UniProt functional annotation for O26314

UniProt code: O26314.

Organism: Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
Taxonomy: Archaea; Euryarchaeota; Methanomada group; Methanobacteria; Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
 
Function: Involved in DNA uracil repair (PubMed:17012282, PubMed:19240141, PubMed:20129830). Recognizes DNA uracil residues within double-stranded DNA and initiates DNA-U repair by endonucleotic incision on the 5'-side of the 2'-d-uridine residue, irrespective of the nature of the opposing nucleotide (PubMed:17012282, PubMed:19240141, PubMed:20129830). In addition, acts as an apurinic/apyrimidinic (AP) endonuclease hydrolyzing the DNA phosphodiester backbone immediately at the 5'-side of AP sites, and as a 3'-5' exonuclease (PubMed:15725624, PubMed:17012282). Strongly binds to double-stranded DNA (PubMed:15725624). {ECO:0000269|PubMed:15725624, ECO:0000269|PubMed:17012282, ECO:0000269|PubMed:19240141, ECO:0000269|PubMed:20129830}.
 
Catalytic activity: Reaction=(DNA)-(deoxyribonucleoside 5'-phosphate)-(deoxyribose 5'- phosphate)-(deoxyribonucleoside 5'-phosphate) = (DNA)-3'- (deoxyribonucleoside 5'-phosphate)-(2,3-dehydro-2,3-deoxyribose 5'- phosphate) + H(+) + phospho-5'-(DNA); Xref=Rhea:RHEA:66592, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695, ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000269|PubMed:15725624, ECO:0000269|PubMed:17012282};
Catalytic activity: Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.2; Evidence={ECO:0000269|PubMed:15725624, ECO:0000269|PubMed:17012282};
Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15725624, ECO:0000269|PubMed:17012282}; Note=Can also use Mn(2+), Co(2+) and Ni(2+). {ECO:0000269|PubMed:15725624};
Disruption phenotype: Depletion leads to the loss of DNA-U repair. {ECO:0000269|PubMed:19240141}.
Miscellaneous: The insertion of the side chain of Arg-209 into the DNA helical base stack seems to be crucial for the uridine recognition. {ECO:0000269|PubMed:20434457}.
Similarity: Belongs to the DNA repair enzymes AP/exoA family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.