The domain within your query sequence starts at position 133 and ends at position 233; the E-value for the GSH_synthase domain shown below is 9e-38.
ANAVVLLIAQEKERNIFDQRAVENELLDRKIHVIRGRFEDVSERGSLDQNRRLFMDDQEV AVVYFRDGYMPSQYNSQNWEARLMLERSRAAKCPDIAIQLA
GSH_synthase |
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| PFAM accession number: | PF03199 |
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| Interpro abstract (IPR004887): | This entry represents the substrate-binding domain of glutathione synthetase ( EC 6.3.2.3 ) (GSS), a homodimeric enzyme that catalyses the conversion of gamma-L-glutamyl-L-cysteine and glycine to phosphate and glutathione in the presence of ATP. This is the second step in glutathione biosynthesis, the first step being catalysed by gamma-glutamylcysteine synthetase [ (PUBMED:15981742) ]. In humans, defects in GSS are inherited in an autosomal recessive way and are the cause of severe metabolic acidosis, 5-oxoprolinuria, and increased rate of haemolysis and defective function of the central nervous system. The substrate-binding domain has a 3-layer alpha/beta/alpha structure [ (PUBMED:10369661) ]. |
| GO process: | glutathione biosynthetic process (GO:0006750) |
| GO function: | ATP binding (GO:0005524), glutathione synthase activity (GO:0004363) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry GSH_synthase