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gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
These peptidases have gamma-glutamyl hydrolase activity; that is they catalyse the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to Pfam:PF00117, but contain extensions in four loops and at the C terminus [1]. [1]. 11953431. Three-dimensional structure of human gamma -glutamyl hydrolase.. A class I glatamine amidotransferase adapted for a complex. substate.. Li H, Ryan TJ, Chave KJ, Van Roey P;. J Biol Chem 2002;277:24522-24529. (from Pfam)
CTP synthase N-terminus
This family consists of the N-terminal region of the CTP synthase protein (EC:6.3.4.2). This family is found in conjunction with Pfam:PF00117 located in the C-terminal region of the protein. CTP synthase catalyses the synthesis of CTP from UTP by amination of the pyrimidine ring at the 4-position [1]. [1]. 12522217. Thr-431 and Arg-433 are part of a conserved sequence motif of. the glutamine amidotransferase domain of CTP synthases and are. involved in GTP activation of the Lactococcus lactis enzyme.. Willemoes M;. J Biol Chem 2003;278:9407-9411. (from Pfam)
Glutamine amidotransferase class-I
CTP synthase
cytidine triphosphate (CTP) synthase catalyzes the conversion of UTP to CTP in the last committed step in pyrimidine nucleotide biosynthesis
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen
glutamine hydrolyzing CTP synthase
CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. The enzyme catalyzes the reaction L-glutamine + H2O + UTP + ATP = CTP + phosphate + ADP + L-glutamate. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. This gene has been found circa 500 bp 5' upstream of enolase in both beta (Nitrosomonas europaea) and gamma (E.coli) subdivisions of proteobacterium (FEMS Microbiol Lett 1998 Aug 1;165(1):153-7).
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