EC number:2.7.7.51

Enzyme

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     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.7 Nucleotidyltransferases
ID:2.7.7.51
Description:Adenylylsulfate--ammonia adenylyltransferase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.7.51
BRENDA Enzyme Link: BRENDA 2.7.7.51
KEGG Enzyme Link: KEGG2.7.7.51
BioCyc Enzyme Link: BioCyc 2.7.7.51
ExPASy Enzyme Link: ExPASy2.7.7.51
EC2PDB Enzyme Link: EC2PDB 2.7.7.51
ExplorEnz Enzyme Link: ExplorEnz 2.7.7.51
PRIAM enzyme-specific profiles Link: PRIAM 2.7.7.51
IntEnz Enzyme Link: IntEnz 2.7.7.51
MEDLINE Enzyme Link: MEDLINE 2.7.7.51

EC number:2.7.7.51

MSA:

2.7.7.51;
Phylogenetic Tree:

2.7.7.51;
Uniprot:
M-CSA:
RHEA:19197 adenosine 5'-phosphosulfate + NH4(+) = adenosine 5'-phosphoramidate + 2 H(+) + sulfate
RULE(radius=1) [*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[O;H0;+0:5]-[*:6].[NH3;+0:7]>>[*:6]-[OH;+0:5].[*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[NH2;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Purification and properties of adenylyl sulphate:ammonia adenylyltransferase from Chlorella catalysing the formation of adenosine 5' -phosphoramidate from adenosine 5' -phosphosulphate and ammonia.Fankhauser H, Schiff JA, Garber LJ1981 Jun 16274307