R7BB86 · R7BB86_9FIRM
- Protein4-hydroxy-tetrahydrodipicolinate reductase
- GenedapB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids250 (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 | 8-13 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GANGKM | ||||||
Binding site | 34 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 85-87 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: ATT | ||||||
Binding site | 109-112 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TYNM | ||||||
Active site | 142 | Proton donor/acceptor | ||||
Sequence: H | ||||||
Binding site | 143 | (S)-2,3,4,5-tetrahydrodipicolinate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 146 | Proton donor | ||||
Sequence: K | ||||||
Binding site | 152-153 | (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
- Taxonomic lineageBacteria > Bacillota
Accessions
- Primary accessionR7BB86
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-112 | Dihydrodipicolinate reductase N-terminal | ||||
Sequence: KLIITGANGKMGKVIKSIVENRDDCEIVAGVDLNTDDNGAFPIYSSINDIKESADAIIDFSNPVLLNDLLSYSEKTSTPLVIATTGYSDEQKKQIAQASKTTPIFFTYNM | ||||||
Domain | 115-248 | Dihydrodipicolinate reductase C-terminal | ||||
Sequence: GVNLLANLAKKAVEVLGDDFDIEIVEKHHNQKIDAPSGTALMLADAMCEEIEKPMKYEYDRHSKREKRTKNEIGIHAVRGGTIVGEHEIIFAGRDEIITLSHSARSKEIFAVGAVNAAVYMNGKGAGLYDMKEL |
Sequence similarities
Belongs to the DapB family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length250
- Mass (Da)27,391
- Last updated2013-07-24 v1
- ChecksumA8DF2C5050053C7D