N-acetyl-gamma-glutamyl-phosphate reductase [Paracidovorax citrulli]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| argC_other super family | cl36993 | N-acetyl-gamma-glutamyl-phosphate reductase, uncommon form; This model represents the less ... |
3-310 | 1.50e-137 | |||||
N-acetyl-gamma-glutamyl-phosphate reductase, uncommon form; This model 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. [Amino acid biosynthesis, Glutamate family] The actual alignment was detected with superfamily member TIGR01851: Pssm-ID: 273833 [Multi-domain] Cd Length: 310 Bit Score: 391.51 E-value: 1.50e-137
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| Name | Accession | Description | Interval | E-value | ||||||
| argC_other | TIGR01851 | N-acetyl-gamma-glutamyl-phosphate reductase, uncommon form; This model represents the less ... |
3-310 | 1.50e-137 | ||||||
N-acetyl-gamma-glutamyl-phosphate reductase, uncommon form; This model 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. [Amino acid biosynthesis, Glutamate family] Pssm-ID: 273833 [Multi-domain] Cd Length: 310 Bit Score: 391.51 E-value: 1.50e-137
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| PLN02968 | PLN02968 | Probable N-acetyl-gamma-glutamyl-phosphate reductase |
1-310 | 1.13e-91 | ||||||
Probable N-acetyl-gamma-glutamyl-phosphate reductase Pssm-ID: 215522 [Multi-domain] Cd Length: 381 Bit Score: 277.48 E-value: 1.13e-91
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| AGPR_2_C | cd23935 | C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and ... |
120-296 | 1.90e-91 | ||||||
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: 269.47 E-value: 1.90e-91
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| ArgC | COG0002 | N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ... |
25-310 | 2.89e-45 | ||||||
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: 156.77 E-value: 2.89e-45
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| Semialdhyde_dh | smart00859 | Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ... |
3-113 | 1.92e-16 | ||||||
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: 74.12 E-value: 1.92e-16
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| Semialdhyde_dh | pfam01118 | Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ... |
11-113 | 6.00e-06 | ||||||
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: 44.82 E-value: 6.00e-06
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| Name | Accession | Description | Interval | E-value | ||||||
| argC_other | TIGR01851 | N-acetyl-gamma-glutamyl-phosphate reductase, uncommon form; This model represents the less ... |
3-310 | 1.50e-137 | ||||||
N-acetyl-gamma-glutamyl-phosphate reductase, uncommon form; This model 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. [Amino acid biosynthesis, Glutamate family] Pssm-ID: 273833 [Multi-domain] Cd Length: 310 Bit Score: 391.51 E-value: 1.50e-137
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| PLN02968 | PLN02968 | Probable N-acetyl-gamma-glutamyl-phosphate reductase |
1-310 | 1.13e-91 | ||||||
Probable N-acetyl-gamma-glutamyl-phosphate reductase Pssm-ID: 215522 [Multi-domain] Cd Length: 381 Bit Score: 277.48 E-value: 1.13e-91
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| AGPR_2_C | cd23935 | C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and ... |
120-296 | 1.90e-91 | ||||||
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: 269.47 E-value: 1.90e-91
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| AGPR_2_N | cd17896 | N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 ... |
2-126 | 9.10e-59 | ||||||
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 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 2 AGPR family. Pssm-ID: 467522 [Multi-domain] Cd Length: 132 Bit Score: 184.73 E-value: 9.10e-59
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| ArgC | COG0002 | N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ... |
25-310 | 2.89e-45 | ||||||
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: 156.77 E-value: 2.89e-45
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| argC | TIGR01850 | N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ... |
3-310 | 1.12e-41 | ||||||
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: 147.34 E-value: 1.12e-41
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| AGPR_C | cd18125 | C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and similar ... |
121-296 | 7.21e-37 | ||||||
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: 129.54 E-value: 7.21e-37
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| AGPR_1_C | cd23934 | C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ... |
120-296 | 1.79e-20 | ||||||
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: 86.38 E-value: 1.79e-20
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| Semialdhyde_dh | smart00859 | Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ... |
3-113 | 1.92e-16 | ||||||
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: 74.12 E-value: 1.92e-16
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| AGPR_N | cd02280 | N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and ... |
3-119 | 6.11e-13 | ||||||
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: 65.67 E-value: 6.11e-13
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| AGPR_C_ARG5_6_like | cd23936 | C-terminal catalytic domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ... |
120-296 | 5.95e-11 | ||||||
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: 59.95 E-value: 5.95e-11
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| AGPR_1_C_LysY | cd23939 | C-terminal catalytic domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase ... |
120-296 | 8.46e-11 | ||||||
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: 59.94 E-value: 8.46e-11
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| AGPR_N_ARG5_6_like | cd24149 | N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ... |
19-120 | 1.87e-10 | ||||||
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: 58.28 E-value: 1.87e-10
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| Semialdhyde_dh | pfam01118 | Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ... |
11-113 | 6.00e-06 | ||||||
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: 44.82 E-value: 6.00e-06
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| AGPR_1_actinobacAGPR_like | cd24148 | N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate ... |
48-119 | 2.36e-05 | ||||||
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: 43.82 E-value: 2.36e-05
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| AGPR_1_N | cd17895 | N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 ... |
291-310 | 3.67e-03 | ||||||
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: 37.41 E-value: 3.67e-03
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