O59791
Gene name |
SRR (SPCC320.14, SPCC330.15c) |
Protein name |
Serine racemase |
Names |
D-serine ammonia-lyase, D-serine dehydratase, L-serine ammonia-lyase, L-serine dehydratase |
Species |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
KEGG Pathway |
spo:SPCC320.14 |
EC number |
4.3.1.17: Ammonia-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
5 structures for O59791
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1V71 | X-ray | 170 A | A | 1-323 | PDB |
| 1WTC | X-ray | 190 A | A | 1-323 | PDB |
| 2ZPU | X-ray | 170 A | A | 1-323 | PDB |
| 2ZR8 | X-ray | 220 A | A | 1-323 | PDB |
| AF-O59791-F1 | Predicted | AlphaFoldDB |
No variants for O59791
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O59791 | |||||
No associated diseases with O59791
1 regional properties for O59791
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Tryptophan synthase beta chain-like, PALP domain | 23 - 309 | IPR001926 |
Functions
| Description | ||
|---|---|---|
| EC Number | 4.3.1.17 | Ammonia-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 |
8 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| D-serine ammonia-lyase activity | Catalysis of the reaction: D-serine = pyruvate + NH3. |
| L-serine ammonia-lyase activity | Catalysis of the reaction: L-serine = pyruvate + NH3. |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| protein homodimerization activity | Binding to an identical protein to form a homodimer. |
| pyridoxal phosphate binding | Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6. |
| serine racemase activity | Catalysis of the synthesis of free D-serine from L-serine. |
| threonine racemase activity | Catalysis of the reaction: L-threonine = D-threonine. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| D-serine biosynthetic process | The chemical reactions and pathways resulting in the formation of D-serine, the D-enantiomer of serine, i.e. (2R)-2-amino-3-hydroxypropanoic acid. D-serine is often formed by racemization of L-serine. |
| D-serine metabolic process | The chemical reactions and pathways involving D-serine, the D-enantiomer of serine, i.e. (2R)-2-amino-3-hydroxypropanoic acid. |
| L-serine metabolic process | The chemical reactions and pathways involving L-serine, the L-enantiomer of serine, i.e. (2S)-2-amino-3-hydroxypropanoic acid. |
| pyruvate biosynthetic process | The chemical reactions and pathways resulting in the formation of pyruvate, 2-oxopropanoate. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSDNLVLPTY | DDVASASERI | KKFANKTPVL | TSSTVNKEFV | AEVFFKCENF | QKMGAFKFRG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ALNALSQLNE | AQRKAGVLTF | SSGNHAQAIA | LSAKILGIPA | KIIMPLDAPE | AKVAATKGYG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GQVIMYDRYK | DDREKMAKEI | SEREGLTIIP | PYDHPHVLAG | QGTAAKELFE | EVGPLDALFV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| CLGGGGLLSG | SALAARHFAP | NCEVYGVEPE | AGNDGQQSFR | KGSIVHIDTP | KTIADGAQTQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| HLGNYTFSII | KEKVDDILTV | SDEELIDCLK | FYAARMKIVV | EPTGCLSFAA | ARAMKEKLKN |
| 310 | 320 | ||||
| KRIGIIISGG | NVDIERYAHF | LSQ |