Protein Family Models for Protein (Select 446581467) - Protein Family Models

Select item 4153501.

dihydrodipicolinate reductase C-terminal domain-containing protein

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. [1]. 8873595. Interaction of pyridine nucleotide substrates with Escherichia coli dihydrodipicolinate reductase: thermodynamic and structural analysis of binary complexes. Reddy SG, Scapin G, Blanchard JS;. Biochemistry 1996;35:13294-13302. [2]. 9398235. Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase in complex with NADH and the inhibitor 2,6-pyridinedicarboxylate. Scapin G, Reddy SG, Zheng R, Blanchard JS;. Biochemistry 1997;36:15081-15088. [3]. 7893645. Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase. Scapin G, Blanchard JS, Sacchettini JC;. Biochemistry 1995;34:3502-3512. (from Pfam)

GO Terms:

Molecular Function:: 4-hydroxy-tetrahydrodipicolinate reductase (GO:0008839)

Biological Process:: lysine biosynthetic process via diaminopimelate (GO:0009089)

Date:: 2024-10-16

Family Accession:: NF017024.5
Method:: HMM

Select item 4125032.

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. [1]. 8873595. Interaction of pyridine nucleotide substrates with Escherichia coli dihydrodipicolinate reductase: thermodynamic and structural analysis of binary complexes. Reddy SG, Scapin G, Blanchard JS;. Biochemistry 1996;35:13294-13302. [2]. 9398235. Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase in complex with NADH and the inhibitor 2,6-pyridinedicarboxylate. Scapin G, Reddy SG, Zheng R, Blanchard JS;. Biochemistry 1997;36:15081-15088. [3]. 7893645. Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase. Scapin G, Blanchard JS, Sacchettini JC;. Biochemistry 1995;34:3502-3512. (from Pfam)

GO Terms:

Molecular Function:: 4-hydroxy-tetrahydrodipicolinate reductase (GO:0008839)

Biological Process:: lysine biosynthetic process via diaminopimelate (GO:0009089)

Date:: 2024-10-16

Family Accession:: NF013293.5
Method:: HMM

Select item 3935413.

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Family Accession:

Select item 3901224.

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Family Accession:

Select item 3503095.

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Family Accession:

Select item 3475926.

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Family Accession:

Select item 1926737.

dihydrodipicolinate reductase

Gene:: dapB

Date:: 2018-10-02

Family Accession:: NBR006821
Method:: BlastRule

Select item 926298.

4-hydroxy-tetrahydrodipicolinate reductase

4-hydroxy-tetrahydrodipicolinate reductase catalyzes the NAD(P)-dependent conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate in amino acid biosynthesis pathways

Date:: 2024-07-16

Family Accession:: 11416656
Method:: Sparcle

Select item 169819.

4-hydroxy-tetrahydrodipicolinate reductase

Gene:: dapB

GO Terms:

Molecular Function:: 4-hydroxy-tetrahydrodipicolinate reductase (GO:0008839)

Biological Process:: lysine biosynthetic process via diaminopimelate (GO:0009089)

Date:: 2021-04-27

Family Accession:: TIGR00036.1
Method:: HMM

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