P37527
Gene name |
pdxS |
Protein name |
Pyridoxal 5'-phosphate synthase subunit PdxS |
Names |
PLP synthase subunit PdxS, Pdx1, Superoxide-inducible protein 7, SOI7 |
Species |
Bacillus subtilis (strain 168) |
KEGG Pathway |
bsu:BSU00110 |
EC number |
4.3.3.6: Amine-lyases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
3 structures for P37527
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 2NV1 | X-ray | 208 A | A/B/C/D/E/F | 1-294 | PDB |
| 2NV2 | X-ray | 212 A | A/C/E/G/I/K/M/O/Q/S/U/W | 1-294 | PDB |
| AF-P37527-F1 | Predicted | AlphaFoldDB |
No variants for P37527
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P37527 | |||||
No associated diseases with P37527
1 regional properties for P37527
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | PdxS/SNZ N-terminal domain | 9 - 213 | IPR033755 |
Functions
| Description | ||
|---|---|---|
| EC Number | 4.3.3.6 | Amine-lyases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| amine-lyase activity | Catalysis of the release of amines by the cleavage of a carbon-nitrogen bond or the reverse reaction with an amine as a substrate. |
| identical protein binding | Binding to an identical protein or proteins. |
| pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity | Catalysis of the reaction: D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate. The reaction occurs in two steps: L-glutamine + H2O = L-glutamate + NH3, and subsequently D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + NH3 = pyridoxal 5'-phosphate + 4 H2O + phosphate. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular amino acid metabolic process | The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups, as carried out by individual cells. |
| pyridoxal phosphate biosynthetic process | The chemical reactions and pathways resulting in the formation of pyridoxal phosphate, pyridoxal phosphorylated at the hydroxymethyl group of C-5, the active form of vitamin B6. |
| pyridoxine biosynthetic process | The chemical reactions and pathways resulting in the formation of pyridoxine, 2-methyl-3-hydroxy-4,5-bis(hydroxymethyl)pyridine, one of the vitamin B6 compounds. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAQTGTERVK | RGMAEMQKGG | VIMDVINAEQ | AKIAEEAGAV | AVMALERVPA | DIRAAGGVAR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| MADPTIVEEV | MNAVSIPVMA | KARIGHIVEA | RVLEAMGVDY | IDESEVLTPA | DEEFHLNKNE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| YTVPFVCGCR | DLGEATRRIA | EGASMLRTKG | EPGTGNIVEA | VRHMRKVNAQ | VRKVVAMSED |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ELMTEAKNLG | APYELLLQIK | KDGKLPVVNF | AAGGVATPAD | AALMMQLGAD | GVFVGSGIFK |
| 250 | 260 | 270 | 280 | 290 | |
| SDNPAKFAKA | IVEATTHFTD | YKLIAELSKE | LGTAMKGIEI | SNLLPEQRMQ | ERGW |