EC number:2.4.2.17

Enzyme

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     2. Transferases
        2.4 Glycosyltransferases
            2.4.2 Pentosyltransferases
ID:2.4.2.17
Description:ATP phosphoribosyltransferase.
Alternative Name: Phosphoribosyl-ATP pyrophosphorylase.
Phosphoribosyl-ATP diphosphorylase.
Prosite: PDOC01020;
PDB:
PDBScop
5U99 8031438; 8031440; 8043816; 8043818;
5LHU 8031438; 8031440; 8043816; 8043818;
5LHT 8031438; 8031440; 8043816; 8043818;
1NH8 8031438; 8031440; 8043816; 8043818;
1NH7 8031438; 8031440; 8043816; 8043818;
 » show all
Cath: 3.30.70.120; 3.40.190.10;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.4.2.17
BRENDA Enzyme Link: BRENDA 2.4.2.17
KEGG Enzyme Link: KEGG2.4.2.17
BioCyc Enzyme Link: BioCyc 2.4.2.17
ExPASy Enzyme Link: ExPASy2.4.2.17
EC2PDB Enzyme Link: EC2PDB 2.4.2.17
ExplorEnz Enzyme Link: ExplorEnz 2.4.2.17
PRIAM enzyme-specific profiles Link: PRIAM 2.4.2.17
IntEnz Enzyme Link: IntEnz 2.4.2.17
MEDLINE Enzyme Link: MEDLINE 2.4.2.17

EC number:2.4.2.17

MSA:

2.4.2.17;
Phylogenetic Tree:

2.4.2.17;
Uniprot:
M-CSA:
RHEA:18473 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]:[n;H0;+0:4](-[CH;+0:5](-[*:6])-[*:7]):[c;H0;+0:8](:[*:9])=[NH;+0:10]>>[*:6]-[CH;+0:5](-[*:7])-[O;H0;+0:2]-[*:1].[*:3]:[n;H0;+0:4]:[c;H0;+0:8](:[*:9])-[NH2;+0:10]
Reaction
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References

TitleAuthorsDatePubMed ID
The structure of Escherichia coli ATP-phosphoribosyltransferase: identification of substrate binding sites and mode of AMP inhibition.Lohkamp B, McDermott G, Campbell SA, Coggins JR, Lapthorn AJ2004 Feb 614741209
Crystal structure of ATP phosphoribosyltransferase from Mycobacterium tuberculosis.Cho Y, Sharma V, Sacchettini JC2003 Mar 712511575