A0A0H3MPU9 · A0A0H3MPU9_MYCLB
- ProteinPyridoxal 5'-phosphate synthase subunit PdxT
- GenepdxT
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids223 (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 | 74-76 | L-glutamine (UniProtKB | ChEBI) | |||
Active site | 106 | Nucleophile | |||
Binding site | 138 | L-glutamine (UniProtKB | ChEBI) | |||
Binding site | 166-167 | L-glutamine (UniProtKB | ChEBI) | |||
Active site | 202 | ||||
Active site | 202 | Charge relay system | |||
Active site | 204 | ||||
Active site | 204 | 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
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium
Accessions
- Primary accessionA0A0H3MPU9
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
- Length223
- Mass (Da)23,704
- Last updated2015-09-16 v1
- Checksum8EB675A7CB74E95B
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FM211192 EMBL· GenBank· DDBJ | CAR70567.1 EMBL· GenBank· DDBJ | Genomic DNA |