A0A923G3B4 · A0A923G3B4_9PSED
- Protein4-hydroxythreonine-4-phosphate dehydrogenase
- GenepdxA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids329 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Miscellaneous
The active site is located at the dimer interface.
Catalytic activity
- 4-(phosphooxy)-L-threonine + NAD+ = 3-amino-2-oxopropyl phosphate + CO2 + NADH
Cofactor
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )
Co2+ (UniProtKB | Rhea| CHEBI:48828 )
Note: Binds 1 divalent metal cation per subunit. Can use ions such as Zn2+, Mg2+ or Co2+.
Pathway
Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 136 | substrate | |||
Binding site | 137 | substrate | |||
Binding site | 166 | a divalent metal cation (UniProtKB | ChEBI); ligand shared between dimeric partners | |||
Binding site | 211 | a divalent metal cation (UniProtKB | ChEBI); ligand shared between dimeric partners | |||
Binding site | 266 | a divalent metal cation (UniProtKB | ChEBI); ligand shared between dimeric partners | |||
Binding site | 274 | substrate | |||
Binding site | 283 | substrate | |||
Binding site | 292 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 4-hydroxythreonine-4-phosphate dehydrogenase activity | |
Molecular Function | cobalt ion binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | NAD binding | |
Molecular Function | zinc ion binding | |
Biological Process | pyridoxal phosphate biosynthetic process | |
Biological Process | pyridoxine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name4-hydroxythreonine-4-phosphate dehydrogenase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionA0A923G3B4
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length329
- Mass (Da)34,960
- Last updated2023-02-22 v1
- MD5 Checksum82721CDE667642EBF52E4FBCD7093D46
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JABWRJ010000001 EMBL· GenBank· DDBJ | MBC3444167.1 EMBL· GenBank· DDBJ | Genomic DNA |