A6V2N1
Gene name |
glk |
Protein name |
Glucokinase |
Names |
Glucose kinase |
Species |
Pseudomonas aeruginosa (strain PA7) |
KEGG Pathway |
pap:PSPA7_1935 |
EC number |
2.7.1.2: Phosphotransferases with an alcohol group as acceptor |
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
1 structures for A6V2N1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A6V2N1-F1 | Predicted | AlphaFoldDB |
No variants for A6V2N1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A6V2N1 | |||||
No associated diseases with A6V2N1
5 regional properties for A6V2N1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Alpha-D-phosphohexomutase, C-terminal | 373 - 443 | IPR005843 |
| domain | Alpha-D-phosphohexomutase, alpha/beta/alpha domain I | 3 - 134 | IPR005844 |
| domain | Alpha-D-phosphohexomutase, alpha/beta/alpha domain II | 166 - 253 | IPR005845 |
| domain | Alpha-D-phosphohexomutase, alpha/beta/alpha domain III | 257 - 366 | IPR005846 |
| conserved_site | Alpha-D-phosphohexomutase, conserved site | 95 - 104 | IPR016066 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.1.2 | Phosphotransferases with an alcohol group as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| glucokinase activity | Catalysis of the reaction: ATP + D-glucose = ADP + D-glucose-6-phosphate. |
| glucose binding | Binding to D- or L-enantiomers of glucose. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| glycolytic process | The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNNDKNGSSG | GLALIGDIGG | TNARFALWRG | QRLESIAVLA | CADYPRPELA | VRDYLARVGE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SLANIDSVCL | ACAGPVGAGD | FRFTNNHWSI | NRAAFREELG | LDHLLLVNDF | STMAWAASRL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GADELVQVRP | GSAQADRARL | IIGPGTGLGV | GSLLPLGEGR | WEVLPCEGGH | VDLPVTSARD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FAVWESLRER | YGHVSAERVL | SGNGLLALYE | ISCALDGIPV | RATSAAEVGA | LALAGDAQAD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AVLEHFFLWL | ARVAGNAALT | VGALGGVYIT | GGIVPRFRER | FLASGFAGAF | ASRGKTSGAY |
| 310 | 320 | 330 | |||
| LQDVPVWIMT | AEHPGLLGAG | VALQQALDAE | SRTGVRATA |