InterPro : IPR029062

Name  Class I glutamine amidotransferase-like Short Name  Class_I_gatase-like
Type  Domain Description  This entry 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 []. 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 [, ]: 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 [, ]. 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.
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

Other

7 Child Features

Id Name Short Name Type
IPR002818 ThiJ/PfpI ThiJ/PfpI Domain
IPR017926 Glutamine amidotransferase GATASE Domain
IPR011698 CobB/CobQ-like glutamine amidotransferase GATase_3 Domain
IPR010768 Domain of unknown function DUF1355 DUF1355 Domain
IPR029010 ThuA-like domain ThuA-like Domain
IPR013738 Beta-galactosidase trimerisation Beta_galactosidase_Trimer Domain
IPR025628 DJ-1 domain, InhA-type DJ-1_InhA Domain

0 Contains

0 Found In

0 Parent Features

5 Publications

First Author Title Year Journal Volume Pages
Buchanan JM The amidotransferases. 1973 Adv Enzymol Relat Areas Mol Biol 39 91-183
Weng ML Structural role for a conserved region in the CTP synthetase glutamine amide transfer domain. 1987 J Bacteriol 169 3023-8
Nyunoya H Sequence of the small subunit of yeast carbamyl phosphate synthetase and identification of its catalytic domain. 1984 J Biol Chem 259 9790-8
Tesmer JJ The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families. 1996 Nat Struct Biol 3 74-86
Massière F The mechanism of glutamine-dependent amidotransferases. 1998 Cell Mol Life Sci 54 205-22



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)