ID A0A3B0CDM4_9FLAO Unreviewed; 826 AA.
AC A0A3B0CDM4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=DNA topoisomerase 1 {ECO:0000256|HAMAP-Rule:MF_00952};
DE EC=5.6.2.1 {ECO:0000256|HAMAP-Rule:MF_00952};
DE AltName: Full=DNA topoisomerase I {ECO:0000256|HAMAP-Rule:MF_00952};
GN Name=topA {ECO:0000256|HAMAP-Rule:MF_00952,
GN ECO:0000313|EMBL:RKN83400.1};
GN ORFNames=D7Z94_06145 {ECO:0000313|EMBL:RKN83400.1};
OS Ulvibacterium marinum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Ulvibacterium.
OX NCBI_TaxID=2419782 {ECO:0000313|EMBL:RKN83400.1, ECO:0000313|Proteomes:UP000276603};
RN [1] {ECO:0000313|EMBL:RKN83400.1, ECO:0000313|Proteomes:UP000276603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMM003 {ECO:0000313|EMBL:RKN83400.1,
RC ECO:0000313|Proteomes:UP000276603};
RA Zhang Z.;
RT "Ulvibacterium marinum gen. nov., sp. nov., a novel marine bacterium of the
RT family Flavobacteriaceae, isolated from a culture of the green alga Ulva
RT prolifera.";
RL Submitted (OCT-2018) 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_00952}.
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_00952};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00952}.
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00009446, ECO:0000256|HAMAP-Rule:MF_00952}.
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:RKN83400.1}.
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DR EMBL; RBCJ01000001; RKN83400.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B0CDM4; -.
DR OrthoDB; 9804262at2; -.
DR Proteomes; UP000276603; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR CDD; cd00186; TOP1Ac; 1.
DR CDD; cd03363; TOPRIM_TopoIA_TopoI; 1.
DR Gene3D; 3.40.50.140; -; 1.
DR Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 2.
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_00952; Topoisom_1_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; IPR005733; TopoI_bac-type.
DR InterPro; IPR028612; Topoisom_1_IA.
DR InterPro; IPR025589; Toprim_C_rpt.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034149; TOPRIM_TopoI.
DR NCBIfam; TIGR01051; topA_bact; 1.
DR PANTHER; PTHR42785; DNA TOPOISOMERASE, TYPE IA, CORE; 1.
DR PANTHER; PTHR42785:SF1; OMEGA-PROTEIN; 1.
DR Pfam; PF01131; Topoisom_bac; 2.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF13368; Toprim_C_rpt; 3.
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_00952};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00952};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000276603};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00952}.
FT DOMAIN 3..113
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 163..168
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT ACT_SITE 284
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 33
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 139
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 140
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 143
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 148
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 155
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 286
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 475
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
SQ SEQUENCE 826 AA; 93306 MW; 8B13CFE373F19D48 CRC64;
MAKNLVIVES PAKAKTIEKF LGKDYKVESS FGHIADLPSK ELGVDVDNNF EPKYIVDKEK
KALVKKLKDL AKKADTIWLA SDEDREGEAI SWHLTETLDL DKKKTKRIVF NSITKSAIQK
AIENPRDINY NLVNAQQARR VLDRLVGYQL SPVLWKKIKP GLSAGRVQSV AVRLIVERER
DIEVFKPEAS FKISAEFKTA DGGVFMAKLN KTFASKDEAG AFLKKNLGAI FSVGNLDKKP
AKKSPSAPFT TSTLQQEASR KLYFSVGRTM QVAQRLYEAG LITYMRTDSV NLSGEAIAMA
KEAIIENYGN EYSSVRNFKG KSKGAQEAHE AIRPTNITNQ SPSLERDQSK LYELIWKRTI
ASQMSDAQLE RTNVKIKSNT HGEEFTANGE VIKFDGFLKV YMEGIDDEDR AEEQEGMLPA
MKEGDVLDNT YISATERFTR PPYRFTEASL VKKLEELGIG RPSTYAPTIS TIQNRGYVEK
GTIEGTERNY VQLVLDSGKI QEKKLAETVG SDKGKLVPTD IGMIVNDFLV SHFANILDYN
FTAKVEENFD EIAEGEEDWQ KIMQDFYKDF RPNVEHVEEN ADRASGERVL GTDPDTGRQV
AVRLGRFGPM VQIGTVEEEE KPLFASLLPD QSLNTITYEE AMELFQLPRK LGAYKGEDIE
ASVGRYGPYV RFGKKFVSLE KGESAFDVDL ERAIELIKEK EKADAPIATY EGKEVTKGKG
RFGPFIKWDG IFINVNKKYD FENLSQENIE ELIEVKKQKE IDKLIQEWPE EGIRIEKARW
GRHNIIKGRT KVELAKTVDV SKIKLEEAKE LLAKKAPKKR SKAKKK
//