Entry
Name
adenosine-5'-diphospho-5'-[DNA] diphosphatase;
aprataxin;
5'-App5'-DNA adenylate hydrolase;
APTX (gene name);
HNT3 (gene name)
Class
Hydrolases;
Acting on acid anhydrides;
In phosphorus-containing anhydrides
BRITE hierarchy
Sysname
adenosine-5'-diphospho-5'-[DNA] hydrolase (adenosine 5'-phosphate-forming)
Reaction(IUBMB)
(1) adenosine-5'-diphospho-5'-[DNA] + H2O = AMP + phospho-5'-[DNA];
(2) adenosine-5'-diphospho-5'-(ribonucleotide)-[DNA] + H2O = AMP + 5'-phospho-(ribonucleotide)-[DNA]
Substrate
adenosine-5'-diphospho-5'-[DNA];
H2O [CPD:
C00001 ];
adenosine-5'-diphospho-5'-(ribonucleotide)-[DNA]
Product
AMP [CPD:
C00020 ];
phospho-5'-[DNA];
5'-phospho-(ribonucleotide)-[DNA]
Comment
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 , ribonuclease H, 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
3.6.1.70 , guanosine-5'-diphospho-5'-[DNA] diphosphatase, and EC
3.6.1.72 , DNA-3'-diphospho-5'-guanosine diphosphatase.
History
EC 3.6.1.71 created 2017 as EC 3.1.11.7, transferred 2019 to EC 3.6.1.71
Orthology
Genes
ANU : 117702473 117708186(Aptx)
PLOP : 125355383 125362898(Aptx)
TOD : 119230949(APTX) 119253332
PCW : 110204302 110220574(APTX)
TACU : 119923918 119948131
GSTE : 104252030 104258213(APTX)
CCAR : 109051898 109065131
PFOR : 103137845 103137850
PLAI : 106943046 106943049
PMEI : 106911873 106919284
PMRN : 116937213 116950843(APTX)
DSI : Dsimw501_GD19289(Dsim_GD19289)
DYA : Dyak_GE25605 Dyak_GE27392 Dyak_GE28076 Dyak_GE29197
DGR : 116806024 116806025 116806026 116806027 116806028 116806306 122322685 122322686 122322689 6569964
DMO : Dmoj_GI16920 Dmoj_GI23101 Dmoj_GI23102
DAZ : 108608649 108614288 108614368
ACOZ : 120951911 120961674
AARA : 120897054 120901540
AMER : 121590176 121590404
ASTE : 118502892 118504672
AMAP : 126565556 126566760
AFUN : 125763320 125774808
AMOU : 128297066 128298194
AMRS : 128708675 128718075
CQU : CpipJ_CPIJ001673 CpipJ_CPIJ001675
CPII : 120418370 120418385
PFUC : 122514504 122520652
APLN : 108734079 108740333
CSAT : 104708982 104734171 104768332
PVY : 116115203 116138719 116138755
PCIN : 129289633 129297600
PALZ : 118037517 118045838
SSPL : 121795633 121800888
PSOM : 113291612 113310226 113322015
TAES : 123085582 123092448 123097769
PVIR : 120652712 120687912
SMO : SELMODRAFT_104482 SELMODRAFT_89021
CGR : 2890291(GVI51_K08789)
NCS : NCAS_0B01160(NCAS0B01160)
NDI : NDAI_0E01030(NDAI0E01030)
TBL : TBLA_0B03650(TBLA0B03650)
TDL : TDEL_0A06520(TDEL0A06520)
KAF : KAFR_0A04000(KAFR0A04000)
KNG : KNAG_0G02710(KNAG0G02710)
LBG : 92206012(LODBEIA_P08160)
CAL : CAALFM_CR03440WA(CaO19.2376) CAALFM_CR03590CA(CaO19.4383)
CDU : CD36_28600 CD36_28780
ASAU : 88175556(PUMCH_004496)
YLI : 2911961(YALI2_E01329g)
NTE : NEUTE1DRAFT136002(NEUTE1DRAFT_136002)
SMP : 10803913(SMAC4_04695)
RTHE : 98125725(VTJ83DRAFT_4577)
TATV : 25779411(TrAtP1_011137)
TASP : 36616225(TrAFT101_008947)
PLJ : 28889959(PLICBS_008635)
CDET : 87941497(CDEST_04994)
BFU : BCIN_08g06920(Bchnt3)
PTRR : 6343811(PtrM4_109000)
ADAC : 96084620(ACET3X_004298)
CDEC : 89987830(IAS62_001055)
CTEG : 91989022(I308_102164)
CBAS : 91982213(I312_102165)
CDEP : 91089741(L203_105532)
KMG : 30167525(I203_106436)
KNE : 92178259(IAR55_001000)
KDJ : 28964778(I303_101076)
KBI : 30207303(I302_104195)
KPIN : 30169345(I206_100349)
KSH : 87953109(IL334_000978)
KER : 91106234(V865_007433)
CCAC : CcaHIS019_0406190(HNT3)
PSQ : PUNSTDRAFT_114838 PUNSTDRAFT_28176
ABP : AGABI1DRAFT122637(AGABI1DRAFT_122637)
ABV : AGABI2DRAFT187227(AGABI2DRAFT_187227)
SCM : SCHCO_02605771(SCHCODRAFT_02605771)
TCR : 506989.50 510149.100
LMAT : 92514372(LSCM1_04351)
LOI : 92359440(LSCM4_03506)
LEIS : 94179103(GH5_03630)
LENR : 94171338(CUR178_04117)
LEIN : 94187411(JIQ42_03738)
PHET : 94286741(JKF63_00613)
EHX : EMIHUDRAFT_424881 EMIHUDRAFT_434812
» show all
Taxonomy
Reference
Authors
Ahel I, Rass U, El-Khamisy SF, Katyal S, Clements PM, McKinnon PJ, Caldecott KW, West SC
Title
The neurodegenerative disease protein aprataxin resolves abortive DNA ligation intermediates.
Journal
Sequence
Reference
Authors
Tumbale P, Williams JS, Schellenberg MJ, Kunkel TA, Williams RS
Title
Aprataxin resolves adenylated RNA-DNA junctions to maintain genome integrity.
Journal
Sequence
Other DBs
ExplorEnz - The Enzyme Database: 3.6.1.71
ExPASy - ENZYME nomenclature database: 3.6.1.71