The domain within your query sequence starts at position 249 and ends at position 535; the E-value for the Glutaminase domain shown below is 4.2e-123.



PFAM accession number:PF04960
Interpro abstract (IPR015868):

Glutaminases ( EC ) deaminate glutamine to glutamate. In Bacillus subtilis, glutaminase is encoded by glnA, which is part of an operon, glnA-glnT (formerly ybgJ-ybgH), where glnT encodes a glutamine transporter. The glnA-glnT operon is regulated by the 2-component system GlnK-GlnL in response to glutamine [ (PUBMED:15995196) ]. This entry represents the core structural motif of a family of glutaminases that include GlnA, which are characterised by their beta-lactamase-like topology, containing a cluster of alpha-helices and an alpha/beta sandwich.

This family describes the enzyme glutaminase, from a larger family that includes serine-dependent beta-lactamases and penicillin-binding proteins. Many bacteria have two isozymes. This model is based on selected known glutaminases and their homologues within prokaryotes, with the exclusion of highly-derived (long branch) and architecturally varied homologues, so as to achieve conservative assignments. A sharp drop in scores occurs below 250, and cutoffs are set accordingly. The enzyme converts glutamine to glutamate, with the release of ammonia. Members tend to be described as glutaminase A (glsA), where B (glsB) is unknown and may not be homologous (as in Rhizobium etli. Some species have two isozymes that may both be designated A (GlsA1 and GlsA2).

GO process:glutamine metabolic process (GO:0006541)
GO function:glutaminase activity (GO:0004359)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Glutaminase