H
IPR029062

Class I glutamine amidotransferase-like

InterPro entry
Short nameClass_I_gatase-like
Overlapping entries
 
DJ-1/PfpI (IPR002818)

Description

This superfamily represents the class I glutamine amidotransferase-like domain.

Glutamine amidotransferase (GATase) enzymes catalyse the removal of the ammonia group from glutamine and then transfer this group to a substrate to form a new carbon-nitrogen group
[3]
. The GATase domain exists either as a separate polypeptidic subunit or as part of a larger polypeptide fused in different ways to a synthase domain. Two classes of GATase domains have been identified
[2, 4]
: class-I (also known as trpG-type or triad) and class-II (also known as purF-type or Ntn). In class I glutamine amidotransferases, a triad of conserved Cys-His-Glu forms the active site, wherein the catalytic cysteine is essential for the amidotransferase activity
[1, 5]
. Different structures show that the active site Cys of type 1 GATase is located at the tip of a nucleophile elbow.

This entry also include the DJ-1/PfpI protein that contains a catalytic triad or dyad different from the class I GAT triad.

References

1.The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families. Tesmer JJ, Klem TJ, Deras ML, Davisson VJ, Smith JL. Nat. Struct. Biol. 3, 74-86, (1996). View articlePMID: 8548458

2.Structural role for a conserved region in the CTP synthetase glutamine amide transfer domain. Weng ML, Zalkin H. J. Bacteriol. 169, 3023-8, (1987). View articlePMID: 3298209

3.The amidotransferases. Buchanan JM. Adv. Enzymol. Relat. Areas Mol. Biol. 39, 91-183, (1973). PMID: 4355768

4.Sequence of the small subunit of yeast carbamyl phosphate synthetase and identification of its catalytic domain. Nyunoya H, Lusty CJ. J. Biol. Chem. 259, 9790-8, (1984). View articlePMID: 6086650

5.The mechanism of glutamine-dependent amidotransferases. Massiere F, Badet-Denisot MA. Cell. Mol. Life Sci. 54, 205-22, (1998). View articlePMID: 9575335

Cross References

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