A0A6B3E603 · A0A6B3E603_9ACTN
- ProteinPyridoxal 5'-phosphate synthase subunit PdxT
- GenepdxT
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids197 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic activity
- L-glutamine + H2O = L-glutamate + NH4+
Pathway
Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 50-52 | L-glutamine (UniProtKB | ChEBI) | |||
Active site | 82 | Nucleophile | |||
Binding site | 111 | L-glutamine (UniProtKB | ChEBI) | |||
Binding site | 140-141 | L-glutamine (UniProtKB | ChEBI) | |||
Active site | 176 | ||||
Active site | 176 | Charge relay system | |||
Active site | 178 | ||||
Active site | 178 | Charge relay system | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | glutaminase complex | |
Molecular Function | glutaminase activity | |
Molecular Function | pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity | |
Biological Process | glutamine catabolic process | |
Biological Process | pyridoxal phosphate biosynthetic process | |
Biological Process | pyridoxine metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyridoxal 5'-phosphate synthase subunit PdxT
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces
Accessions
- Primary accessionA0A6B3E603
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
In the presence of PdxS, forms a dodecamer of heterodimers. Only shows activity in the heterodimer.
Structure
Sequence
- Sequence statusComplete
- Length197
- Mass (Da)20,787
- Last updated2020-06-17 v1
- Checksum2DFD6916ACC7A2B3
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JAAGLP010000007 EMBL· GenBank· DDBJ | NED78586.1 EMBL· GenBank· DDBJ | Genomic DNA |