A0A1E3S3L3 · A0A1E3S3L3_MYCIE
- ProteinPyridoxal 5'-phosphate synthase subunit PdxT
- GenepdxT
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids198 (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
- H2O + L-glutamine = 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 | 49-51 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: GES | ||||||
Active site | 81 | Nucleophile | ||||
Sequence: C | ||||||
Binding site | 113 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 141-142 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: IR | ||||||
Active site | 177 | |||||
Sequence: H | ||||||
Active site | 177 | Charge relay system | ||||
Sequence: H | ||||||
Active site | 179 | |||||
Sequence: E | ||||||
Active site | 179 | Charge relay system | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | glutaminase activity | |
Molecular Function | pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity | |
Molecular Function | transferase activity | |
Biological Process | glutamine catabolic process | |
Biological Process | pyridoxal phosphate biosynthetic 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
- Strains
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium simiae complex
Accessions
- Primary accessionA0A1E3S3L3
Proteomes
Interaction
Subunit
In the presence of PdxS, forms a dodecamer of heterodimers. Only shows activity in the heterodimer.
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length198
- Mass (Da)21,197
- Last updated2017-01-18 v1
- ChecksumC2C25B208553E6AE
Keywords
- Technical term