CATH Classification

Domain Context

CATH Clusters

Superfamily HIT-like
Functional Family aprataxin isoform X2

Enzyme Information

3.1.12.2
DNA-3'-diphospho-5'-guanosine diphosphatase.
based on mapping to UniProt Q7Z2E3
(DNA)-3'-diphospho-5'-guanosine + H(2)O = (DNA)-3'-phosphate + GMP.
-!- Aprataxin is a DNA-binding protein that catalyzes (among other activities) the 3' decapping of DNA-ppG (formed by EC 6.5.1.8). -!- The enzyme binds the guanylate group to a histidine residue at its active site, forming a covalent enzyme-nucleotide phosphate intermediate, followed by the hydrolysis of the guanylate from the nucleic acid and its eventual release. -!- The enzyme also possesses the activity of EC 3.1.11.7 and EC 3.1.11.8.
3.1.11.7
Adenosine-5'-diphospho-5'-(DNA) diphosphatase.
based on mapping to UniProt Q7Z2E3
(1) Adenosine-5'-diphospho-5'-(DNA) + H(2)O = AMP + phospho-5'-(DNA). (2) Adenosine-5'-diphospho-5'-(ribonucleotide)-(DNA) + H(2)O = AMP + 5'-phospho-(ribonucleotide)-(DNA).
-!- Aprataxin is a DNA-binding protein involved in different types of DNA break repair. -!- The enzyme acts (among other activities) on abortive DNA ligation intermediates that contain an adenylate covalently linked to the 5'-phosphate DNA terminus. -!- It also acts when the adenylate is covalently linked to the 5'-phosphate of a ribonucleotide linked to a DNA strand, which is the result of abortive ligase activty on products of EC 3.1.26.4, an enzyme that cleaves RNA-DNA hybrids on the 5' side of the ribonucleotide found in the 5'-RNA-DNA-3' junction. -!- Aprataxin binds the adenylate group to a histidine residue within the active site, followed by its hydrolysis from the nucleic acid and eventual release, leaving a 5'-phosphate terminus that can be efficiently rejoined. -!- The enzyme also possesses the activities of EC 3.1.11.8 and EC 3.1.12.2.

UniProtKB Entries (1)

Q7Z2E3
APTX_HUMAN
Homo sapiens
Aprataxin

PDB Structure

PDB 6CVO
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Mechanism of APTX nicked DNA sensing and pleiotropic inactivation in neurodegenerative disease.
Tumbale, P., Schellenberg, M.J., Mueller, G.A., Fairweather, E., Watson, M., Little, J.N., Krahn, J., Waddell, I., London, R.E., Williams, R.S.
EMBO J.
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