conserveddomain/PSSMID153225

Predicate	Object
abstract	Type 1 glutamine amidotransferase (GATase1)-like domain found in homoserine trans-succinylase (HTS). Type 1 glutamine amidotransferase (GATase1)-like domain found in homoserine trans-succinylase (HTS). HTS, the first enzyme in methionine biosynthesis in Escherichia coli, transfers a succinyl group from succinyl-CoA to homoserine forming succinyl homoserine. It has been suggested that the succinyl group of succinyl-CoA is initially transferred to an enzyme nucleophile before subsequent transfer to homoserine. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with GATase1 domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. It has been proposed that this cys is in the active site of the molecule. However, as succinyl has been found bound to a conserved lysine residue, this conserved cys may play a role in dimer formation. HTS activity is tightly regulated by several mechanisms including feedback inhibition and proteolysis. It represents a critical control point for cell growth and viability.
title	GATase1_HTS
isDiscussedBy	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9789165 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/24079090
type	http://purl.obolibrary.org/obo/SO_0000417

Predicate	Subject
has component	http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCA0A1D3PCK2 http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ03V79 http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCA0A120HUS7

Total number of triples: 8.