Q03148 · SNZ1_YEAST
- ProteinPyridoxal 5'-phosphate synthase subunit SNZ1
- GeneSNZ1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids297 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by a SNO isoform. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively.
Catalytic activity
- aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H+ + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.11 mM | ribose 5-phosphate | |||||
0.3 mM | glyceraldehyde 3-phosphate |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
1.45 nmol/min/mg | with ribose 5-phosphate as substrate | ||||
1.54 nmol/min/mg | with glyceraldehyde 3-phosphate as substrate |
Pathway
Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 23 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 80 | Schiff-base intermediate with D-ribose 5-phosphate | ||||
Sequence: K | ||||||
Binding site | 152 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 164 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 214 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 235-236 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: GS |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | glutaminase complex | |
Molecular Function | amine-lyase activity | |
Molecular Function | pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity | |
Biological Process | amino acid metabolic process | |
Biological Process | glutamine catabolic process | |
Biological Process | pyridoxal phosphate biosynthetic process | |
Biological Process | pyridoxine biosynthetic process | |
Biological Process | vitamin B6 biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyridoxal 5'-phosphate synthase subunit SNZ1
- EC number
- Short namesPLP synthase subunit SNZ1
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionQ03148
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Disruption phenotype
Defects cause some sensibility to 6-azauracil, an inhibitor of purine and pyrimidine biosynthetic enzymes, and methylene blue, a producer of singlet oxygen. These effects are probably due to the inability to synthesize pyridoxal 5'-phosphate.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 116 | No effect. | ||||
Sequence: E → A | ||||||
Mutagenesis | 117 | No activity. | ||||
Sequence: K → A | ||||||
Mutagenesis | 136-137 | No pyridoxal 5'-phosphate synthesis activity. Retains ability to isomerize dihydroxyacetone phosphate to glyceraldehyde 3-phosphate. | ||||
Sequence: RR → AA | ||||||
Mutagenesis | 148 | No activity. | ||||
Sequence: K → A | ||||||
Mutagenesis | 164 | No pyridoxal 5'-phosphate synthesis activity. Retains ability to isomerize dihydroxyacetone phosphate to glyceraldehyde 3-phosphate. | ||||
Sequence: R → A | ||||||
Mutagenesis | 240 | No effect. | ||||
Sequence: K → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 6 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000109358 | 1-297 | Pyridoxal 5'-phosphate synthase subunit SNZ1 | |||
Sequence: MTGEDFKIKSGLAQMLKGGVIMDVVTPEQAKIAEKSGACAVMALESIPADMRKSGKVCRMSDPKMIKDIMNSVSIPVMAKVRIGHFVEAQIIEALEVDYIDESEVLTPADWTHHIEKDKFKVPFVCGAKDLGEALRRINEGAAMIRTKGEAGTGDVSEAVKHIRRITEEIKACQQLKSEDDIAKVAEEMRVPVSLLKDVLEKGKLPVVNFAAGGVATPADAALLMQLGCDGVFVGSGIFKSSNPVRLATAVVEATTHFDNPSKLLEVSSDLGELMGGVSIESISHASNGVRLSEIGW |
Proteomic databases
PTM databases
Expression
Developmental stage
Shows increased synthesis after entry into stationary phase.
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q03148 | SNO1 Q03144 | 4 | EBI-17618, EBI-28190 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Length297
- Mass (Da)31,817
- Last updated1997-11-01 v1
- ChecksumC5BC77711B415D9F
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z49807 EMBL· GenBank· DDBJ | CAA89897.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006946 EMBL· GenBank· DDBJ | DAA09993.1 EMBL· GenBank· DDBJ | Genomic DNA |