_07305; -.
DR OrthoDB; 9803554at2; -.
DR Proteomes; UP000187371; 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:UP000187371};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00953}.
FT DOMAIN 2..135
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 186..191
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT ACT_SITE 308
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT BINDING 104
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT SITE 60
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT SITE 167
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT SITE 175
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT SITE 310
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
SQ SEQUENCE 697 AA; 79624 MW; 7C414F89BD3356EE CRC64;
MKQLVLAEKP SVGRDIARVL HCKKAVNGGL EGEKYIVTWA LGHLVELKDP EGYDKKYQTW
RMEDLPMMPE KMQVQVIKKT AKQYKAVTAL MNRKDVGTII IATDAGREGE LVARLILLKS
HNKKPIKRLW ISSVTDKAIK EGFSRLKDGR EYQHLYEAAM SRAEADWLVG MNATRALTCK
HNAQLSCGRV QTPTLSLIAQ REEEIRNFQP KAYYGLEARG AGLTFTWRDE KNNTRTFVKE
KCKDVEKKVS GEMLTVDNVV VKQKKSYAPA LYDLNELQRD ASQRFHFSPK ETLNIMQRLY
EHHKILTYPR TDSRYLTDDI VPTIPERLRS CGIGPYRKAA AGILKNKIKA NGHFVNNKKV
SDHHAIIPTE QFVNLSELSS EERKIYDLVV RRFLAVLMPP YEYEEMTIEG NMSGERFVSK
GSRMLKAGWK AAYEEEEELA DVSEVKKGQK LIVVVKETEG KTKPPAYYTE ATLLTAMEQR
GLGTVATRAD IIDKLFRTFL LEKKEEGIRT TSKAKQLLAL VPEELKQPEL TADWEKKLSR
ISDGKLKRQV FMSEIKDYTV EIVDEIKGSQ GKFHHDNMSN KKCPNCGKRL LKVNGKKSRM
LVCQDRECGY RETVCVISNA RCPVCHKKME LWGKGEDASF ICSCGHKEKM SKFKERREKE
GAGVSKRDVA RYMKKQAKEA KEPINNAFAD ALKNIKL
//
