Q86S40
Gene name |
C50D2.7 |
Protein name |
Probable ADP-dependent glucokinase |
Names |
ADP-GK, ADPGK |
Species |
Caenorhabditis elegans |
KEGG Pathway |
cel:CELE_C50D2.7 |
EC number |
2.7.1.147: 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 Q86S40
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q86S40-F1 | Predicted | AlphaFoldDB |
No variants for Q86S40
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q86S40 | |||||
No associated diseases with Q86S40
No regional properties for Q86S40
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q86S40 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.1.147 | Phosphotransferases with an alcohol group as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| extracellular region | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| ADP-specific glucokinase activity | Catalysis of the reaction: ADP + D-glucose = AMP + D-glucose 6-phosphate. |
| metal ion binding | Binding to a metal ion. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| carbohydrate metabolic process | The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. |
| glucose metabolic process | The chemical reactions and pathways involving glucose, the aldohexose gluco-hexose. D-glucose is dextrorotatory and is sometimes known as dextrose; it is an important source of energy for living organisms and is found free as well as combined in homo- and hetero-oligosaccharides and polysaccharides. |
| 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 |
| MFSETFVPSI | FSYKHRLLHL | SVLFFIVPYW | YSYYNDQHRL | SSYSVETAMF | LSWERAIVKP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GAMFKKAVIG | FNCNVDLIVS | GVRVVDALNT | TCSEGKDQET | LETLADLHQT | FAHFFQRGAA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AERYMSSEDQ | FNLLVAESEA | STRSHHHIGG | NAALMADRIA | ANFPSTEVYL | VGPIGPRSQA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LLHPSVKRTN | STRILKDELH | VILEYKQGEI | LGDWVAPSSS | RFITSHDHFS | GSMVVMEMFF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KAIAQFRPDL | VVITGVHLLE | FQSKEMRQEK | MRLIKRNLLQ | IPPKVPIHLE | LGSLADEIFS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TDVINKILPY | VDSLGINEQE | LTFLSHIANG | PHMEEYPVQA | GTVHVHKVVE | MLHWLLKTYG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RDPTGQIASK | TGYRLSRIHF | HCLTYHIMVS | SGTDWSNLAA | GLAAGARIAG | RLSCNIGANT |
| 430 | 440 | 450 | 460 | 470 | 480 |
| MDSELLEIRT | PANFVLDKKI | EKNYQFEAHN | PIASWMREDV | LFVFTPVLVC | RLPSKTVGID |
| 490 | 500 | ||||
| DAISATGLLY | SQFYRLNRPT | HW |