Enzyme

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     2. Transferases
        2.4 Glycosyltransferases
            2.4.2 Pentosyltransferases
ID:2.4.2.14
Description:Amidophosphoribosyltransferase.
Alternative Name: Phosphoribosyldiphosphate 5-amidotransferase.
Glutamine phosphoribosylpyrophosphate amidotransferase.
Prosite: PDOC00406; PDOC00096;
PDB:
PDBScop
Cath: 3.60.20.10; 3.40.50.20; 3.40.50.2020;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.4.2.14
BRENDA Enzyme Link: BRENDA 2.4.2.14
KEGG Enzyme Link: KEGG2.4.2.14
BioCyc Enzyme Link: BioCyc 2.4.2.14
ExPASy Enzyme Link: ExPASy2.4.2.14
EC2PDB Enzyme Link: EC2PDB 2.4.2.14
ExplorEnz Enzyme Link: ExplorEnz 2.4.2.14
PRIAM enzyme-specific profiles Link: PRIAM 2.4.2.14
IntEnz Enzyme Link: IntEnz 2.4.2.14
MEDLINE Enzyme Link: MEDLINE 2.4.2.14
MSA:

2.4.2.14;

Phylogenetic Tree:

2.4.2.14;

Uniprot:
M-CSA:
RHEA:14905 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[NH2;+0:4].[*:5]-[OH;+0:6].[*:7]=[C;H0;+0:8](-[*:9])-[OH;+0:10]>>[*:1]-[CH;+0:2](-[*:3])-[O;H0;+0:6]-[*:5].[*:7]=[C;H0;+0:8](-[*:9])-[NH2;+0:4].[OH2;+0:10]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Purification and properties of glutamine phosphoribosylpyrophosphate amidotransferase from Bacillus subtilis.Wong JY, Bernlohr DA, Turnbough CL, Switzer RL1981 Sep 296794613
Glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli. Purification and properties.Messenger LJ, Zalkin H1979 May 10372191
Chemical genetic identification of glutamine phosphoribosylpyrophosphate amidotransferase as the target for a novel bleaching herbicide in Arabidopsis.Walsh TA, Bauer T, Neal R, Merlo AO, Schmitzer PR, Hicks GR, Honma M, Matsumura W, Wolff K, Davies JP2007 Jul17616508