aspartate dehydrogenase domain-containing protein isoform 2 [Homo sapiens]
L-aspartate dehydrogenase family protein( domain architecture ID 10395547)
L-aspartate dehydrogenase family protein catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate
List of domain hits
Name | Accession | Description | Interval | E-value | |||
Asp_DH_C | pfam01958 | Aspartate dehydrogenase, C-terminal; This entry represents the C-terminal domain of aspartate ... |
68-156 | 3.04e-21 | |||
Aspartate dehydrogenase, C-terminal; This entry represents the C-terminal domain of aspartate dehydrogenases that belong to a unique class of amino acid dehydrogenases. The structure of Thermotoga maritima TM1643 has been found to contain an N-terminal Rossmann fold domain (which binds the NAD(P)+ cofactor) and a C-terminal alpha/beta domain. Enzymatic characterization of TM1643 revealed that it possesses NAD or NADP-dependent dehydrogenase activity toward L-aspartate but no aspartate oxidase activity. Members of this group share some structural similarity to several other NAD(P)+-dependent oxidoreductases, including inositol 1-phosphate synthase, dihydrodipicolinate reductase, and ASA-DH. It has been proposed that in Thermotoga maritima, TM1643 catalyzes the first reaction of de novo biosynthesis of NAD from aspartate, and it produces iminoaspartate required for this pathway. : Pssm-ID: 426531 [Multi-domain] Cd Length: 87 Bit Score: 82.54 E-value: 3.04e-21
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NADB_Rossmann super family | cl21454 | Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ... |
12-35 | 2.25e-03 | |||
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction. The actual alignment was detected with superfamily member pfam03447: Pssm-ID: 473865 [Multi-domain] Cd Length: 116 Bit Score: 36.13 E-value: 2.25e-03
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Name | Accession | Description | Interval | E-value | |||
Asp_DH_C | pfam01958 | Aspartate dehydrogenase, C-terminal; This entry represents the C-terminal domain of aspartate ... |
68-156 | 3.04e-21 | |||
Aspartate dehydrogenase, C-terminal; This entry represents the C-terminal domain of aspartate dehydrogenases that belong to a unique class of amino acid dehydrogenases. The structure of Thermotoga maritima TM1643 has been found to contain an N-terminal Rossmann fold domain (which binds the NAD(P)+ cofactor) and a C-terminal alpha/beta domain. Enzymatic characterization of TM1643 revealed that it possesses NAD or NADP-dependent dehydrogenase activity toward L-aspartate but no aspartate oxidase activity. Members of this group share some structural similarity to several other NAD(P)+-dependent oxidoreductases, including inositol 1-phosphate synthase, dihydrodipicolinate reductase, and ASA-DH. It has been proposed that in Thermotoga maritima, TM1643 catalyzes the first reaction of de novo biosynthesis of NAD from aspartate, and it produces iminoaspartate required for this pathway. Pssm-ID: 426531 [Multi-domain] Cd Length: 87 Bit Score: 82.54 E-value: 3.04e-21
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NAD_binding_3 | pfam03447 | Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ... |
12-35 | 2.25e-03 | |||
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. The C-terminal domain of homoserine dehydrogenase contributes a single helix to this structural domain, which is not included in the Pfam model. Pssm-ID: 281446 [Multi-domain] Cd Length: 116 Bit Score: 36.13 E-value: 2.25e-03
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AspD | COG1712 | L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism]; |
10-35 | 9.56e-03 | |||
L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism]; Pssm-ID: 441318 [Multi-domain] Cd Length: 263 Bit Score: 35.55 E-value: 9.56e-03
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Name | Accession | Description | Interval | E-value | |||
Asp_DH_C | pfam01958 | Aspartate dehydrogenase, C-terminal; This entry represents the C-terminal domain of aspartate ... |
68-156 | 3.04e-21 | |||
Aspartate dehydrogenase, C-terminal; This entry represents the C-terminal domain of aspartate dehydrogenases that belong to a unique class of amino acid dehydrogenases. The structure of Thermotoga maritima TM1643 has been found to contain an N-terminal Rossmann fold domain (which binds the NAD(P)+ cofactor) and a C-terminal alpha/beta domain. Enzymatic characterization of TM1643 revealed that it possesses NAD or NADP-dependent dehydrogenase activity toward L-aspartate but no aspartate oxidase activity. Members of this group share some structural similarity to several other NAD(P)+-dependent oxidoreductases, including inositol 1-phosphate synthase, dihydrodipicolinate reductase, and ASA-DH. It has been proposed that in Thermotoga maritima, TM1643 catalyzes the first reaction of de novo biosynthesis of NAD from aspartate, and it produces iminoaspartate required for this pathway. Pssm-ID: 426531 [Multi-domain] Cd Length: 87 Bit Score: 82.54 E-value: 3.04e-21
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NAD_binding_3 | pfam03447 | Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ... |
12-35 | 2.25e-03 | |||
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. The C-terminal domain of homoserine dehydrogenase contributes a single helix to this structural domain, which is not included in the Pfam model. Pssm-ID: 281446 [Multi-domain] Cd Length: 116 Bit Score: 36.13 E-value: 2.25e-03
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AspD | COG1712 | L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism]; |
10-35 | 9.56e-03 | |||
L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism]; Pssm-ID: 441318 [Multi-domain] Cd Length: 263 Bit Score: 35.55 E-value: 9.56e-03
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Blast search parameters | ||||
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