The domain within your query sequence starts at position 333 and ends at position 426; the E-value for the GARS_C domain shown below is 1.33e-44.

SAVTVVMASKGYPGAYTKGVEITGFPEAQALGLQVFHAGTALKDGKVVTSGGRVLTVTAV
QENLMSALAEARKGLAALKFEGAIYRKDIGFRAV

GARS_C

Phosphoribosylglycinamide synthetase, C domain
GARS_C
SMART accession number:SM01210
Description: Phosphoribosylglycinamide synthetase catalyses the second step in the de novo biosynthesis of purine. The reaction catalysed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the C-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase (Pfam PF02787).
Interpro abstract (IPR020560):

Phosphoribosylglycinamide synthetase (EC 6.3.4.13) (GARS) (phosphoribosylamine glycine ligase) [(PUBMED:2687276)] catalyses the second step in the de novo biosynthesis of purine. The reaction catalysed by phosphoribosylglycinamide synthetase is the ATP-dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide: ATP + 5-phosphoribosylamine + glycine = ADP + Pi + 5'-phosphoribosylglycinamide In bacteria, GARS is a monofunctional enzyme (encoded by the purD gene). In yeast, GARS is part of a bifunctional enzyme (encoded by the ADE5,7 gene) in conjunction with phosphoribosylformylglycinamidine cyclo-ligase (AIRS) [(PUBMED:3097325)]. In higher eukaryotes, GARS is part of a trifunctional enzyme in conjunction with AIRS and with phosphoribosylglycinamide formyltransferase (GART), forming GARS-AIRS-GART [(PUBMED:2147474)].

This entry represents the C-domain, which is related to the C-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase (IPR005480).

GO process:purine nucleobase biosynthetic process (GO:0009113)
GO function:phosphoribosylamine-glycine ligase activity (GO:0004637)
Family alignment:
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There are 23116 GARS_C domains in 23108 proteins in SMART's nrdb database.

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