aspartate dehydrogenase specifically catalyzes the NAD(P)-dependent dehydrogenation of L-aspartate to iminoaspartate, which decomposes to oxaloacetate and ammonia in solution, in the first step of NAD biosynthesis from aspartate
Aspartate dehydrogenase, C-terminal; This entry represents the C-terminal domain of aspartate ...
165-251
8.18e-41
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: 135.70 E-value: 8.18e-41
Aspartate dehydrogenase, C-terminal; This entry represents the C-terminal domain of aspartate ...
165-251
8.18e-41
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: 135.70 E-value: 8.18e-41
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ...
8-116
7.55e-08
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: 49.61 E-value: 7.55e-08
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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