P23651
Gene name |
rbcL |
Protein name |
Ribulose bisphosphate carboxylase large chain |
Names |
RuBisCO large subunit |
Species |
Pylaiella littoralis (Seaweed) (Conferva littoralis) |
KEGG Pathway |
|
EC number |
4.1.1.39: Carboxy-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
1 structures for P23651
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P23651-F1 | Predicted | AlphaFoldDB |
No variants for P23651
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P23651 | |||||
No associated diseases with P23651
3 regional properties for P23651
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Ribulose bisphosphate carboxylase, large subunit, C-terminal | 158 - 465 | IPR000685 |
| domain | Ribulose bisphosphate carboxylase, large subunit, ferrodoxin-like N-terminal | 28 - 148 | IPR017443 |
| active_site | Ribulose bisphosphate carboxylase, large chain, active site | 200 - 208 | IPR020878 |
Functions
| Description | ||
|---|---|---|
| EC Number | 4.1.1.39 | Carboxy-lyases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| chloroplast | A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| monooxygenase activity | Catalysis of the incorporation of one atom from molecular oxygen into a compound and the reduction of the other atom of oxygen to water. |
| ribulose-bisphosphate carboxylase activity | Catalysis of the reaction: 2 (2R)-3-phosphoglycerate + 2 H+ = CO2 + D-ribulose 1,5-bisphosphate + H2O. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| 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 |
| MPEDVQNRTR | IKSERYESGV | IPYAKMGYWD | ADYNVKDTDI | LALFRITPQP | GVDPVEARAA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VAGESSTATW | TVVWTDLLTA | CDIYRAKAYR | VDPVPGTSDQ | FFAYIAYECD | LFEEGSLANL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TASIIGNVFG | FKAVKALRLE | DMRIPYAYLK | TFQGPATGVV | VERERLDKFG | RPLLGATVKP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KLGLSGKNYG | RVVYEGLAGG | LDFLKDDENI | NSQPFMRWKE | RFLYCMEGVN | RAAAATGEVK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GSYLNITAAT | MEQMYERAEY | AHSIGSVIVM | IDLVIGYTAI | QSMAIWARKY | EMILHLHRAG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| NSTYARQKNH | GINFRVICKW | MRMCGVDHIH | AGTVVGKLEG | DPLMVKGFYN | SLLLTHLKIN |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LAEGLFFDMD | WAALRKCVPV | ASGGIHCGQM | HQLLYYLGDD | VVLQFGGGTI | GHPDGIQSGA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| TANRVALESM | VLARNEGRDY | VGEGPEILRR | AAATCGPLKA | ALDLWKDITF | DYTSTDTPDF |
| VEVATESR |