A0A9C7BJ48 · A0A9C7BJ48_9THEO

Function

function

Repair polymerase that plays a key role in base-excision repair. During this process, the damaged base is excised by specific DNA glycosylases, the DNA backbone is nicked at the abasic site by an apurinic/apyrimidic (AP) endonuclease, and POLB removes 5'-deoxyribose-phosphate from the preincised AP site acting as a 5'-deoxyribose-phosphate lyase (5'-dRP lyase); through its DNA polymerase activity, it adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. It is also able to cleave sugar-phosphate bonds 3' to an intact AP site, acting as an AP lyase.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular FunctionDNA binding
Molecular FunctionDNA-directed DNA polymerase activity
Molecular Functionexonuclease activity
Molecular Functionphosphoric ester hydrolase activity
Molecular Functionzinc ion binding
Biological Processbacterial-type flagellum-dependent swarming motility
Biological ProcessDNA repair

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    DNA polymerase beta
  • EC number
  • Alternative names
    • 5'-deoxyribose-phosphate lyase
    • AP lyase

Gene names

    • ORF names
      kuro4_20440

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Kuro-4
  • Taxonomic lineage
    Bacteria > Bacillota > Clostridia > Thermoanaerobacterales > Thermoanaerobacteraceae > Gelria

Accessions

  • Primary accession
    A0A9C7BJ48

Proteomes

Subcellular Location

PTM/Processing

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-315DNA-directed DNA polymerase X
Domain51-70Helix-hairpin-helix DNA-binding motif class 1
Domain91-110Helix-hairpin-helix DNA-binding motif class 1
Domain126-145Helix-hairpin-helix DNA-binding motif class 1
Domain339-418Polymerase/histidinol phosphatase N-terminal

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    580
  • Mass (Da)
    63,183
  • Last updated
    2023-05-03 v1
  • Checksum
    4A80CF3CBBB6F007
MNNLEISWVFLEIADLLEIQGESPFKVRAYRQAAHVLAELEEDVAHYARVGRLTELPGIGAALAAKIEELLKTGSLGYLERLRREVPAGLRAMLALPGVGPRTVRTVFTHLGVSNLDELEAAARAKKLRALPGLGVKTESAIQKGIELLRSRPRGLPLGLAYPAGAELQEILAQLHPVERVSLAGEVRRREELVEELVFVAAVAGRGRAEVHRTFQAAPYVRETLAEDAESVRVVLGLGLEARLITVPPAEFPTQVCYHTGPPAHWTALTERAAARGLELTPAVLKGPAGPVALATERELYAALGLQYVVPELRAGGEEVRAAARGRLPELIKLEDVRGDLHLHSNWSDGAENIAGLAQAAAGCGYAYIAVTDHSQSLSIAHGLSPERLKEQEKEIAAVRARFPELTILSGIEVDILADGRLDLPDEVLTARDIVVASVHSGFKQDRDSMTRRILTALAHPHVDVLAHPSGRLLGRRDPYAVDLEQVLSAAQRYGKILEINASPERLDLSAGWARRAKELGVKLVISTDAHDARRLADMEYGVSVARRAGLTQDDVVNTWPLARLQHYIRLRRDLDGEDT

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP024619
EMBL· GenBank· DDBJ
BCV25271.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp