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   27-MAR-2024, entry version 142.
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};
GN   OrderedLocusNames=ZMO1193;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Pseudomonadota; 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; Evidence={ECO:0000255|HAMAP-
CC         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};
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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   KEGG; zmo:ZMO1193; -.
DR   eggNOG; COG0550; Bacteria.
DR   eggNOG; COG1754; Bacteria.
DR   HOGENOM; CLU_002929_0_2_5; -.
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; 3.40.50.140; -; 1.
DR   Gene3D; 3.30.65.10; Bacterial Topoisomerase I, domain 1; 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_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   NCBIfam; TIGR01051; topA_bact; 1.
DR   PANTHER; PTHR42785:SF1; DNA TOPOISOMERASE; 1.
DR   PANTHER; PTHR42785; DNA TOPOISOMERASE, TYPE IA, CORE; 1.
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; Prokaryotic type I DNA topoisomerase; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR   PROSITE; PS00396; TOPO_IA_1; 1.
DR   PROSITE; PS52039; TOPO_IA_2; 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   DOMAIN          130..556
FT                   /note="Topo IA-type catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01383"
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|PROSITE-ProRule:PRU01383"
FT   BINDING         7
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
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_note="catalytic"
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
//