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Q9CP53 (TOP3_PASMU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 84. 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 3

EC=5.99.1.2
Alternative name(s):
DNA topoisomerase III
Gene names
Name:topB
Ordered Locus Names:PM0207
OrganismPasteurella multocida (strain Pm70) [Complete proteome] [HAMAP]
Taxonomic identifier272843 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella

Protein attributes

Sequence length650 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_00953

Catalytic activity

ATP-independent breakage of single-stranded DNA, followed by passage and rejoining. HAMAP-Rule MF_00953

Cofactor

Magnesium. Binds two Mg2+ per subunit By similarity. HAMAP-Rule MF_00953

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 – 650650DNA topoisomerase 3 HAMAP-Rule MF_00953
PRO_0000145188

Regions

Domain1 – 134134Toprim
Region194 – 1996Interaction with DNA By similarity

Sites

Active site3421O-(5'-phospho-DNA)-tyrosine intermediate By similarity
Metal binding71Magnesium 1; catalytic By similarity
Metal binding1031Magnesium 1; catalytic By similarity
Metal binding1031Magnesium 2 By similarity
Metal binding1051Magnesium 2 By similarity
Site611Interaction with DNA By similarity
Site1701Interaction with DNA By similarity
Site1781Interaction with DNA By similarity
Site1851Interaction with DNA By similarity
Site3441Interaction with DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CP53 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: AE779A388CC7D166

FASTA65074,196
        10         20         30         40         50         60 
MRLFIAEKPS LARAIADVLP KPHQRGDGFI KCGADDYVTW CIGHLLEQAE PDAYDPKFKQ 

        70         80         90        100        110        120 
WRLEHLPIIP EKWQLIPRKD VHKQLTIVEK LIHQADILIN AGDPDREGQL LVDEVFSYAN 

       130        140        150        160        170        180 
LSVDKLNQIQ RCLISDLNPS AVEKAVNKLQ SNRNFIPLAT SALARARADW LYGINMTRAY 

       190        200        210        220        230        240 
TLRGRQAGYQ GVLSVGRVQT PVLGLIVRRD LEIENFKPQD FFEVLAHIQA ETPEKITALS 

       250        260        270        280        290        300 
AQEKANIPQF KALWQPSKAC EDYQDEEGRV LSLGLVENVV KRIAQQPAEV VEYVDKREHE 

       310        320        330        340        350        360 
SAPLPYSLSA LQIDAAKRYG LSAQEVLDIC QRLYETHRLI TYPRSDCRYL PEEHFGERTK 

       370        380        390        400        410        420 
VFQAISRHIS DYQPLPDILN PEQKNRCWND KKVEAHHAII PTAKNTPVNL NQREWQIYHL 

       430        440        450        460        470        480 
IARQYLMQFC PDAEYRKSKI TLNIAGGTFI AQARNLQVAG WKQLLGKEDS DEQQEPLLPV 

       490        500        510        520        530        540 
VKKGQILFCE KGEIVSKKTQ PPKPFTDATL LSAMTGIARF VQDKELKKIL RETDGLGTEA 

       550        560        570        580        590        600 
TRAGIIELLF KRGFLYKKGR NIHSTETGRI LIQALPDVAT QPDMTAHWES QLTSISQKEM 

       610        620        630        640        650 
SYQQFMSTLT NFLPELMRYV NFAALRQLSQ VEKPQSFSKK MSAKSKKRPT 

« Hide

References

[1]"Complete genomic sequence of Pasteurella multocida Pm70."
May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pm70.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004439 Genomic DNA. Translation: AAK02291.1.
RefSeqNP_245144.1. NC_002663.1.

3D structure databases

ProteinModelPortalQ9CP53.
SMRQ9CP53. Positions 1-617.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272843.PM0207.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK02291; AAK02291; PM0207.
GeneID1243554.
KEGGpmu:PM0207.
PATRIC22869560. VBIPasMul88067_0213.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0550.
HOGENOMHOG000086848.
KOK03169.
OMAFCPDAEY.
OrthoDBEOG60CWM6.

Enzyme and pathway databases

BioCycPMUL272843:GC8W-210-MONOMER.

Family and domain databases

Gene3D1.10.460.10. 2 hits.
2.70.20.10. 2 hits.
3.40.50.140. 1 hit.
HAMAPMF_00953. Topoisom_3_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.
IPR005738. TopoIII.
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.
TIGRFAMsTIGR01056. topB. 1 hit.
PROSITEPS00396. TOPOISOMERASE_I_PROK. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTOP3_PASMU
AccessionPrimary (citable) accession number: Q9CP53
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 84 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