Member database | Pfam |
Pfam type | domain |
Short name | GATase_2 |
Clan | NTN |
Author | Finn RD;0000-0001-8626-2148 Bateman A;0000-0002-6982-4660 Eberhardt R;0000-0001-6152-1369 |
Sequence Ontology | 0000417 |
Description Imported from IPR017932
* Amido phosphoribosyltransferase (glutamine phosphoribosylpyrophosphate amidotransferase). An enzyme which catalyses the first step in purine biosynthesis, the transfer of the ammonia group of glutamine to PRPP to form 5-phosphoribosylamine (gene purF in bacteria, ADE4 in yeast).
* Glucosamine--fructose-6-phosphate aminotransferase. This enzyme catalyses a key reaction in amino sugar synthesis, the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine (gene glmS in Escherichia coli, nodM in Rhizobium, GFA1 in yeast).
* Asparagine synthetase (glutamine-hydrolyzing). This enzyme is responsible for the synthesis of asparagine from aspartate and glutamine.
* Glutamate synthase (gltS), an enzyme which participates in the ammonia assimilation process by catalysing the formation of glutamate from glutamine and 2-oxoglutarate. Glutamate synthase is a multicomponent iron-sulphur flavoprotein and three types occur which use a different electron donor: NADPH-dependent gltS (large chain), ferredoxin-dependent gltS and NADH-dependent gltS
References Imported from IPR017932
1.The amidotransferases. Buchanan JM. Adv. Enzymol. Relat. Areas Mol. Biol. 39, 91-183, (1973). PMID: 4355768
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.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
4.Glutamate synthase: a complex iron-sulfur flavoprotein. Vanoni MA, Curti B. Cell. Mol. Life Sci. 55, 617-38, (1999). View articlePMID: 10357231
5.The glutamine-utilizing site of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase. Vollmer SJ, Switzer RL, Hermodson MA, Bower SG, Zalkin H. J. Biol. Chem. 258, 10582-5, (1983). View articlePMID: 6411716
6.The N-terminal cysteine of human asparagine synthetase is essential for glutamine-dependent activity. Van Heeke G, Schuster SM. J. Biol. Chem. 264, 19475-7, (1989). View articlePMID: 2573597
7.The mechanism of glutamine-dependent amidotransferases. Massiere F, Badet-Denisot MA. Cell. Mol. Life Sci. 54, 205-22, (1998). View articlePMID: 9575335
8.Glutamate synthase: a fascinating pathway from L-glutamine to L-glutamate. van den Heuvel RH, Curti B, Vanoni MA, Mattevi A. Cell. Mol. Life Sci. 61, 669-81, (2004). View articlePMID: 15052410