Enzyme

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EC Tree
     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.4 In cyclic amidines
ID:3.5.4.18
Description:ATP deaminase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.4.18
BRENDA Enzyme Link: BRENDA 3.5.4.18
KEGG Enzyme Link: KEGG3.5.4.18
BioCyc Enzyme Link: BioCyc 3.5.4.18
ExPASy Enzyme Link: ExPASy3.5.4.18
EC2PDB Enzyme Link: EC2PDB 3.5.4.18
ExplorEnz Enzyme Link: ExplorEnz 3.5.4.18
PRIAM enzyme-specific profiles Link: PRIAM 3.5.4.18
IntEnz Enzyme Link: IntEnz 3.5.4.18
MEDLINE Enzyme Link: MEDLINE 3.5.4.18
MSA:

3.5.4.18;

Phylogenetic Tree:

3.5.4.18;

Uniprot:
M-CSA:
RHEA:13037 ATP + H(+) + H2O = ITP + NH4(+)
RULE(radius=1) [*:1]:[c;H0;+0:2](-[NH2;+0:3]):[n;H0;+0:4]:[*:5].[H+;H0:6].[OH2;+0:7]>>[*:1]:[c;H0;+0:2](=[O;H0;+0:7]):[nH;+0:4]:[*:5].[NH3;+0:3]
Reaction
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References

TitleAuthorsDatePubMed ID
Purification and properties of ATP deaminase from Microsporum audouini.Chung ST, Aida K1967 Jan6048966
A new adenylate deaminase from red marine alga Porphyra crispata.Su JC, Li CC, Ting CC1966 Feb5940938
A non-specific adenine nucleotide deaminase from desulfovibrio desulfuricans.Yates MG1969 Feb 115773435