aspartate-semialdehyde dehydrogenase [Corynebacterium striatum]
Protein Classification
aspartate-semialdehyde dehydrogenase( domain architecture ID 11487465)
aspartate-semialdehyde dehydrogenase catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| PRK14874 | PRK14874 | aspartate-semialdehyde dehydrogenase; Provisional |
1-345 | 0e+00 | ||||||
aspartate-semialdehyde dehydrogenase; Provisional : Pssm-ID: 237845 [Multi-domain] Cd Length: 334 Bit Score: 543.98 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||
| PRK14874 | PRK14874 | aspartate-semialdehyde dehydrogenase; Provisional |
1-345 | 0e+00 | ||||||
aspartate-semialdehyde dehydrogenase; Provisional Pssm-ID: 237845 [Multi-domain] Cd Length: 334 Bit Score: 543.98 E-value: 0e+00
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| Asd | COG0136 | Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ... |
3-345 | 5.02e-179 | ||||||
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: 498.79 E-value: 5.02e-179
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| asd_B | TIGR01296 | aspartate-semialdehyde dehydrogenase (peptidoglycan organisms); Two closely related families ... |
4-345 | 1.15e-151 | ||||||
aspartate-semialdehyde dehydrogenase (peptidoglycan organisms); Two closely related families of aspartate-semialdehyde dehydrogenase are found. They differ by a deep split in phylogenetic and percent identity trees and in gap patterns. This model represents a branch more closely related to the USG-1 protein than to the other aspartate-semialdehyde dehydrogenases represented in model TIGR00978. [Amino acid biosynthesis, Aspartate family] Pssm-ID: 273543 [Multi-domain] Cd Length: 338 Bit Score: 430.00 E-value: 1.15e-151
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| ASADH_C_bac_euk_like | cd18131 | C-terminal catalytic domain of bacterial/eukaryotic aspartate beta-semialdehyde dehydrogenase ... |
131-329 | 5.98e-77 | ||||||
C-terminal catalytic domain of bacterial/eukaryotic aspartate beta-semialdehyde dehydrogenase (ASADH) and similar proteins; The family corresponds to a new branch of bacterial aspartate beta-semialdehyde dehydrogenase (ASADH) enzymes that has a similar overall fold and domain organization but share 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 and are members of the GAPDH superfamily of proteins. Pssm-ID: 467681 Cd Length: 188 Bit Score: 234.33 E-value: 5.98e-77
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| Semialdhyde_dhC | pfam02774 | Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ... |
140-331 | 8.61e-47 | ||||||
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: 156.32 E-value: 8.61e-47
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| Semialdhyde_dh | smart00859 | Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ... |
3-120 | 1.53e-29 | ||||||
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: 109.95 E-value: 1.53e-29
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| Name | Accession | Description | Interval | E-value | ||||||
| PRK14874 | PRK14874 | aspartate-semialdehyde dehydrogenase; Provisional |
1-345 | 0e+00 | ||||||
aspartate-semialdehyde dehydrogenase; Provisional Pssm-ID: 237845 [Multi-domain] Cd Length: 334 Bit Score: 543.98 E-value: 0e+00
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| Asd | COG0136 | Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ... |
3-345 | 5.02e-179 | ||||||
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: 498.79 E-value: 5.02e-179
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| asd_B | TIGR01296 | aspartate-semialdehyde dehydrogenase (peptidoglycan organisms); Two closely related families ... |
4-345 | 1.15e-151 | ||||||
aspartate-semialdehyde dehydrogenase (peptidoglycan organisms); Two closely related families of aspartate-semialdehyde dehydrogenase are found. They differ by a deep split in phylogenetic and percent identity trees and in gap patterns. This model represents a branch more closely related to the USG-1 protein than to the other aspartate-semialdehyde dehydrogenases represented in model TIGR00978. [Amino acid biosynthesis, Aspartate family] Pssm-ID: 273543 [Multi-domain] Cd Length: 338 Bit Score: 430.00 E-value: 1.15e-151
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| PLN02383 | PLN02383 | aspartate semialdehyde dehydrogenase |
3-345 | 1.43e-114 | ||||||
aspartate semialdehyde dehydrogenase Pssm-ID: 178009 [Multi-domain] Cd Length: 344 Bit Score: 335.97 E-value: 1.43e-114
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| ASADH_C_bac_euk_like | cd18131 | C-terminal catalytic domain of bacterial/eukaryotic aspartate beta-semialdehyde dehydrogenase ... |
131-329 | 5.98e-77 | ||||||
C-terminal catalytic domain of bacterial/eukaryotic aspartate beta-semialdehyde dehydrogenase (ASADH) and similar proteins; The family corresponds to a new branch of bacterial aspartate beta-semialdehyde dehydrogenase (ASADH) enzymes that has a similar overall fold and domain organization but share 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 and are members of the GAPDH superfamily of proteins. Pssm-ID: 467681 Cd Length: 188 Bit Score: 234.33 E-value: 5.98e-77
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| PRK06728 | PRK06728 | aspartate-semialdehyde dehydrogenase; Provisional |
4-345 | 9.31e-75 | ||||||
aspartate-semialdehyde dehydrogenase; Provisional Pssm-ID: 136022 [Multi-domain] Cd Length: 347 Bit Score: 234.56 E-value: 9.31e-75
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| VcASADH2_like_N | cd02316 | N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase ... |
3-130 | 1.53e-66 | ||||||
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: 206.13 E-value: 1.53e-66
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| PRK05671 | PRK05671 | aspartate-semialdehyde dehydrogenase; Reviewed |
4-345 | 5.23e-61 | ||||||
aspartate-semialdehyde dehydrogenase; Reviewed Pssm-ID: 168165 [Multi-domain] Cd Length: 336 Bit Score: 198.41 E-value: 5.23e-61
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| PRK08040 | PRK08040 | putative semialdehyde dehydrogenase; Provisional |
4-345 | 2.90e-55 | ||||||
putative semialdehyde dehydrogenase; Provisional Pssm-ID: 181205 [Multi-domain] Cd Length: 336 Bit Score: 183.74 E-value: 2.90e-55
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| PRK08664 | PRK08664 | aspartate-semialdehyde dehydrogenase; Reviewed |
1-345 | 3.58e-52 | ||||||
aspartate-semialdehyde dehydrogenase; Reviewed Pssm-ID: 236329 [Multi-domain] Cd Length: 349 Bit Score: 175.78 E-value: 3.58e-52
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| Semialdhyde_dhC | pfam02774 | Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ... |
140-331 | 8.61e-47 | ||||||
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: 156.32 E-value: 8.61e-47
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| asd_EA | TIGR00978 | aspartate-semialdehyde dehydrogenase (non-peptidoglycan organisms); Two closely related ... |
4-344 | 1.35e-46 | ||||||
aspartate-semialdehyde dehydrogenase (non-peptidoglycan organisms); Two closely related families of aspartate-semialdehyde dehydrogenase are found. They differ by a deep split in phylogenetic and percent identity trees and in gap patterns. Separate models are built for the two types in order to exclude the USG-1 protein, found in several species, which is specifically related to the Bacillus subtilis type of aspartate-semialdehyde dehydrogenase. Members of this type are found primarily in organisms that lack peptidoglycan. [Amino acid biosynthesis, Aspartate family] Pssm-ID: 273376 [Multi-domain] Cd Length: 341 Bit Score: 161.08 E-value: 1.35e-46
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| ASADH_C_USG1_like | cd18129 | C-terminal domain of USG-1 protein and similar proteins; The family includes Escherichia coli ... |
133-329 | 1.15e-43 | ||||||
C-terminal 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 its biological function remains unknown, it is found to be homologous 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: 467679 Cd Length: 186 Bit Score: 148.88 E-value: 1.15e-43
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| Semialdhyde_dh | pfam01118 | Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ... |
3-120 | 1.06e-36 | ||||||
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: 128.41 E-value: 1.06e-36
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| ASADH_N_like | cd24147 | N-terminal NAD(P)-binding domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ... |
3-139 | 2.92e-35 | ||||||
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: 125.53 E-value: 2.92e-35
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| ASADH_USG1_N | cd17894 | N-terminal NAD(P)-binding domain of USG-1 protein and similar proteins; The family includes ... |
3-130 | 2.08e-33 | ||||||
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: 120.80 E-value: 2.08e-33
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| Semialdhyde_dh | smart00859 | Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ... |
3-120 | 1.53e-29 | ||||||
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: 109.95 E-value: 1.53e-29
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| ASADH_AGPR_N | cd02281 | N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and ... |
2-143 | 2.15e-27 | ||||||
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: 104.75 E-value: 2.15e-27
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| ASADH_C_arch_fung_like | cd18130 | C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase ... |
131-329 | 1.74e-26 | ||||||
C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase (ASADH) and similar proteins; The family corresponds to a new branch of aspartate beta-semialdehyde dehydrogenase (ASADH) enzymes that has a similar overall fold and domain organization but share 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 and are members of the GAPDH superfamily of proteins. This 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: 467680 [Multi-domain] Cd Length: 180 Bit Score: 103.47 E-value: 1.74e-26
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| ASADH_C_like | cd18124 | C-terminal catalytic domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ... |
131-329 | 3.65e-24 | ||||||
C-terminal catalytic 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. These proteins 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: 467674 [Multi-domain] Cd Length: 193 Bit Score: 97.66 E-value: 3.65e-24
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| ASADH_C | cd18128 | C-terminal catalytic domain of aspartate beta-semialdehyde dehydrogenase (ASADH) and similar ... |
131-329 | 3.22e-22 | ||||||
C-terminal catalytic domain of aspartate beta-semialdehyde dehydrogenase (ASADH) and similar proteins; Aspartate beta-semialdehyde dehydrogenase (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 and are members of the GAPDH superfamily of proteins. Pssm-ID: 467678 [Multi-domain] Cd Length: 165 Bit Score: 91.80 E-value: 3.22e-22
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| ScASADH_like_N | cd02315 | N-terminal NAD(P)-binding domain of Saccharomyces cerevisiae aspartate beta-semialdehyde ... |
4-136 | 4.63e-15 | ||||||
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: 71.75 E-value: 4.63e-15
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| ASADH_C_bac_like | cd23938 | C-terminal catalytic domain of bacterial aspartate beta-semialdehyde dehydrogenase (ASADH) and ... |
154-309 | 1.28e-13 | ||||||
C-terminal catalytic domain of bacterial aspartate beta-semialdehyde dehydrogenase (ASADH) and similar proteins; The family corresponds to a branch of bacterial aspartate beta-semialdehyde dehydrogenase (ASADH) enzymes mainly found in proteobacteria, such as Escherichia coli, Haemophilus influenzae, Pseudomonas aeruginosa and Vibrio cholerae. These proteins have similar overall folds and domain organizations but share less sequence homology with fungal and archaeal ASADHs. 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 and are members of the GAPDH superfamily of proteins. Pssm-ID: 467687 Cd Length: 217 Bit Score: 68.87 E-value: 1.28e-13
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| PRK06598 | PRK06598 | aspartate-semialdehyde dehydrogenase; Reviewed |
154-334 | 2.39e-11 | ||||||
aspartate-semialdehyde dehydrogenase; Reviewed Pssm-ID: 235839 Cd Length: 369 Bit Score: 64.08 E-value: 2.39e-11
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| argC | TIGR01850 | N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ... |
3-339 | 3.62e-11 | ||||||
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: 63.37 E-value: 3.62e-11
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| ArgC | COG0002 | N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ... |
3-334 | 1.13e-08 | ||||||
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: 55.85 E-value: 1.13e-08
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| GAPDH_like_C | cd18122 | C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
131-329 | 1.23e-08 | ||||||
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: 53.68 E-value: 1.23e-08
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| AGPR_1_N | cd17895 | N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 ... |
4-130 | 7.60e-06 | ||||||
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: 45.50 E-value: 7.60e-06
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| SDR_a5 | cd05243 | atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ... |
3-84 | 1.57e-05 | ||||||
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Pssm-ID: 187554 [Multi-domain] Cd Length: 203 Bit Score: 45.30 E-value: 1.57e-05
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| ASADH_MCR_N | cd24150 | N-terminal NAD(P)-binding domain of archaeal NADP-dependent malonyl-CoA reductase (MCR) and ... |
5-115 | 2.78e-05 | ||||||
N-terminal NAD(P)-binding domain of archaeal NADP-dependent malonyl-CoA reductase (MCR) and similar proteins; Archaeal NADP-dependent MCR (EC 1.2.1.75) 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 malonyl-CoA reductase gene (mcr) has evolved from the duplication of a common ancestral aspartate beta-semialdehyde dehydrogenase (ASADH) gene (asd). MCR contains an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain. Pssm-ID: 467526 Cd Length: 163 Bit Score: 43.86 E-value: 2.78e-05
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| AGPR_C_ARG5_6_like | cd23936 | C-terminal catalytic domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ... |
254-333 | 2.97e-05 | ||||||
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: 43.78 E-value: 2.97e-05
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| NmrA_TMR_like_1_SDR_a | cd05231 | NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, ... |
4-97 | 5.47e-05 | ||||||
NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, subgroup 1, atypical (a) SDRs; Atypical SDRs related to NMRa, TMR, and HSCARG (an NADPH sensor). This subgroup resembles the SDRs and has a partially conserved characteristic [ST]GXXGXXG NAD-binding motif, but lacks the conserved active site residues. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Atypical SDRs are distinct from classical SDRs. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Pssm-ID: 187542 [Multi-domain] Cd Length: 259 Bit Score: 44.24 E-value: 5.47e-05
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| GAPDH_II_C | cd18127 | C-terminal catalytic domain of type II glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
241-311 | 3.26e-04 | ||||||
C-terminal catalytic domain of type II glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). The family corresponds to type II NADP+ utilizing GAPDHs, mainly from archaea. Pssm-ID: 467677 Cd Length: 162 Bit Score: 40.65 E-value: 3.26e-04
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| YbjT | COG0702 | Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ... |
3-95 | 7.26e-04 | ||||||
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only]; Pssm-ID: 440466 [Multi-domain] Cd Length: 215 Bit Score: 40.21 E-value: 7.26e-04
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| SDR_a3 | cd05229 | atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a ... |
3-95 | 1.96e-03 | ||||||
atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a glycine-rich NAD(P)-binding motif consensus that is very similar to the extended SDRs, GXXGXXG. Generally, this group has poor conservation of the active site tetrad, However, individual sequences do contain matches to the YXXXK active site motif, and generally Tyr or Asn in place of the upstream Ser found in most SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Pssm-ID: 187540 [Multi-domain] Cd Length: 302 Bit Score: 39.62 E-value: 1.96e-03
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| AGPR_1_C | cd23934 | C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ... |
241-333 | 4.39e-03 | ||||||
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: 37.46 E-value: 4.39e-03
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| PRK08289 | PRK08289 | glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
91-154 | 6.94e-03 | ||||||
glyceraldehyde-3-phosphate dehydrogenase; Reviewed Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 37.98 E-value: 6.94e-03
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