Enzyme

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     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.7 Nucleotidyltransferases
ID:2.7.7.96
Description:ADP-D-ribose pyrophosphorylase.
Alternative Name: NUDIX5.
Diphosphate--ADP-D-ribose adenylyltransferase.
Diphosphate adenylyltransferase.
Cath: 3.90.79.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.7.96
BRENDA Enzyme Link: BRENDA 2.7.7.96
KEGG Enzyme Link: KEGG2.7.7.96
BioCyc Enzyme Link: BioCyc 2.7.7.96
ExPASy Enzyme Link: ExPASy2.7.7.96
EC2PDB Enzyme Link: EC2PDB 2.7.7.96
ExplorEnz Enzyme Link: ExplorEnz 2.7.7.96
PRIAM enzyme-specific profiles Link: PRIAM 2.7.7.96
IntEnz Enzyme Link: IntEnz 2.7.7.96
MEDLINE Enzyme Link: MEDLINE 2.7.7.96
MSA:

2.7.7.96;

Phylogenetic Tree:

2.7.7.96;

Uniprot:
M-CSA:
RHEA:50248 ATP + D-ribose 5-phosphate + H(+) = ADP-D-ribose + diphosphate
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8].[H+;H0:9]>>[*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1]
Reaction
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References

TitleAuthorsDatePubMed ID
ADP-ribose-derived nuclear ATP synthesis by NUDIX5 is required for chromatin remodeling.Wright RH, Lioutas A, Le Dily F, Soronellas D, Pohl A, Bonet J, Nacht AS, Samino S, Font-Mateu J, Vicent GP, Wierer M, Trabado MA, Schelhorn C, Carolis C, Macias MJ, Yanes O, Oliva B, Beato M2016 Jun 327257257