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pantoate--beta-alanine ligase
Pantoate-beta-alanine ligase, also know as pantothenate synthase, (EC:6.3.2.1) catalyses the formation of pantothenate from pantoate and alanine [1]. [1]. 374975. Pantothenate synthetase from Escherichia coli [D-pantoate: beta-alanine ligase (AMP-forming), EC 6.3.2.1]. Miyatake K, Nakano Y, Kitaoka S;. Methods Enzymol 1979;62:215-219. (from Pfam)
4-phosphopantoate--beta-alanine ligase
4-phosphopantoate--beta-alanine ligase catalyzes the conversion of (R)-4-phosphopantoate and beta-alanine to 4'-phosphopantothenate in the CoA biosynthesis pathway
adenylyltransferase/cytidyltransferase family protein
Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.
This type of pantothenate synthetase, EC 6.3.2.1, is found in bacteria, and is unrelated to an archaeal form, EC 6.3.2.44 (see PRK13761).
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