A0A7K4AJ78 · A0A7K4AJ78_METSH
- ProteinPyridoxal 5'-phosphate synthase subunit PdxT
- GenepdxT
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids192 (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 | 49-51 | L-glutamine (UniProtKB | ChEBI) | |||
Active site | 81 | Nucleophile | |||
Binding site | 109 | L-glutamine (UniProtKB | ChEBI) | |||
Binding site | 137-138 | L-glutamine (UniProtKB | ChEBI) | |||
Active site | 173 | ||||
Active site | 173 | Charge relay system | |||
Active site | 175 | ||||
Active site | 175 | 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 lineageArchaea > Euryarchaeota > Stenosarchaea group > Methanomicrobia > Methanotrichales > Methanotrichaceae > Methanothrix
Accessions
- Primary accessionA0A7K4AJ78
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
- Length192
- Mass (Da)20,602
- Last updated2021-04-07 v1
- MD5 Checksum8C41836DE9D8CB40F4CB08D1CE78C1EA
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JAAYUN010000141 EMBL· GenBank· DDBJ | NLJ23066.1 EMBL· GenBank· DDBJ | Genomic DNA |