4-hydroxy-tetrahydrodipicolinate reductase catalyzes the NAD(P)-dependent conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate in amino acid biosynthesis pathways
4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; ...
4-265
3.33e-99
4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; 4-hydroxy-tetrahydrodipicolinate reductase is part of the Pathway/BioSystem: Lysine biosynthesis
:
Pssm-ID: 440058 [Multi-domain] Cd Length: 257 Bit Score: 290.48 E-value: 3.33e-99
4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; ...
4-265
3.33e-99
4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; 4-hydroxy-tetrahydrodipicolinate reductase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 440058 [Multi-domain] Cd Length: 257 Bit Score: 290.48 E-value: 3.33e-99
Dihydrodipicolinate reductase, C-terminus; Dihydrodipicolinate reductase (DapB) reduces the ...
137-265
3.37e-43
Dihydrodipicolinate reductase, C-terminus; Dihydrodipicolinate reductase (DapB) reduces the alpha,beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso-diaminopimelate, which are critical for both protein and cell wall biosynthesis. The C-terminal domain of DapB has been proposed to be the substrate- binding domain.
Pssm-ID: 461568 Cd Length: 122 Bit Score: 143.03 E-value: 3.37e-43
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ...
4-138
2.07e-38
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: 131.14 E-value: 2.07e-38
4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; ...
4-265
3.33e-99
4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; 4-hydroxy-tetrahydrodipicolinate reductase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 440058 [Multi-domain] Cd Length: 257 Bit Score: 290.48 E-value: 3.33e-99
Dihydrodipicolinate reductase, C-terminus; Dihydrodipicolinate reductase (DapB) reduces the ...
137-265
3.37e-43
Dihydrodipicolinate reductase, C-terminus; Dihydrodipicolinate reductase (DapB) reduces the alpha,beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso-diaminopimelate, which are critical for both protein and cell wall biosynthesis. The C-terminal domain of DapB has been proposed to be the substrate- binding domain.
Pssm-ID: 461568 Cd Length: 122 Bit Score: 143.03 E-value: 3.37e-43
Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the ...
4-128
1.28e-38
Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the alpha,beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso-diaminopimelate, which are critical for both protein and cell wall biosynthesis. The N-terminal domain of DapB binds the dinucleotide NADPH.
Pssm-ID: 460069 [Multi-domain] Cd Length: 121 Bit Score: 131.20 E-value: 1.28e-38
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ...
4-138
2.07e-38
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: 131.14 E-value: 2.07e-38
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
4-110
3.83e-06
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.
Pssm-ID: 467616 [Multi-domain] Cd Length: 157 Bit Score: 45.61 E-value: 3.83e-06
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.
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