TOP1_ZYMMO
ID TOP1_ZYMMO Reviewed; 1212 AA.
AC Q9X3X7; Q5NN93;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=DNA topoisomerase 1 {ECO:0000255|HAMAP-Rule:MF_00952};
DE EC=5.6.2.1 {ECO:0000255|HAMAP-Rule:MF_00952};
DE AltName: Full=DNA topoisomerase I {ECO:0000255|HAMAP-Rule:MF_00952};
DE AltName: Full=Omega-protein;
DE AltName: Full=Relaxing enzyme;
DE AltName: Full=Swivelase;
DE AltName: Full=Untwisting enzyme;
GN Name=topA {ECO:0000255|HAMAP-Rule:MF_00952}; OrderedLocusNames=ZMO1193;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RA Lee H.J., Kang H.S.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
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_00952}.
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_00952};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00952};
CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP-Rule:MF_00952};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00952}.
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00952}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD21553.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF088896; AAD21553.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE008692; AAV89817.2; -; Genomic_DNA.
DR RefSeq; WP_011241016.1; NZ_CP035711.1.
DR AlphaFoldDB; Q9X3X7; -.
DR SMR; Q9X3X7; -.
DR STRING; 264203.ZMO1193; -.
DR EnsemblBacteria; AAV89817; AAV89817; ZMO1193.
DR GeneID; 58026966; -.
DR KEGG; zmo:ZMO1193; -.
DR eggNOG; COG0550; Bacteria.
DR eggNOG; COG1754; Bacteria.
DR HOGENOM; CLU_002929_0_2_5; -.
DR OMA; PECKYTR; -.
DR OrthoDB; 223233at2; -.
DR Proteomes; UP000001173; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
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; 1.10.290.10; -; 1.
DR Gene3D; 1.10.460.10; -; 1.
DR Gene3D; 2.70.20.10; -; 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; IPR013498; Topo_IA_Znf.
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 PANTHER; PTHR42785; PTHR42785; 3.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF13368; Toprim_C_rpt; 3.
DR Pfam; PF01396; zf-C4_Topoisom; 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; TIGR01051; topA_bact; 1.
DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW DNA-binding; Isomerase; Magnesium; Metal-binding; Reference proteome;
KW Topoisomerase; Zinc; Zinc-finger.
FT CHAIN 1..1212
FT /note="DNA topoisomerase 1"
FT /id="PRO_0000145175"
FT DOMAIN 1..114
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT ZN_FING 592..619
FT /note="C4-type"
FT REGION 164..169
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT REGION 687..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..818
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..842
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..872
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..937
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1135
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1186..1200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 293
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT BINDING 80
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT BINDING 80
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT BINDING 82
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT SITE 31
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT SITE 140
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT SITE 141
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT SITE 144
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT SITE 156
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT SITE 295
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT SITE 488
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT CONFLICT 171..172
FT /note="VA -> AR (in Ref. 1; AAD21553)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="V -> F (in Ref. 1; AAD21553)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="V -> F (in Ref. 1; AAD21553)"
FT /evidence="ECO:0000305"
FT CONFLICT 1017
FT /note="S -> F (in Ref. 1; AAD21553)"
FT /evidence="ECO:0000305"
FT CONFLICT 1174
FT /note="K -> I (in Ref. 1; AAD21553)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1212 AA; 130689 MW; 498231607911400F CRC64;
MKLVVVESPA KAKTIEKYLG SGYQVLASYG HIRDLPSKDG SVNPDNGFSM VWQNYPDKAH
RLKAIEDAVK ESDSLILATD PDREGEAISW HILELLKTKK LLPDDVERVT FNAITKAAVT
DAMAHPRQLD NDLINAYLAR RALDYLVGFT LSPILWRKLP GAKSAGRVQS VALRLVVDRE
QEIEGFKPQE YWSVEADMEA DSIGFTSRLI QWRGQKLEKL SIADKTQAEA AQSDVESGHF
TVSNVETKPV SRNPQPPFTT STLQQEAARK LGFAASHTMR LAQSLYEEGL ITYMRTDGVQ
MDESAIAAAR KTITQRYDGG YVPDKPRQYQ VKAKNAQEAH EAIRPTDFSR DKAASGDHAR
LYELIWKRAL ASQMASAKLE RTTVDLTDGT GQNVLRVTGQ VVLFSGFLTL YEESADDNAN
DRDGKEGRAR LPLLRAGDAP LKKEVRADQH FTQPPPRYSE ASLVKKMEDL GIGRPSTYAS
VIQVLKDRAY VTLERNRFIP SEAGRLLTAF LERFFERYVS YDFTAGLEDS LDEISGGRAD
WQKVLDAFWH DFKPKTAEVM EQQPSAITAE LDKFLEPWLF PDKGDGHDPR ECPSCHTGRL
ALKGGRFGAF IACSNYPECK YTRGFGQGED GVDDNEPVLL GYMPENSDDD GYMAFSDQGD
ILPANTASAS ETGVTDGGIA ANAAFSGKGN SASHTDRDDL PFDPDEPASS TGNVASSQSR
MTGDETASSG NSRDSSAHGV STTAGIDAES QAGISNQALA GKNNAGRTAV SDNKGNNSSS
TIAAARKGGS TDDNATVSDP DGDIGSGASS SGQDADNRLL SHRNGDIDSR AIPADHKDSS
SDQNASHALS PDRNSDDASV SNSDKKIDSK AVSTGHDVGN AITSDNSPSD NVAHLASTPS
SATSSVKVAL ETENNDTAAS KADEQAKEEE ESRKARAVTR RTGRFGPYIQ LGEGKNAKRV
SVPRDVNPRE VDFSLASRLL ALPREIGLHP ESGKMIIAGT GRYGPYLNCD GKYARLSSTE
ELLDIDIDRA VVKLAEAAQN KGRTGATLSR EPLKVFGDSP VTEKPVQLMN GRYGPYVTDG
ETNASLPKDT TPESLTFEEA LALLEARAKM PKKKKTKKAA AKKPAAKKTT TKKAAPKKAT
TKTATPKSAT TDNATSEDGD ATPAKSPAKK AVAKKTTAKK PASKSATKKA PSSKTTAAKK
TSKATPKDEV AE
