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P46799 (TOP1_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:TM_0258
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length633 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 – 633633DNA topoisomerase 1 HAMAP-Rule MF_00952
PRO_0000145169

Regions

Domain6 – 115110Toprim
Zinc finger559 – 58022C4-type HAMAP-Rule MF_00952
Region164 – 1696Interaction with DNA By similarity

Sites

Active site2881O-(5'-phospho-DNA)-tyrosine intermediate By similarity
Metal binding121Magnesium 1; catalytic By similarity
Metal binding841Magnesium 1; catalytic By similarity
Metal binding841Magnesium 2 By similarity
Metal binding861Magnesium 2 By similarity
Site361Interaction with DNA By similarity
Site1401Interaction with DNA By similarity
Site1411Interaction with DNA By similarity
Site1441Interaction with DNA By similarity
Site1491Interaction with DNA By similarity
Site1561Interaction with DNA By similarity
Site2901Interaction with DNA By similarity
Site4751Interaction with DNA By similarity

Amino acid modifications

Disulfide bond559 ↔ 578 HAMAP-Rule MF_00952
Disulfide bond561 ↔ 580 HAMAP-Rule MF_00952

Secondary structure

...................................................................................... 633
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P46799 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: F7262A044060CFE9

FASTA63372,695
        10         20         30         40         50         60 
MSKKVKKYIV VESPAKAKTI KSILGNEYEV FASMGHIIDL PKSKFGVDLE KDFEPEFAVI 

        70         80         90        100        110        120 
KGKEKVVEKL KDLAKKGELL IASDMDREGE AIAWHIARVT NTLGRKNRIV FSEITPRVIR 

       130        140        150        160        170        180 
EAVKNPREID MKKVRAQLAR RILDRIVGYS LSPVLWRNFK SNLSAGRVQS ATLKLVCDRE 

       190        200        210        220        230        240 
REILRFVPKK YHRITVNFDG LTAEIDVKEK KFFDAETLKE IQSIDELVVE EKKVSVKKFA 

       250        260        270        280        290        300 
PPEPFKTSTL QQEAYSKLGF SVSKTMMIAQ QLYEGVETKD GHIAFITYMR TDSTRVSDYA 

       310        320        330        340        350        360 
KEEARNLITE VFGEEYVGSK RERRKSNAKI QDAHEAIRPT NVFMTPEEAG KYLNSDQKKL 

       370        380        390        400        410        420 
YELIWKRFLA SQMKPSQYEE TRFVLRTKDG KYRFKGTVLK KIFDGYEKVW KTERNTGEFP 

       430        440        450        460        470        480 
FEEGESVKPV VVKIEEQETK PKPRYTEGSL VKEMERLGIG RPSTYASTIK LLLNRGYIKK 

       490        500        510        520        530        540 
IRGYLYPTIV GSVVMDYLEK KYSDVVSVSF TAEMEKDLDE VEQGKKTDKI VLREFYESFS 

       550        560        570        580        590        600 
SVFDRNDRIV VDFPTNQKCS CGKEMRLSFG KYGFYLKCEC GKTRSVKNDE IAVIDDGKIF 

       610        620        630 
LGRKDSESGS PDGRSVEGKG NLSEKRRKGK KGS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing of the gene coding for topoisomerase I from the extremely thermophilic eubacterium, Thermotoga maritima."
Bouthier de la Tour C., Kaltoum H., Portemer C., Confalonieri F., Huber R., Duguet M.
Biochim. Biophys. Acta 1264:279-283(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[3]"Crystal structure of full length topoisomerase I from Thermotoga maritima."
Hansen G., Harrenga A., Wieland B., Schomburg D., Reinemer P.
J. Mol. Biol. 358:1328-1340(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 3-633.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U27841 Genomic DNA. Translation: AAA68949.1.
AE000512 Genomic DNA. Translation: AAD35346.1.
PIRS62737.
RefSeqNP_228071.1. NC_000853.1.
YP_007976607.1. NC_021214.1.
YP_008990768.1. NC_023151.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GAIX-ray1.70A/B3-633[»]
2GAJX-ray1.95A/B3-633[»]
ProteinModelPortalP46799.
SMRP46799. Positions 7-601.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243274.TM0258.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD35346; AAD35346; TM_0258.
GeneID897168.
KEGGtma:TM0258.
tmi:THEMA_03435.
tmm:Tmari_0256.
PATRIC23935393. VBITheMar51294_0262.

Phylogenomic databases

eggNOGCOG0551.
KOK03168.
OMAWINKAKK.
OrthoDBEOG6S7XQ9.

Family and domain databases

Gene3D1.10.460.10. 2 hits.
2.70.20.10. 2 hits.
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.
IPR013825. Topo_IA_cen_sub2.
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...

Other

EvolutionaryTraceP46799.

Entry information

Entry nameTOP1_THEMA
AccessionPrimary (citable) accession number: P46799
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 118 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references