EC number:7.2.2.15

Enzyme

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EC Tree
     7. Translocases
        7.2 Catalysing the translocation of inorganic cations
            7.2.2 Linked to the hydrolysis of a nucleoside triphosphate
ID:7.2.2.15
Description:P-type Ag(+) transporter.
Prosite: PDOC00139;
PDB:
PDBScop

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 7.2.2.15
BRENDA Enzyme Link: BRENDA 7.2.2.15
KEGG Enzyme Link: KEGG7.2.2.15
BioCyc Enzyme Link: BioCyc 7.2.2.15
ExPASy Enzyme Link: ExPASy7.2.2.15
EC2PDB Enzyme Link: EC2PDB 7.2.2.15
ExplorEnz Enzyme Link: ExplorEnz 7.2.2.15
PRIAM enzyme-specific profiles Link: PRIAM 7.2.2.15
IntEnz Enzyme Link: IntEnz 7.2.2.15
MEDLINE Enzyme Link: MEDLINE 7.2.2.15

EC number:7.2.2.15

MSA:

7.2.2.15;
Phylogenetic Tree:

7.2.2.15;
Uniprot:
M-CSA:
RHEA:14733 Ag(+)(in) + ATP + H2O = ADP + Ag(+)(out) + H(+) + phosphate
RULE(radius=1) [*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[O;H0;+0:5]-[*:6].[OH2;+0:7]>>[*:6]-[OH;+0:5].[*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[OH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Molecular basis for resistance to silver cations in Salmonella.Gupta A, Matsui K, Lo JF, Silver S1999 Feb9930866
ATP-dependent silver transport across the basolateral membrane of rainbow trout gills.Bury NR, Grosell M, Grover AK, Wood CM1999 Aug 1510448119