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O51768 (TOP1_BORBU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA topoisomerase 1

EC=5.99.1.2
Alternative name(s):
DNA topoisomerase I
Omega-protein
Relaxing enzyme
Swivelase
Untwisting enzyme
Gene names
Name:topA
Ordered Locus Names:BB_0828
OrganismBorrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680) [Reference proteome] [HAMAP]
Taxonomic identifier224326 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorreliaBorrelia burgdorferi group

Protein attributes

Sequence length848 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone By similarity. HAMAP-Rule MF_00952

Catalytic activity

ATP-independent breakage of single-stranded DNA, followed by passage and rejoining. HAMAP-Rule MF_00952

Cofactor

Magnesium. Binds two Mg2+ per subunit By similarity. HAMAP-Rule MF_00952

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00952

Sequence similarities

Belongs to the type IA topoisomerase family.

Contains 1 Toprim domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 848848DNA topoisomerase 1 HAMAP-Rule MF_00952
PRO_0000145143

Regions

Domain4 – 128125Toprim
Region176 – 1816Interaction with DNA By similarity

Sites

Active site3241O-(5'-phospho-DNA)-tyrosine intermediate By similarity
Metal binding101Magnesium 1; catalytic By similarity
Metal binding971Magnesium 1; catalytic By similarity
Metal binding971Magnesium 2 By similarity
Metal binding991Magnesium 2 By similarity
Site341Interaction with DNA By similarity
Site1521Interaction with DNA By similarity
Site1531Interaction with DNA By similarity
Site1561Interaction with DNA By similarity
Site1611Interaction with DNA By similarity
Site1681Interaction with DNA By similarity
Site3261Interaction with DNA By similarity
Site5111Interaction with DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
O51768 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 37DEA5FB1E12FA2C

FASTA84897,663
        10         20         30         40         50         60 
MQNKKLIIVE SPTKAKTIKK FLDESFLVEA CIGHVVDLPN NAKEIPKEYK KYEWANISID 

        70         80         90        100        110        120 
YNNGFNPIYI IPSNKKPIVS KLKKLVKTIN EIYLATDQDR EGETIAFHLK EVLKIKNYKR 

       130        140        150        160        170        180 
MIFHEITETA ITESLKNTRN IDMNLVNAGE ARRILDRLYG YTISPLLWKK VAYGLSAGRV 

       190        200        210        220        230        240 
QSVGLKLLIE KEKTRINFKK ANYYSILLQC KHEKKNLLLE AKLEEIDGKN IAEGKDFVNE 

       250        260        270        280        290        300 
TGKLKNIAKT TIITQDLMIE LEKELKNGQK IELISIETKK IKIPPPKPFT TSTLQQEINK 

       310        320        330        340        350        360 
RLKIGTKQIM QHAQKLYEHG YITYMRTDSH NIAKIAKDKI TKIIKNKYGK EYIEEKDRIY 

       370        380        390        400        410        420 
EKEKMAQNAH EAIRPSEIFI PNETIEIESK TAKEIYKIIW DRTIISGMKD AIKENIKLTF 

       430        440        450        460        470        480 
KYKNLIFRSS FTKIIFDGFL KHTKEQDEHL NINFDLIKKG DTFSIVKMKT SEHETKAPFR 

       490        500        510        520        530        540 
YTEASLVQKM EKEGIGRPST YSTIISTLLE REYAFKLNNT LMPTIKGAAV INLLEKYFPV 

       550        560        570        580        590        600 
LIELNFTSNM EEKLDKIAIG KLDKIKYLSK FYNGKKGLKD TVMQLEPKID SSEFRTVIES 

       610        620        630        640        650        660 
QKIENKNSIN YTINIGKYGP YLIFKGHNYS INAKTPLENL YKKDEIEKII NEKELKPNIL 

       670        680        690        700        710        720 
GVDPLTGLNV IFKNTIYGNI VQLGEDTHAP QEYTKKGKPK KLKIIKAKKA STKKIDPENI 

       730        740        750        760        770        780 
TLELALKLLS LPKPIGKHPQ TNEQIIAATG VFGDYIKTES GSIACSLKKD LKAYDITLDK 

       790        800        810        820        830        840 
AISLLNERAN KVGIIVKTIT FSKNKIGNKI YIYKKNDKFY AKIKRKKIDL PDNINLEEIN 


EKYVFSLL 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000783 Genomic DNA. Translation: AAC67161.1.
PIRC70203.
RefSeqNP_212962.1. NC_001318.1.

3D structure databases

ProteinModelPortalO51768.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224326.BB0828.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC67161; AAC67161; BB_0828.
GeneID1195686.
KEGGbbu:BB_0828.
PATRIC20558321. VBIBorBur75917_1220.

Phylogenomic databases

eggNOGCOG1754.
KOK03168.
OMATIMDRGY.
OrthoDBEOG6S7XQ9.
ProtClustDBCLSK507867.

Enzyme and pathway databases

BioCycBBUR224326:G9SO-837-MONOMER.

Family and domain databases

Gene3D1.10.290.10. 1 hit.
1.10.460.10. 1 hit.
3.40.50.140. 1 hit.
HAMAPMF_00952. Topoisom_1_prok.
InterProIPR000380. Topo_IA.
IPR003601. Topo_IA_2.
IPR023406. Topo_IA_AS.
IPR013497. Topo_IA_cen.
IPR013824. Topo_IA_cen_sub1.
IPR013826. Topo_IA_cen_sub3.
IPR023405. Topo_IA_core_domain.
IPR003602. Topo_IA_DNA-bd.
IPR005733. TopoI_bac-type.
IPR028612. Topoisom_1_IA.
IPR006171. Toprim_domain.
[Graphical view]
PANTHERPTHR11390. PTHR11390. 1 hit.
PfamPF01131. Topoisom_bac. 1 hit.
PF01751. Toprim. 1 hit.
[Graphical view]
PRINTSPR00417. PRTPISMRASEI.
SMARTSM00437. TOP1Ac. 1 hit.
SM00436. TOP1Bc. 1 hit.
SM00493. TOPRIM. 1 hit.
[Graphical view]
SUPFAMSSF56712. SSF56712. 1 hit.
TIGRFAMsTIGR01051. topA_bact. 1 hit.
PROSITEPS00396. TOPOISOMERASE_I_PROK. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTOP1_BORBU
AccessionPrimary (citable) accession number: O51768
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: February 19, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families