Q2JJG9
Gene name |
CYB_2257 |
Protein name |
D-fructose 1,6-bisphosphatase class 2/sedoheptulose 1,7-bisphosphatase |
Names |
FBPase class 2/SBPase |
Species |
Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium Yellowstone B-Prime) |
KEGG Pathway |
cyb:CYB_2257 |
EC number |
3.1.3.11: Phosphoric monoester hydrolases |
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 Q2JJG9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q2JJG9-F1 | Predicted | AlphaFoldDB |
No variants for Q2JJG9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q2JJG9 | |||||
No associated diseases with Q2JJG9
No regional properties for Q2JJG9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q2JJG9 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 3.1.3.11 | Phosphoric monoester hydrolases |
| 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 |
|---|---|
| fructose 1,6-bisphosphate 1-phosphatase activity | Catalysis of the reaction: D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate. |
| metal ion binding | Binding to a metal ion. |
| sedoheptulose-bisphosphatase activity | Catalysis of the reaction: sedoheptulose 1,7-bisphosphate + H2O = sedoheptulose 7-phosphate + phosphate. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| gluconeogenesis | The formation of glucose from noncarbohydrate precursors, such as pyruvate, amino acids and glycerol. |
| glycerol metabolic process | The chemical reactions and pathways involving glycerol, 1,2,3-propanetriol, a sweet, hygroscopic, viscous liquid, widely distributed in nature as a constituent of many lipids. |
| reductive pentose-phosphate cycle | The fixation of carbon dioxide (CO2) as glucose in the chloroplasts of C3 plants; uses ATP and NADPH formed in the light reactions of photosynthesis; carbon dioxide reacts with ribulose 1,5-bisphosphate (catalyzed by the function of ribulose-bisphosphate carboxylase) to yield two molecules of 3-phosphoglycerate; these are then phosphorylated by ATP to 1,3-bisphosphateglyceraldehyde which, in turn, is then reduced by NADPH to glyceraldehyde 3-phosphate. The glyceraldehyde 3-phosphate is converted to fructose 5-phosphate and ribulose 5-phosphate by aldolase and other enzymes; the ribulose 5-phosphate is phosphorylated by ATP to ribulose 1,5-bisphosphate. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDNKLGLEII | EVVEQAAIAA | ARWMGKGDNK | TADQVAVEAM | REKLNQIPMR | GRIVIGEGTR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DEAPMLYIGE | EVGICTRPDA | EQFCRVEELV | EIDIAVDPCE | GTNLVAKGQN | GSMAVLAISE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KGGLLHAPDI | YMQKLAAPPQ | AKGKVHIDYP | PEKNLKIIAE | SLDREISDLT | VVVMDRKRHL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DLIRQIREAG | ARVKLITDGD | ISAALSAGFN | GTGIHALMGI | GAAPEGVISA | AALRCLGAHF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QGRLIYDPEV | VQAGTYLPPV | EETRRELKEK | GIEDPDKVWE | CEELASGKEV | LFAATGITDG |
| 310 | 320 | 330 | 340 | ||
| DLMRGVRFFG | GGARTETLVI | SSQSRTVRFV | DTIHMKDGQQ | PRGLQLR |