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Search results 1 to 10 out of 10 for Nags

Category restricted to ProteinDomain (x)

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Categories

Category: ProteinDomain
Type Details Score
Protein Domain
Type: Domain
Description: The N-acetyltransferases (NAT) (EC 2.3.1.-) are enzymes that use acetylcoenzyme A (CoA) to transfer an acetyl group to a substrate, a reactionimplicated in various functions from bacterial antibiotic resistance tomammalian circadian rhythm and chromatin remodeling. The Gcn5-relatedN-acetyltransferases (GNAT) catalyze the transfer of the acetyl from the CoAdonor to a primary amine of the acceptor. The GNAT proteins share a domaincomposed of four conserved sequence motifs A-D [, ]. This GNAT domain isnamed after yeast GCN5 (from General Control Nonrepressed) and related histoneacetyltransferases (HATs) like Hat1 and PCAF. HATs acetylate lysine residuesof amino terminal histone tails, resulting in transcription activation.Another category of GNAT, the aminoglycoside N-acetyltransferases, conferantibiotic resistance by catalyzing the acetylation of amino groups inaminoglycoside antibiotics []. GNAT proteins can also have anabolic andcatabolic functions in both prokaryotes and eukaryotes [, , , , ].The acetyltransferase/GNAT domain forms a structurally conserved fold of 6 to7 beta strands (B) and 4 helices (H) in the topologyB1-H1-H2-B2-B3-B4-H3-B5-H4-B6, followed by a C-terminal strand which may befrom the same monomer or contributed by another [, ]. MotifsD (B2-B3), A (B4-H3) and B (B5-H4) are collectively called the HAT core[, , ], while the N-terminal motif C (B1-H1) is less conserved.This entry represents the vertebrate-likeNAGS-type GNAT domain [].
Protein Domain
Type: Family
Description: N -Acetylglutamate (NAG) fulfils distinct biological roles in lower and higher organisms. In prokaryotes, lower eukaryotes and plants it is the first intermediate in the biosynthesis of arginine, whereas in ureotelic (excreting nitrogen mostly in the form of urea) vertebrates, it is an essential allosteric cofactor for carbamyl phosphate synthetase I (CPSI), the first enzyme of the urea cycle. The pathway that leads from glutamate to arginine in lower organisms employs eight steps, starting with the acetylation of glutamate to form NAG. In these species, NAG can be produced by two enzymatic reactions: one catalysed by NAG synthase (NAGS) and the other by ornithine acetyltransferase (OAT). In ureotelic species, NAG is produced exclusively by NAGS. In lower organisms, NAGS is feedback-inhibited by L-arginine, whereas mammalian NAGS activity is significantly enhanced by this amino acid. The NAGS genes of bacteria, fungi and mammals are more diverse than other arginine-biosynthesis and urea-cycle genes. The evolutionary relationship between the distinctly different roles of NAG and its metabolism in lower and higher organisms remains to be determined [].The pathway from glutamate to arginine is: NAGS; N-acetylglutamate synthase () (glutamate to N-acetylglutamate)NAGK; N-acetylglutamate kinase () (N-acetylglutamate to N-acetylglutamate-5P)N-acetyl-gamma-glutamyl-phosphate reductase () (N-acetylglutamate-5P to N-acetylglumate semialdehyde)Acetylornithine aminotransferase () (N-acetylglumate semialdehyde to N-acetylornithine)Acetylornithine deacetylase () (N-acetylornithine to ornithine)Arginase () (ornithine to arginine)This family represents acetylglutamate kinase ArgB ().
Protein Domain
Type: Family
Description: N -Acetylglutamate (NAG) fulfils distinct biological roles in lower and higher organisms. In prokaryotes, lower eukaryotes and plants it is the first intermediate in the biosynthesis of arginine, whereas in ureotelic (excreting nitrogen mostly in the form of urea) vertebrates, it is an essential allosteric cofactor for carbamyl phosphate synthetase I (CPSI), the first enzyme of the urea cycle. The pathway that leads from glutamate to arginine in lower organisms employs eight steps, starting with the acetylation of glutamate to form NAG. In these species, NAG can be produced by two enzymatic reactions: one catalysed by NAG synthase (NAGS) and the other by ornithine acetyltransferase (OAT). In ureotelic species, NAG is produced exclusively by NAGS. In lower organisms, NAGS is feedback-inhibited by L-arginine, whereas mammalian NAGS activity is significantly enhanced by this amino acid. The NAGS genes of bacteria, fungi and mammals are more diverse than other arginine-biosynthesis and urea-cycle genes. The evolutionary relationship between the distinctly different roles of NAG and its metabolism in lower and higher organisms remains to be determined [].The pathway from glutamate to arginine is: NAGS; N-acetylglutamate synthase () (glutamate to N-acetylglutamate)NAGK; N-acetylglutamate kinase () (N-acetylglutamate to N-acetylglutamate-5P)N-acetyl-gamma-glutamyl-phosphate reductase () (N-acetylglutamate-5P to N-acetylglumate semialdehyde)Acetylornithine aminotransferase () (N-acetylglumate semialdehyde to N-acetylornithine)Acetylornithine deacetylase () (N-acetylornithine to ornithine)Arginase () (ornithine to arginine)This family includes acetylglutamate kinase and related enzymes [LysW]-aminoadipate/[LysW]-glutamate kinase (LysZ), which is involved both in the biosynthesis of lysine and arginine [], and [LysW]-aminoadipate kinase [].
Protein Domain
Type: Family
Description: N -Acetylglutamate (NAG) fulfils distinct biological roles in lower and higher organisms. In prokaryotes, lower eukaryotes and plants it is the first intermediate in the biosynthesis of arginine, whereas in ureotelic (excreting nitrogen mostly in the form of urea) vertebrates, it is an essential allosteric cofactor for carbamyl phosphate synthetase I (CPSI), the first enzyme of the urea cycle. The pathway that leads from glutamate to arginine in lower organisms employs eight steps, starting with the acetylation of glutamate to form NAG. In these species, NAG can be produced by two enzymatic reactions: one catalysed by NAG synthase (NAGS) and the other by ornithine acetyltransferase (OAT). In ureotelic species, NAG is produced exclusively by NAGS. In lower organisms, NAGS is feedback-inhibited by L-arginine, whereas mammalian NAGS activity is significantly enhanced by this amino acid. The NAGS genes of bacteria, fungi and mammals are more diverse than other arginine-biosynthesis and urea-cycle genes. The evolutionary relationship between the distinctly different roles of NAG and its metabolism in lower and higher organisms remains to be determined [].The pathway from glutamate to arginine is: NAGS; N-acetylglutamate synthase () (glutamate to N-acetylglutamate)NAGK; N-acetylglutamate kinase () (N-acetylglutamate to N-acetylglutamate-5P)N-acetyl-gamma-glutamyl-phosphate reductase () (N-acetylglutamate-5P to N-acetylglumate semialdehyde)Acetylornithine aminotransferase () (N-acetylglumate semialdehyde to N-acetylornithine)Acetylornithine deacetylase () (N-acetylornithine to ornithine)Arginase () (ornithine to arginine)This entry represents N-acetylglutamate kinase (NAGK) with a C-terminal GNAT domain. Majority of proteins in this entry are from bacteria, including argB from Xylella fastidiosa (UniProt:Q9PEM7).
Protein Domain
Type: Family
Description: N -Acetylglutamate (NAG) fulfils distinct biological roles in lower and higher organisms. In prokaryotes, lower eukaryotes and plants it is the first intermediate in the biosynthesis of arginine, whereas in ureotelic (excreting nitrogen mostly inthe form of urea) vertebrates, it is an essential allosteric cofactor for carbamyl phosphate synthetase I (CPSI), the first enzyme of the urea cycle. The pathway that leads from glutamate to arginine in lower organisms employs eight steps, starting with the acetylation of glutamate to form NAG. In these species, NAG can be produced by two enzymatic reactions: one catalysed by NAG synthase (NAGS) and the other by ornithine acetyltransferase (OAT). In ureotelic species, NAG is produced exclusively by NAGS. In lower organisms, NAGS is feedback-inhibited by L-arginine, whereas mammalian NAGS activity is significantly enhanced by this amino acid. The NAGS genes of bacteria, fungi and mammals are more diverse than other arginine-biosynthesis and urea-cycle genes. The evolutionary relationship between the distinctly different roles of NAG and its metabolism in lower and higher organisms remains to be determined [].The pathway from glutamate to arginine is: NAGS; N-acetylglutamate synthase () (glutamate to N-acetylglutamate)NAGK; N-acetylglutamate kinase () (N-acetylglutamate to N-acetylglutamate-5P)N-acetyl-gamma-glutamyl-phosphate reductase () (N-acetylglutamate-5P to N-acetylglumate semialdehyde)Acetylornithine aminotransferase () (N-acetylglumate semialdehyde to N-acetylornithine)Acetylornithine deacetylase () (N-acetylornithine to ornithine)Arginase () (ornithine to arginine)This group represents a N-acetylglutamate synthase, animal type [].
Protein Domain
Type: Family
Description: N -Acetylglutamate (NAG) fulfils distinct biological roles in lower and higher organisms. In prokaryotes, lower eukaryotes and plants it is the first intermediate in the biosynthesis of arginine, whereas in ureotelic (excreting nitrogen mostly in the form of urea) vertebrates, it is an essential allosteric cofactor for carbamyl phosphate synthetase I (CPSI), the first enzyme of the urea cycle. The pathway that leads from glutamate to arginine in lower organisms employs eight steps, starting with the acetylation of glutamate to form NAG. In these species, NAG can be produced by two enzymatic reactions: one catalysed by NAG synthase (NAGS) and the other by ornithine acetyltransferase (OAT). In ureotelic species, NAG is produced exclusively by NAGS. In lower organisms, NAGS is feedback-inhibited by L-arginine, whereas mammalian NAGS activity is significantly enhanced by this amino acid. The NAGS genes of bacteria, fungi and mammals are more diverse than other arginine-biosynthesis and urea-cycle genes. The evolutionary relationship between the distinctly different roles of NAG and its metabolism in lower and higher organisms remains to be determined [].The pathway from glutamate to arginine is: NAGS; N-acetylglutamate synthase () (glutamate to N-acetylglutamate)NAGK; N-acetylglutamate kinase () (N-acetylglutamate to N-acetylglutamate-5P)N-acetyl-gamma-glutamyl-phosphate reductase () (N-acetylglutamate-5P to N-acetylglumate semialdehyde)Acetylornithine aminotransferase () (N-acetylglumate semialdehyde to N-acetylornithine)Acetylornithine deacetylase () (N-acetylornithine to ornithine)Arginase () (ornithine to arginine)This group represents a N-acetylglutamate synthase, belonging to the Ascomycetes [, ].
Protein Domain
Type: Active_site
Description: N -Acetylglutamate (NAG) fulfils distinct biological roles in lower and higher organisms. In prokaryotes, lower eukaryotes and plants it is the first intermediate in the biosynthesis of arginine, whereas in ureotelic (excreting nitrogen mostly in the form of urea) vertebrates, it is an essential allosteric cofactor for carbamyl phosphate synthetase I (CPSI), the first enzyme of the urea cycle. The pathway that leads from glutamate to arginine in lower organisms employs eight steps, starting with the acetylation of glutamate to form NAG. In these species, NAG can be produced by two enzymatic reactions: one catalysed by NAG synthase (NAGS) and the other by ornithine acetyltransferase (OAT). In ureotelic species, NAG is produced exclusively by NAGS. In lower organisms, NAGS is feedback-inhibited by L-arginine, whereas mammalian NAGS activity is significantly enhanced by this amino acid. The NAGS genes of bacteria, fungi and mammals are more diverse than other arginine-biosynthesis and urea-cycle genes. The evolutionary relationship between the distinctly different roles of NAG and its metabolism in lower and higher organisms remains to be determined [].The pathway from glutamate to arginine is: NAGS; N-acetylglutamate synthase () (glutamate to N-acetylglutamate)NAGK; N-acetylglutamate kinase () (N-acetylglutamate to N-acetylglutamate-5P)N-acetyl-gamma-glutamyl-phosphate reductase () (N-acetylglutamate-5P to N-acetylglumate semialdehyde)Acetylornithine aminotransferase () (N-acetylglumate semialdehyde to N-acetylornithine)Acetylornithine deacetylase () (N-acetylornithine to ornithine)Arginase () (ornithine to arginine)N-acetyl-gamma-glutamyl-phosphate reductase () (AGPR) [, ]is the enzyme that catalyzes the third step in the biosynthesis of arginine from glutamate, the NADP-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. In bacteria it is a monofunctional protein of 35 to 38kDa (gene argC) while in fungi it is part of a bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) which contains a N-terminal acetylglutamate kinase (() domain and a C-terminal AGPR domain. In the Mycobacterium tuberculosis enzyme, a cysteine has been shown to be implicated in the catalytic activity; the region around this residue is well conserved and is used as a signature pattern for the proteins in this entry [, ].
Protein Domain
Type: Domain
Description: This is the N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the arginine-biosynthesis pathway (ABP) found in gamma- and beta-proteobacteria and higher plant chloroplasts. The domain architecture of these NAGS consists of an N-terminal NAG kinase-like (ArgB) domain and a C-terminal NAG synthase, acetyltransferase (ArgA) domain. Both bacterial and plant sequences have a conserved N-terminal extension; a similar sequence in the NAG kinases of the cyclic arginine-biosynthesis pathway has been implicated in feedback inhibition sensing. Plant sequences also have an N-terminal chloroplast transit peptide and an insert (approx. 70 residues) in the C-terminal region of ArgB [, ].
Protein Domain
Type: Family
Description: N -Acetylglutamate (NAG) fulfils distinct biological roles in lower and higher organisms. In prokaryotes, lower eukaryotes and plants it is the first intermediate in the biosynthesis of arginine, whereas in ureotelic (excreting nitrogen mostly in the form of urea) vertebrates, it is an essential allosteric cofactor for carbamyl phosphate synthetase I (CPSI), the first enzyme of the urea cycle. The pathway that leads from glutamate to arginine in lower organisms employs eight steps, starting with the acetylation of glutamate to formNAG. In these species, NAG can be produced by two enzymatic reactions: one catalysed by NAG synthase (NAGS) and the other by ornithine acetyltransferase (OAT). In ureotelic species, NAG is produced exclusively by NAGS. In lower organisms, NAGS is feedback-inhibited by L-arginine, whereas mammalian NAGS activity is significantly enhanced by this amino acid. The NAGS genes of bacteria, fungi and mammals are more diverse than other arginine-biosynthesis and urea-cycle genes. The evolutionary relationship between the distinctly different roles of NAG and its metabolism in lower and higher organisms remains to be determined [].The pathway from glutamate to arginine is: NAGS; N-acetylglutamate synthase () (glutamate to N-acetylglutamate)NAGK; N-acetylglutamate kinase () (N-acetylglutamate to N-acetylglutamate-5P)N-acetyl-gamma-glutamyl-phosphate reductase () (N-acetylglutamate-5P to N-acetylglumate semialdehyde)Acetylornithine aminotransferase () (N-acetylglumate semialdehyde to N-acetylornithine)Acetylornithine deacetylase () (N-acetylornithine to ornithine)Arginase () (ornithine to arginine)N-acetyl-gamma-glutamyl-phosphate reductase () (AGPR, NAGSA dehydrogenase) [, ]is the enzyme that catalyses the third step in the biosynthesis of arginine from glutamate, the NADP-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. In bacteria it is a monofunctional protein of 35 to 38kDa (gene argC), while in fungi it is part of a bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) which contains a N-terminal acetylglutamate kinase () domain and a C-terminal AGPR domain. In the Escherichia coli enzyme, a cysteine has been shown to be implicated in the catalytic activity, and the region around this residue is well conserved.This entry represents the less common of two related families of N-acetyl-gamma-glutamyl-phosphate reductase, an enzyme catalyzing the third step or Arg biosynthesis from Glu. The two families differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment.
Protein Domain
Type: Family
Description: N -Acetylglutamate (NAG) fulfils distinct biological roles in lower and higher organisms. In prokaryotes, lower eukaryotes and plants it is the first intermediate in the biosynthesis of arginine, whereas in ureotelic (excreting nitrogen mostly in the form of urea) vertebrates, it is an essential allosteric cofactor for carbamyl phosphate synthetase I (CPSI), the first enzyme of the urea cycle. The pathway that leads from glutamate to arginine in lower organisms employs eight steps, starting with the acetylation of glutamate to form NAG. In these species, NAG can be produced by two enzymatic reactions: one catalysed by NAG synthase (NAGS) and the other by ornithine acetyltransferase (OAT). In ureotelic species, NAG is produced exclusively by NAGS. In lower organisms, NAGS is feedback-inhibited by L-arginine, whereas mammalian NAGS activity is significantly enhanced by this amino acid. The NAGS genes of bacteria, fungi and mammals are more diverse than other arginine-biosynthesis and urea-cycle genes. The evolutionary relationship between the distinctly different roles of NAG and its metabolism in lower and higher organisms remains to be determined [].The pathway from glutamate to arginine is: NAGS; N-acetylglutamate synthase () (glutamate to N-acetylglutamate)NAGK; N-acetylglutamate kinase () (N-acetylglutamate to N-acetylglutamate-5P)N-acetyl-gamma-glutamyl-phosphate reductase () (N-acetylglutamate-5P to N-acetylglumate semialdehyde)Acetylornithine aminotransferase () (N-acetylglumate semialdehyde to N-acetylornithine)Acetylornithine deacetylase () (N-acetylornithine to ornithine)Arginase () (ornithine to arginine)N-acetyl-gamma-glutamyl-phosphate reductase () (AGPR, NAGSA dehydrogenase) [, ]is the enzyme that catalyses the third step in the biosynthesis of arginine from glutamate, the NADP-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. In bacteria it is a monofunctional protein of 35 to 38kDa (gene argC), while in fungi it is part of a bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) which contains a N-terminal acetylglutamate kinase () domain and a C-terminal AGPR domain. In the Escherichia coli enzyme, a cysteine has been shown to be implicated in the catalytic activity, and the region around this residue is well conserved.This entry represents the more common of two related families of N-acetyl-gamma-glutamyl-phosphate reductase, an enzyme catalyzing the third step or Arg biosynthesis from Glu. The two families differ by phylogeny, similarity clustering, and the gap architecture in a multiple sequence alignment. Bacterial members of this family tend to be found within Arg biosynthesis operons. This family also includes LysY (LysW-L-2-aminoadipate/LysW-L-glutamate phosphate reductase), which is involved in both the arginine and lysine biosynthetic pathways. Several bacteria and archaea utilize the amino group-carrier protein, LysW, for lysine biosynthesis from alpha-aminoadipate (AAA). In some cases, such as Sulfolobus, LysW is also used to protect the amino group of glutamate in arginine biosynthesis. After LysW modification, AAA and glutamate are converted to lysine and ornithine, respectively, by a single set of enzymes with dual functions []. LysY is the third enzyme in lysine biosynthesis from AAA []. LysY shows high sequence identity and functional similarities with ArgC, and they are considered to have evolved from a common ancestor [, ].