P08312
Gene name |
pheS (b1714, JW5277) |
Protein name |
Phenylalanine--tRNA ligase alpha subunit |
Names |
Phenylalanyl-tRNA synthetase alpha subunit, PheRS |
Species |
Escherichia coli (strain K12) |
KEGG Pathway |
eco:b1714 |
EC number |
6.1.1.20: Ligases forming aminoacyl-tRNA and related compounds |
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 P08312
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 3PCO | X-ray | 302 A | A/C | 1-327 | PDB |
| 6OZ5 | X-ray | 250 A | A/C | 2-327 | PDB |
| 6P24 | X-ray | 212 A | A/C | 2-327 | PDB |
| 6P26 | X-ray | 316 A | A/C | 2-327 | PDB |
| AF-P08312-F1 | Predicted | AlphaFoldDB |
2 variants for P08312
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| 98 | G>D | thermosensitive mutant pheS5; might cause subunit disaggregation due to electrostatic repulsion [UniProt] | No | ||
| 191 | G>D | decreased affinity for Phe [UniProt] | No |
No associated diseases with P08312
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.20 | Ligases forming aminoacyl-tRNA and related compounds |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| phenylalanine-tRNA ligase complex | An enzyme complex that catalyzes the ligation of phenylalanine to tRNA(Phe), forming L-phenylalanyl-tRNA(Phe). |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| phenylalanine-tRNA ligase activity | Catalysis of the reaction: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe). |
| tRNA binding | Binding to a transfer RNA. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| phenylalanyl-tRNA aminoacylation | The process of coupling phenylalanine to phenylalanyl-tRNA, catalyzed by phenylalanyl-tRNA synthetase. The phenylalanyl-tRNA synthetase is a class-II synthetase. However, unlike other class II enzymes, The activated amino acid is transferred to the 2'-OH group of a phenylalanine-accepting tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification. |
5 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q5ZJQ2 | FARSA | Phenylalanine--tRNA ligase alpha subunit | Gallus gallus (Chicken) | PR |
| Q9Y285 | FARSA | Phenylalanine--tRNA ligase alpha subunit | Homo sapiens (Human) | PR |
| Q9BRP7 | FDXACB1 | Ferredoxin-fold anticodon-binding domain-containing protein 1 | Homo sapiens (Human) | PR |
| Q505J8 | Farsa | Phenylalanine--tRNA ligase alpha subunit | Rattus norvegicus (Rat) | PR |
| Q1JPX3 | farsa | Phenylalanine--tRNA ligase alpha subunit | Danio rerio (Zebrafish) (Brachydanio rerio) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSHLAELVAS | AKAAISQASD | VAALDNVRVE | YLGKKGHLTL | QMTTLRELPP | EERPAAGAVI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NEAKEQVQQA | LNARKAELES | AALNARLAAE | TIDVSLPGRR | IENGGLHPVT | RTIDRIESFF |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GELGFTVATG | PEIEDDYHNF | DALNIPGHHP | ARADHDTFWF | DTTRLLRTQT | SGVQIRTMKA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QQPPIRIIAP | GRVYRNDYDQ | THTPMFHQME | GLIVDTNISF | TNLKGTLHDF | LRNFFEEDLQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IRFRPSYFPF | TEPSAEVDVM | GKNGKWLEVL | GCGMVHPNVL | RNVGIDPEVY | SGFAFGMGME |
| 310 | 320 | ||||
| RLTMLRYGVT | DLRSFFENDL | RFLKQFK |