MULTISPECIES: N-acetyl-gamma-glutamyl-phosphate reductase [Lelliottia]
Protein Classification
NAGSA dehydrogenase family protein( domain architecture ID 11493209)
NAGSA (N-acetyl-glutamate semialdehyde) dehydrogenase family protein such as N-acetyl-gamma-glutamyl-phosphate reductase (also called NAGSA dehydrogenase) that catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to N-acetyl-L-glutamate 5-semialdehyde, as part of the L-arginine biosynthesis
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| argC | TIGR01850 | N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ... |
2-334 | 0e+00 | ||||||
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model 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. [Amino acid biosynthesis, Glutamate family] : Pssm-ID: 273832 [Multi-domain] Cd Length: 346 Bit Score: 503.27 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||
| argC | TIGR01850 | N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ... |
2-334 | 0e+00 | ||||||
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model 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. [Amino acid biosynthesis, Glutamate family] Pssm-ID: 273832 [Multi-domain] Cd Length: 346 Bit Score: 503.27 E-value: 0e+00
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| ArgC | COG0002 | N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ... |
2-333 | 2.60e-176 | ||||||
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; N-acetyl-gamma-glutamylphosphate reductase is part of the Pathway/BioSystem: Arginine biosynthesis Pssm-ID: 439773 [Multi-domain] Cd Length: 345 Bit Score: 491.89 E-value: 2.60e-176
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| AGPR_1_C | cd23934 | C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ... |
153-313 | 8.19e-80 | ||||||
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and similar proteins; N-acetyl-gamma-glutamyl-phosphate reductase (AGPR; EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the NADPH-dependent reduction of N-acetyl-gamma-glutamyl-phosphate phosphate, the third step of arginine biosynthesis. N-acetyl-gamma-glutamyl-phosphate phosphate, the product of the second step catalyzed by acetylglutamate kinase, undergoes reductive dephosphorylation to give N-acetylglutamic semialdehyde, which is converted to ornithine by acetylornithine aminotransferase and acetylornithine deacetylase. AGPR proteins contain an N-terminal Rossmann fold NAD(P)H-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. NADP(+) binds in a cleft between these domains and contacts both. There are two related families of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The model corresponds to type 1 AGPR family. Bacterial members of this family tend to be found within Arg biosynthesis operons. The type 1 AGPR family also includes LysY (LysW-L-2-aminoadipate/LysW-L-glutamate phosphate reductase), which is involved in both, the arginine and lysine, biosynthetic pathways. Pssm-ID: 467683 Cd Length: 171 Bit Score: 240.46 E-value: 8.19e-80
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| PLN02968 | PLN02968 | Probable N-acetyl-gamma-glutamyl-phosphate reductase |
6-333 | 9.34e-75 | ||||||
Probable N-acetyl-gamma-glutamyl-phosphate reductase Pssm-ID: 215522 [Multi-domain] Cd Length: 381 Bit Score: 235.11 E-value: 9.34e-75
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| Semialdhyde_dh | pfam01118 | Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ... |
6-146 | 1.92e-40 | ||||||
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: N-acetyl-glutamine semialdehyde dehydrogenase (AgrC) Aspartate-semialdehyde dehydrogenase Pssm-ID: 426059 [Multi-domain] Cd Length: 121 Bit Score: 138.04 E-value: 1.92e-40
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| Semialdhyde_dh | smart00859 | Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ... |
6-146 | 1.06e-34 | ||||||
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found in N-acetyl-glutamine semialdehyde dehydrogenase (AgrC), which is involved in arginine biosynthesis, and aspartate-semialdehyde dehydrogenase, an enzyme involved in the biosynthesis of various amino acids from aspartate. This family is also found in yeast and fungal Arg5,6 protein, which is cleaved into the enzymes N-acety-gamma-glutamyl-phosphate reductase and acetylglutamate kinase. These are also involved in arginine biosynthesis. All proteins in this entry contain a NAD binding region of semialdehyde dehydrogenase. Pssm-ID: 214863 [Multi-domain] Cd Length: 123 Bit Score: 123.04 E-value: 1.06e-34
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| Name | Accession | Description | Interval | E-value | ||||||
| argC | TIGR01850 | N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ... |
2-334 | 0e+00 | ||||||
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model 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. [Amino acid biosynthesis, Glutamate family] Pssm-ID: 273832 [Multi-domain] Cd Length: 346 Bit Score: 503.27 E-value: 0e+00
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| ArgC | COG0002 | N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ... |
2-333 | 2.60e-176 | ||||||
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; N-acetyl-gamma-glutamylphosphate reductase is part of the Pathway/BioSystem: Arginine biosynthesis Pssm-ID: 439773 [Multi-domain] Cd Length: 345 Bit Score: 491.89 E-value: 2.60e-176
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| AGPR_1_C | cd23934 | C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ... |
153-313 | 8.19e-80 | ||||||
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and similar proteins; N-acetyl-gamma-glutamyl-phosphate reductase (AGPR; EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the NADPH-dependent reduction of N-acetyl-gamma-glutamyl-phosphate phosphate, the third step of arginine biosynthesis. N-acetyl-gamma-glutamyl-phosphate phosphate, the product of the second step catalyzed by acetylglutamate kinase, undergoes reductive dephosphorylation to give N-acetylglutamic semialdehyde, which is converted to ornithine by acetylornithine aminotransferase and acetylornithine deacetylase. AGPR proteins contain an N-terminal Rossmann fold NAD(P)H-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. NADP(+) binds in a cleft between these domains and contacts both. There are two related families of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The model corresponds to type 1 AGPR family. Bacterial members of this family tend to be found within Arg biosynthesis operons. The type 1 AGPR family also includes LysY (LysW-L-2-aminoadipate/LysW-L-glutamate phosphate reductase), which is involved in both, the arginine and lysine, biosynthetic pathways. Pssm-ID: 467683 Cd Length: 171 Bit Score: 240.46 E-value: 8.19e-80
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| PLN02968 | PLN02968 | Probable N-acetyl-gamma-glutamyl-phosphate reductase |
6-333 | 9.34e-75 | ||||||
Probable N-acetyl-gamma-glutamyl-phosphate reductase Pssm-ID: 215522 [Multi-domain] Cd Length: 381 Bit Score: 235.11 E-value: 9.34e-75
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| AGPR_1_N | cd17895 | N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 ... |
6-152 | 3.17e-71 | ||||||
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and similar proteins; AGPR (EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the NADPH-dependent reduction of N-acetyl-gamma-glutamyl-phosphate phosphate; the third step of arginine biosynthesis. N-acetyl-gamma-glutamyl-phosphate phosphate, the product of the second step catalyzed by acetylglutamate kinase, undergoes reductive dephosphorylation to give N-acetylglutamic semialdehyde, which is converted to ornithine by acetylornithine aminotransferase and acetylornithine deacetylase. AGPR proteins contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. NADP(+) binds in a cleft between these domains and contacts both. There are two related families of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The model corresponds to type 1 AGPR family. Bacterial members of this family tend to be found within Arg biosynthesis operons. The type 1 AGPR family also includes LysY (LysW-L-2-aminoadipate/LysW-L-glutamate phosphate reductase), which is involved in both the arginine and lysine biosynthetic pathways. Pssm-ID: 467521 [Multi-domain] Cd Length: 170 Bit Score: 218.45 E-value: 3.17e-71
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| AGPR_C | cd18125 | C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and similar ... |
154-313 | 2.67e-43 | ||||||
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and similar proteins; N-acetyl-gamma-glutamyl-phosphate reductase (AGPR; EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, 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 (EC 2.7.2.8) domain and a C-terminal AGPR domain. There are two related families (type 1 and type 2) of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. This family also includes LysY (LysW-L-2-aminoadipate/LysW-L-glutamate phosphate reductase, EC 1.2.1.103/EC 1.2.1.106), which is involved in both the arginine and lysine biosynthetic pathways. Pssm-ID: 467675 Cd Length: 166 Bit Score: 146.88 E-value: 2.67e-43
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| Semialdhyde_dh | pfam01118 | Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ... |
6-146 | 1.92e-40 | ||||||
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: N-acetyl-glutamine semialdehyde dehydrogenase (AgrC) Aspartate-semialdehyde dehydrogenase Pssm-ID: 426059 [Multi-domain] Cd Length: 121 Bit Score: 138.04 E-value: 1.92e-40
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| AGPR_C_ARG5_6_like | cd23936 | C-terminal catalytic domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ... |
153-313 | 3.85e-37 | ||||||
C-terminal catalytic domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) and similar proteins; The family includes bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) from fungi, which contains a N-terminal acetylglutamate kinase ( EC 2.7.2.8, also known as N-acetyl-L-glutamate 5-phosphotransferase/NAG kinase/AGK) domain and a C-terminal N-acetyl-gamma-glutamyl-phosphate reductase (AGPR; EC 1.2.1.38, also known as AGPR/N-acetyl-glutamate semialdehyde dehydrogenase/NAGSA dehydrogenase) domain. This model corresponds to the AGPR C-terminal catalytic domain. AGPR 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. The budding yeast member, Arg5,6, is expressed as a precursor that is then maturated in the mitochondria into acetylglutamate kinase and acetylglutamyl-phosphate reductase. It is involved in the arginine biosynthesis pathway, catalyzing the second and third steps in the pathway. Pssm-ID: 467685 Cd Length: 161 Bit Score: 130.83 E-value: 3.85e-37
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| Semialdhyde_dh | smart00859 | Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ... |
6-146 | 1.06e-34 | ||||||
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found in N-acetyl-glutamine semialdehyde dehydrogenase (AgrC), which is involved in arginine biosynthesis, and aspartate-semialdehyde dehydrogenase, an enzyme involved in the biosynthesis of various amino acids from aspartate. This family is also found in yeast and fungal Arg5,6 protein, which is cleaved into the enzymes N-acety-gamma-glutamyl-phosphate reductase and acetylglutamate kinase. These are also involved in arginine biosynthesis. All proteins in this entry contain a NAD binding region of semialdehyde dehydrogenase. Pssm-ID: 214863 [Multi-domain] Cd Length: 123 Bit Score: 123.04 E-value: 1.06e-34
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| AGPR_1_C_LysY | cd23939 | C-terminal catalytic domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase ... |
153-313 | 1.21e-34 | ||||||
C-terminal catalytic domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase (LysY) and similar proteins; [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase (LysY; EC 1.2.1.103/EC 1.2.1.106) is involved in both, the arginine and lysine, biosynthetic pathways. LysY interacts with LysW. It may form a ternary complex with LysW and LysZ. 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. Pssm-ID: 467688 Cd Length: 174 Bit Score: 124.66 E-value: 1.21e-34
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| AGPR_1_N_LysY | cd24151 | N-terminal NAD(P)-binding domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate ... |
6-150 | 1.09e-32 | ||||||
N-terminal NAD(P)-binding domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase (LysY) and similar proteins; LysY (EC 1.2.1.103/EC 1.2.1.106) is involved in both the arginine and lysine biosynthetic pathways. LysY interacts with LysW. It may form a ternary complex with LysW and LysZ. 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. Members in this subfamily belong to the type 1 AGPR family. They contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain. Pssm-ID: 467527 [Multi-domain] Cd Length: 170 Bit Score: 119.30 E-value: 1.09e-32
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| AGPR_2_C | cd23935 | C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and ... |
153-313 | 2.54e-28 | ||||||
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and similar proteins; N-acetyl-gamma-glutamyl-phosphate reductase (AGPR; EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the NADPH-dependent reduction of N-acetyl-gamma-glutamyl-phosphate phosphate, the third step of arginine biosynthesis. N-acetyl-gamma-glutamyl-phosphate phosphate, the product of the second step catalyzed by acetylglutamate kinase, undergoes reductive dephosphorylation to give N-acetylglutamic semialdehyde, which is converted to ornithine by acetylornithine aminotransferase and acetylornithine deacetylase. AGPR proteins contain an N-terminal Rossmann fold NAD(P)H-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. NADP(+) binds in a cleft between these domains and contacts both. There are two related families of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The model corresponds to type 2 AGPR family. Pssm-ID: 467684 Cd Length: 178 Bit Score: 108.07 E-value: 2.54e-28
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| AGPR_1_actinobacAGPR_like | cd24148 | N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate ... |
6-152 | 1.36e-27 | ||||||
N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate reductase (actinobacAGPR) and similar proteins; AGPR (EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the third step in the biosynthesis of arginine from glutamate, the NADPH-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). There are two related families (type 1 and type 2) of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The family includes N-acetyl-gamma-glutamyl-phosphate reductases mainly from actinobacteria. They belong to the type 1 AGPR family. Members in this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain. Pssm-ID: 467524 [Multi-domain] Cd Length: 164 Bit Score: 105.83 E-value: 1.36e-27
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| Semialdhyde_dhC | pfam02774 | Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ... |
163-311 | 7.12e-24 | ||||||
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following members: N-acetyl-glutamine semialdehyde dehydrogenase (AgrC) Aspartate-semialdehyde dehydrogenase. Pssm-ID: 397067 [Multi-domain] Cd Length: 167 Bit Score: 95.84 E-value: 7.12e-24
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| AGPR_N | cd02280 | N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and ... |
6-152 | 1.93e-19 | ||||||
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and similar proteins; AGPR (EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the third step in the biosynthesis of arginine from glutamate, the NADPH-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 (EC 2.7.2.8) domain and a C-terminal AGPR domain. There are two related families (type 1 and type 2) of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. This family also includes LysY (LysW-L-2-aminoadipate/LysW-L-glutamate phosphate reductase, EC 1.2.1.103/EC 1.2.1.106), which is involved in both the arginine and lysine biosynthetic pathways. Members in this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain. Pssm-ID: 467515 [Multi-domain] Cd Length: 160 Bit Score: 83.77 E-value: 1.93e-19
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| AGPR_N_ARG5_6_like | cd24149 | N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ... |
6-153 | 1.74e-14 | ||||||
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) and similar proteins; The family includes bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) from fungi, which contains a N-terminal acetylglutamate kinase ( EC 2.7.2.8, also known as N-acetyl-L-glutamate 5-phosphotransferase/NAG kinase/AGK) domain and a C-terminal N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38, also known as AGPR/N-acetyl-glutamate semialdehyde dehydrogenase/NAGSA dehydrogenase) domain. The model corresponds to the AGPR N-terminal NAD(P)-binding domain. AGPR 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. The budding yeast member, Arg5,6, is expressed as a precursor that is then maturated in the mitochondria into acetylglutamate kinase and acetylglutamyl-phosphate reductase. It is involved in the arginine biosynthesis pathway, catalyzing the second and third steps in the pathway. Pssm-ID: 467525 [Multi-domain] Cd Length: 154 Bit Score: 69.83 E-value: 1.74e-14
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| Asd | COG0136 | Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ... |
6-323 | 2.34e-13 | ||||||
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; Aspartate-semialdehyde dehydrogenase is part of the Pathway/BioSystem: Lysine biosynthesis Pssm-ID: 439906 [Multi-domain] Cd Length: 333 Bit Score: 69.68 E-value: 2.34e-13
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| ASADH_AGPR_N | cd02281 | N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and ... |
6-152 | 1.74e-12 | ||||||
N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and N-acetyl-gamma-glutamyl-phosphate reductase (AGPR); Aspartate-beta-semialdehyde dehydrogenase (ASADH, EC 1.2.1.11), also called ASA dehydrogenase (ASD), or aspartate-beta-semialdehyde dehydrogenase, catalyzes the second step of the aspartate biosynthetic pathway, an essential enzyme found in bacteria, fungi, and higher plants. ASADH catalyses the formation of L-aspartate-beta-semialdehyde (ASA) by the reductive dephosphorylation of L-beta-aspartyl phosphate (BAP), utilizing the reducing power of NADPH. ASA can either be further reduced to homoserine, which leads to methionine, threonine, or isoleucine, or it can be condensed with pyruvate and cyclized into dihydrodipicolinate, and then converted into diaminopimelate, a component of bacterial cell walls, and finally decarboxylated to produce lysine. N-acetyl-gamma-glutamyl-phosphate reductase (AGPR, EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, reversibly catalyses the NADPH-dependent reduction of N-acetyl-gamma-glutamyl phosphate; the third step of arginine biosynthesis. ASADH and AGPR proteins contain an N-terminal Rossmann fold NAD(P)H binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain. Pssm-ID: 467516 [Multi-domain] Cd Length: 145 Bit Score: 63.92 E-value: 1.74e-12
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| ScASADH_like_N | cd02315 | N-terminal NAD(P)-binding domain of Saccharomyces cerevisiae aspartate beta-semialdehyde ... |
6-107 | 1.27e-09 | ||||||
N-terminal NAD(P)-binding domain of Saccharomyces cerevisiae aspartate beta-semialdehyde dehydrogenase (ASADH) and similar proteins; The family corresponds to a new branch of ASADH enzymes that has a similar overall fold and domain organization but sharing very little sequence homology with the typical bacterial ASADHs. They are mainly from archaea and fungi. ASADH (EC 1.2.1.11), also called ASA dehydrogenase (ASD), or aspartate-beta-semialdehyde dehydrogenase, catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate, which is the second step of the aspartate biosynthetic pathway. ASA can either be further reduced to homoserine, which leads to methionine, threonine, or isoleucine, or it can be condensed with pyruvate and cyclized into dihydrodipicolinate, and then converted into diaminopimelate, a component of bacterial cell walls, and finally decarboxylated to produce lysine. ASADH contains an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain. Family also includes NADP-dependent malonyl-CoA reductase (MCR, EC 1.2.1.75), which catalyzes the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles. It can also use succinyl-CoA and succinate semialdehyde as substrates but at a lower rate than malonyl-CoA. Pssm-ID: 467518 Cd Length: 162 Bit Score: 56.35 E-value: 1.27e-09
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| PRK08664 | PRK08664 | aspartate-semialdehyde dehydrogenase; Reviewed |
1-190 | 3.17e-09 | ||||||
aspartate-semialdehyde dehydrogenase; Reviewed Pssm-ID: 236329 [Multi-domain] Cd Length: 349 Bit Score: 57.53 E-value: 3.17e-09
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| ASADH_USG1_N | cd17894 | N-terminal NAD(P)-binding domain of USG-1 protein and similar proteins; The family includes ... |
6-112 | 3.91e-09 | ||||||
N-terminal NAD(P)-binding domain of USG-1 protein and similar proteins; The family includes Escherichia coli USG-1 protein, Pseudomonas aeruginosa USG-1 homolog proteins and similar proteins. Although their biological function remains unknown, they are homologs to aspartate beta-semialdehyde dehydrogenase (ASADH) which contains an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain. However, USG-1 proteins lack the conserved active site residues of the ASADH protein C-terminal domain. Pssm-ID: 467520 [Multi-domain] Cd Length: 144 Bit Score: 54.55 E-value: 3.91e-09
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| PRK14874 | PRK14874 | aspartate-semialdehyde dehydrogenase; Provisional |
1-321 | 7.23e-09 | ||||||
aspartate-semialdehyde dehydrogenase; Provisional Pssm-ID: 237845 [Multi-domain] Cd Length: 334 Bit Score: 56.32 E-value: 7.23e-09
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| GAPDH_like_C | cd18122 | C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
154-309 | 8.03e-09 | ||||||
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) superfamily of proteins; GAPDH-like C-terminal catalytic domains are typically associated with a classic N-terminal Rossmann fold NAD(P)-binding domain. This superfamily includes the C-terminal domains of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), aspartate beta-semialdehyde dehydrogenase (ASADH), acetaldehyde dehydrogenase (ALDH) and USG-1 homolog proteins. Pssm-ID: 467672 [Multi-domain] Cd Length: 166 Bit Score: 54.06 E-value: 8.03e-09
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| VcASADH2_like_N | cd02316 | N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase ... |
6-110 | 6.01e-08 | ||||||
N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase 2 (ASADH2) and similar proteins; The family corresponds to a new branch of bacterial ASADH enzymes that has a similar overall fold and domain organization but sharing less sequence homology with the other bacterial ASADHs. The second isoform of ASADH in Vibrio cholerae is one of the prototypes of this family. It also includes ASADHs from Streptococcus pneumoniae, Mycobacterium tuberculosis, Thermus thermophilus, as well as from eukaryotes. ASADH (EC 1.2.1.11), also called ASA dehydrogenase (ASD), or aspartate-beta-semialdehyde dehydrogenase, catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate, which is the second step of the aspartate biosynthetic pathway. ASA can either be further reduced to homoserine, which leads to methionine, threonine, or isoleucine, or it can be condensed with pyruvate and cyclized into dihydrodipicolinate, and then converted into diaminopimelate, a component of bacterial cell walls, and finally decarboxylated to produce lysine. ASADH contains an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain. Pssm-ID: 467519 [Multi-domain] Cd Length: 142 Bit Score: 50.90 E-value: 6.01e-08
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| ASADH_N_like | cd24147 | N-terminal NAD(P)-binding domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ... |
2-112 | 6.22e-08 | ||||||
N-terminal NAD(P)-binding domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 protein and similar proteins; The family includes aspartate beta-semialdehyde dehydrogenase (ASADH), NADP-dependent malonyl-CoA reductase (MCR), and USG-1 protein. They contain an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain and are members of the GAPDH superfamily of proteins. ASADH (EC 1.2.1.11), also called ASA dehydrogenase (ASD), or aspartate-beta-semialdehyde dehydrogenase, catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate, which is the second step of the aspartate biosynthetic pathway. ASA can either be further reduced to homoserine, which leads to methionine, threonine, or isoleucine, or it can be condensed with pyruvate and cyclized into dihydrodipicolinate, and then converted into diaminopimelate, a component of bacterial cell walls, and finally decarboxylated to produce lysine. NADP-dependent MCR (EC 1.2.1.75) is mainly found in Archaea. It catalyzes the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles. It can also use succinyl-CoA and succinate semialdehyde as substrates but at a lower rate than malonyl-CoA. Sequence comparison suggests that the archaeal MCR gene (mcr) has evolved from the duplication of a common ancestral ASADH gene (asd). The biological function of USG-1 protein and homologs remains unclear. They are homologs to ASADH but lack the conserved active site residues of the ASADH protein C-terminal catalytic domain. Pssm-ID: 467523 [Multi-domain] Cd Length: 142 Bit Score: 51.18 E-value: 6.22e-08
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| PRK05671 | PRK05671 | aspartate-semialdehyde dehydrogenase; Reviewed |
2-193 | 1.06e-07 | ||||||
aspartate-semialdehyde dehydrogenase; Reviewed Pssm-ID: 168165 [Multi-domain] Cd Length: 336 Bit Score: 52.81 E-value: 1.06e-07
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| PRK06728 | PRK06728 | aspartate-semialdehyde dehydrogenase; Provisional |
6-321 | 1.66e-06 | ||||||
aspartate-semialdehyde dehydrogenase; Provisional Pssm-ID: 136022 [Multi-domain] Cd Length: 347 Bit Score: 49.28 E-value: 1.66e-06
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| PLN02383 | PLN02383 | aspartate semialdehyde dehydrogenase |
6-110 | 1.15e-03 | ||||||
aspartate semialdehyde dehydrogenase Pssm-ID: 178009 [Multi-domain] Cd Length: 344 Bit Score: 40.14 E-value: 1.15e-03
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| DHDPR_N | cd02274 | N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ... |
6-96 | 2.18e-03 | ||||||
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; DHDPR (EC 1.17.1.8), also called 4-hydroxy-tetrahydrodipicolinate reductase, or HTPA reductase, is a product of an essential gene referred to as dapB. It catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). DHDPR could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. DHDPR is a component of the biosynthetic pathway that generates meso-diaminopimelate, a component of bacterial cell walls, and the amino acid L-lysine in various bacteria, archaea, cyanobacteria and higher plants. The enzyme is a homotetramer where each monomer is composed of two domains, an N-terminal NAD(P)-binding domain which forms a Rossmann fold, and a C-terminal substrate-binding domain that forms an open, mixed alpha-beta sandwich. Pssm-ID: 467611 [Multi-domain] Cd Length: 139 Bit Score: 37.92 E-value: 2.18e-03
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