Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0A621 (TOP1_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 70. 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:Mb3670c
OrganismMycobacterium bovis (strain ATCC BAA-935 / AF2122/97) [Complete proteome] [HAMAP]
Taxonomic identifier233413 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length934 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.

Ontologies

Keywords
   LigandDNA-binding
Magnesium
Metal-binding
   Molecular functionIsomerase
Topoisomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processDNA topological change

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA topoisomerase type I activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 934934DNA topoisomerase 1 HAMAP-Rule MF_00952
PRO_0000145157

Regions

Domain18 – 142125Toprim
Region191 – 1966Interaction with DNA By similarity

Sites

Active site3421O-(5'-phospho-DNA)-tyrosine intermediate By similarity
Metal binding241Magnesium 1; catalytic By similarity
Metal binding1111Magnesium 1; catalytic By similarity
Metal binding1111Magnesium 2 By similarity
Metal binding1131Magnesium 2 By similarity
Site481Interaction with DNA By similarity
Site1671Interaction with DNA By similarity
Site1681Interaction with DNA By similarity
Site1711Interaction with DNA By similarity
Site1761Interaction with DNA By similarity
Site1831Interaction with DNA By similarity
Site3441Interaction with DNA By similarity
Site5471Interaction with DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A621 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: B29E2C17897781BA

FASTA934102,336
        10         20         30         40         50         60 
MADPKTKGRG SGGNGSGRRL VIVESPTKAR KLASYLGSGY IVESSRGHIR DLPRAASDVP 

        70         80         90        100        110        120 
AKYKSQPWAR LGVNVDADFE PLYIISPEKR STVSELRGLL KDVDELYLAT DGDREGEAIA 

       130        140        150        160        170        180 
WHLLETLKPR IPVKRMVFHE ITEPAIRAAA EHPRDLDIDL VDAQETRRIL DRLYGYEVSP 

       190        200        210        220        230        240 
VLWKKVAPKL SAGRVQSVAT RIIVARERDR MAFRSAAYWD ILAKLDASVS DPDAAPPTFS 

       250        260        270        280        290        300 
ARLTAVAGRR VATGRDFDSL GTLRKGDEVI VLDEGSATAL AAGLDGTQLT VASAEEKPYA 

       310        320        330        340        350        360 
RRPYPPFMTS TLQQEASRKL RFSAERTMSI AQRLYENGYI TYMRTDSTTL SESAINAART 

       370        380        390        400        410        420 
QARQLYGDEY VAPAPRQYTR KVKNAQEAHE AIRPAGETFA TPDAVRRELD GPNIDDFRLY 

       430        440        450        460        470        480 
ELIWQRTVAS QMADARGMTL SLRITGMSGH QEVVFSATGR TLTFPGFLKA YVETVDELVG 

       490        500        510        520        530        540 
GEADDAERRL PHLTPGQRLD IVELTPDGHA TNPPARYTEA SLVKALEELG IGRPSTYSSI 

       550        560        570        580        590        600 
IKTIQDRGYV HKKGSALVPS WVAFAVTGLL EQHFGRLVDY DFTAAMEDEL DEIAAGNERR 

       610        620        630        640        650        660 
TNWLNNFYFG GDHGVPDSVA RSGGLKKLVG INLEGIDARE VNSIKLFDDT HGRPIYVRVG 

       670        680        690        700        710        720 
KNGPYLERLV AGDTGEPTPQ RANLSDSITP DELTLQVAEE LFATPQQGRT LGLDPETGHE 

       730        740        750        760        770        780 
IVAREGRFGP YVTEILPEPA ADAAAAAQGV KKRQKAAGPK PRTGSLLRSM DLQTVTLEDA 

       790        800        810        820        830        840 
LRLLSLPRVV GVDPASGEEI TAQNGRYGPY LKRGNDSRSL VTEDQIFTIT LDEALKIYAE 

       850        860        870        880        890        900 
PKRRGRQSAS APPLRELGTD PASGKPMVIK DGRFGPYVTD GETNASLRKG DDVASITDER 

       910        920        930 
AAELLADRRA RGPAKRPARK AARKVPAKKA AKRD 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248333 Genomic DNA. Translation: CDO44941.1.
RefSeqNP_857309.1. NC_002945.3.

3D structure databases

ProteinModelPortalP0A621.
SMRP0A621. Positions 17-608.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING233413.Mb3670c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD95856; CAD95856; Mb3670c.
GeneID1093317.
KEGGmbo:Mb3670c.
PATRIC18009784. VBIMycBov88188_4018.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1754.
HOGENOMHOG000004020.
KOK03168.
OMAFRSAEYW.
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.
IPR025589. Toprim_C_rpt.
IPR006171. Toprim_domain.
[Graphical view]
PANTHERPTHR11390. PTHR11390. 1 hit.
PfamPF01131. Topoisom_bac. 1 hit.
PF01751. Toprim. 1 hit.
PF13368. Toprim_C_rpt. 3 hits.
[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_MYCBO
AccessionPrimary (citable) accession number: P0A621
Secondary accession number(s): O08383, Q59567, X2BPY1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: July 9, 2014
This is version 70 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