The domain within your query sequence starts at position 1 and ends at position 404; the E-value for the GSH_synth_ATP domain shown below is 9.2e-130.
MDFNILVDAVSQNPAFLEQTLSSTIKKDDYTARLFDIYKQVLKEGIAQTVFLGLNRSDYM FQCGADGSKALKQIEINTISASFGGLASRTPAVHRHVLNVLNKTKEASKILSNNPSKGLA LGIAKAWELYGSANAVVLLIAQEKERNIFDQRAVENELLDRKIHVIRGRFEDVSERGSLD QNRRLFMDDQEVAVVYFRDGYMPSQYNSQNWEARLMLERSRAAKCPDIAIQLAGTKKVQQ ELSRVGLLEALLPGQPEAVARLRATFAGLYSLDMGEEGDQAIAEALAAPSHFVLKPQREG GGNNLYGEEMVQALEQLKDSEERASYILMEKIEPEPFRNCLLRPGSPAQVVQCISELGIF GVYVRQGTTLVMNKHVGHLLRTKAVEHADGGVAAGVAVLDNPYP
GSH_synth_ATP |
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PFAM accession number: | PF03917 |
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Interpro abstract (IPR005615): | This entry represents 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. |
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_synth_ATP