A0A2M7SFQ4 · A0A2M7SFQ4_9DELT
- Protein4-hydroxythreonine-4-phosphate dehydrogenase
- GenepdxA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids345 (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
Note: Binds 1 divalent metal cation per subunit.
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 | 139 | substrate | |||
Binding site | 140 | substrate | |||
Binding site | 169 | a divalent metal cation (UniProtKB | ChEBI); ligand shared between dimeric partners | |||
Binding site | 214 | a divalent metal cation (UniProtKB | ChEBI); ligand shared between dimeric partners | |||
Binding site | 269 | a divalent metal cation (UniProtKB | ChEBI); ligand shared between dimeric partners | |||
Binding site | 277 | substrate | |||
Binding site | 286 | substrate | |||
Binding site | 295 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 4-hydroxythreonine-4-phosphate dehydrogenase activity | |
Molecular Function | metal ion binding | |
Molecular Function | NAD 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
- Strain
- Taxonomic lineageBacteria > Deltaproteobacteria
Accessions
- Primary accessionA0A2M7SFQ4
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length345
- Mass (Da)37,054
- Last updated2018-04-25 v1
- Checksum9F4FD063EB3CDBCE
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
PFMT01000457 EMBL· GenBank· DDBJ | PIZ18367.1 EMBL· GenBank· DDBJ | Genomic DNA |