A0AA96UK92 · A0AA96UK92_9BACI
- 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 | 12-17 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GPRGRM | ||||||
Binding site | 42 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 100-102 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GTT | ||||||
Binding site | 126-129 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: APNF | ||||||
Active site | 156 | Proton donor/acceptor | ||||
Sequence: H | ||||||
Binding site | 157 | (S)-2,3,4,5-tetrahydrodipicolinate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 160 | Proton donor | ||||
Sequence: K | ||||||
Binding site | 166-167 | (S)-2,3,4,5-tetrahydrodipicolinate (UniProtKB | ChEBI) | ||||
Sequence: GT |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
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 > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionA0AA96UK92
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 6-129 | Dihydrodipicolinate reductase N-terminal | ||||
Sequence: IKVVIAGPRGRMGQEAVKLAERTPHFDLVGAIDHTYDQQKLSDVMPVESDAFIYTDIHACFTETQPDVLIDLTTPEIGKVHTKIALEHGVRPVVGTTGFSEADLKELTSLTEEKGIGAIIAPNF | ||||||
Domain | 132-265 | Dihydrodipicolinate reductase C-terminal | ||||
Sequence: GAILMMKFSKMAANYFEDVEIIELHHDQKLDAPSGTALKTAEMISEVRKEKQQGHPDEKEILPGARGAEQNGIRLHSVRLPGLIAHQEVMFGMDGQTLQIRHDSYNRASFMSGVKLSVEQVMKIDQLVYGLENI |
Sequence similarities
Belongs to the DapB family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length267
- Mass (Da)29,474
- Last updated2024-03-27 v1
- Checksum2EC536E27665EC00