A0A5P9Q920 · A0A5P9Q920_9MICO
- Protein4-hydroxy-tetrahydrodipicolinate reductase
- GenedapB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids267 (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 + H2O + NAD+ = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H+ + NADH
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 | 23-28 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GAEGRM | ||||||
Binding site | 47 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 92-94 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GTT | ||||||
Binding site | 123-126 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: APNF | ||||||
Active site | 153 | Proton donor/acceptor | ||||
Sequence: H | ||||||
Binding site | 154 | (S)-2,3,4,5-tetrahydrodipicolinate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 157 | Proton donor | ||||
Sequence: K | ||||||
Binding site | 163-164 | (S)-2,3,4,5-tetrahydrodipicolinate (UniProtKB | ChEBI) | ||||
Sequence: GT |
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
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Micrococcales > Luteimicrobium
Accessions
- Primary accessionA0A5P9Q920
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 18-126 | Dihydrodipicolinate reductase N-terminal | ||||
Sequence: RVAVLGAEGRMGRTTCDAVEAAAGLELVARVTRGDDVAQALADSGADVAVDFTRPDVTEENVHAALDAGVHVVVGTTGWTAERQGRVREHLARRAAEGLDLGVIVAPNF | ||||||
Domain | 130-264 | Dihydrodipicolinate reductase C-terminal | ||||
Sequence: AVLAMTFAAKAARYFESVEVIELHHPDKLDAPSGTATHTARAVAAARAAAGVAPSPDATESGFGARGADVDGVRVHAVRLRGLVAHEEILLGNVGEQLVIRQDSFDRVSFMPGVVLAVREVGRRPGLTVGLEHVL |
Sequence similarities
Belongs to the DapB family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length267
- Mass (Da)27,855
- Last updated2020-04-22 v1
- Checksum34CDB145DB17B35D
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP045529 EMBL· GenBank· DDBJ | QFU97931.1 EMBL· GenBank· DDBJ | Genomic DNA |