A0A7J5QB49 · A0A7J5QB49_9BACE
- ProteinErythronate-4-phosphate dehydrogenase
- GenepdxB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids346 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
Catalytic activity
- 4-phospho-D-erythronate + NAD+ = (R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + H+ + NADH
Pathway
Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 2/5.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 46 | substrate | ||||
Sequence: T | ||||||
Binding site | 67 | substrate | ||||
Sequence: T | ||||||
Binding site | 147 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 209 | |||||
Sequence: R | ||||||
Binding site | 233 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 238 | |||||
Sequence: E | ||||||
Active site | 255 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 258 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 259 | substrate | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 4-phosphoerythronate dehydrogenase activity | |
Molecular Function | NAD binding | |
Molecular Function | protein dimerization activity | |
Biological Process | pyridoxine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameErythronate-4-phosphate dehydrogenase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Bacteroidia > Bacteroidales > Bacteroidaceae > Bacteroides
Accessions
- Primary accessionA0A7J5QB49
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 14-280 | D-isomer specific 2-hydroxyacid dehydrogenase catalytic | ||||
Sequence: EAIQRIADEVVYVPGKDFTPELVRDADALIVRTRTHCNRNLLEGSRVKFIATATIGFDHIDTEYCKQAGIEWTNAPGCNSASVAQYIQSSLLVWKSCRNKKLNELTIGIIGVGNVGSKVAKVARDFGMRVLLNDLPREEKEGTELFASLKKIAEECDIITFHVPLYKEGKYKTFHLADENFFQSLKRKPAIINTSRGEVIDTDALLKALDSRIISDAIIDVWEHEPEINRELLEKAFIGTPHIAGYSADGKANATRMSLDAICKFFQ | ||||||
Domain | 108-257 | D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding | ||||
Sequence: KSCRNKKLNELTIGIIGVGNVGSKVAKVARDFGMRVLLNDLPREEKEGTELFASLKKIAEECDIITFHVPLYKEGKYKTFHLADENFFQSLKRKPAIINTSRGEVIDTDALLKALDSRIISDAIIDVWEHEPEINRELLEKAFIGTPHIA | ||||||
Domain | 300-345 | Erythronate-4-phosphate dehydrogenase dimerisation | ||||
Sequence: KNHEEAILQIYNPVEDSTRLKNQPEQFETLRGDYPLRREETAYLIK |
Sequence similarities
Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. PdxB subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length346
- Mass (Da)39,066
- Last updated2021-04-07 v1
- ChecksumC254AA15BE425E48