A0A384KQC4 · A0A384KQC4_HALVD
- Protein4-hydroxy-tetrahydrodipicolinate reductase
- GenedapB
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids253 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic activity
- (S)-2,3,4,5-tetrahydrodipicolinate + NAD+ + H2O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADH + H+
Pathway
Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 9-14 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 91-93 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 115-118 | NAD+ (UniProtKB | ChEBI) | |||
Active site | 147 | Proton donor/acceptor | |||
Binding site | 148 | (S)-2,3,4,5-tetrahydrodipicolinate (UniProtKB | ChEBI) | |||
Active site | 151 | Proton donor | |||
Binding site | 157-158 | (S)-2,3,4,5-tetrahydrodipicolinate (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | 4-hydroxy-tetrahydrodipicolinate reductase | |
Molecular Function | NAD binding | |
Molecular Function | NADP binding | |
Molecular Function | oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor | |
Biological Process | diaminopimelate biosynthetic process | |
Biological Process | lysine biosynthetic process via diaminopimelate |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name4-hydroxy-tetrahydrodipicolinate reductase
- EC number
- Short namesHTPA reductase
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Haloferacaceae > Haloferax
Accessions
- Primary accessionA0A384KQC4
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 4-118 | Dihydrodipicolinate reductase N-terminal | |||
Domain | 121-252 | Dihydrodipicolinate reductase C-terminal | |||
Region | 172-191 | Disordered | |||
Sequence similarities
Belongs to the DapB family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length253
- Mass (Da)26,062
- Last updated2018-11-07 v1
- Checksum82A5E76A933E03D7
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AOHU01000092 EMBL· GenBank· DDBJ | ELY27512.1 EMBL· GenBank· DDBJ | Genomic DNA |