O09452
Gene name |
GAPC1 |
Protein name |
Glyceraldehyde-3-phosphate dehydrogenase, chloroplastic |
Names |
NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase |
Species |
Guillardia theta (Cryptophyte) (Cryptomonas phi) |
KEGG Pathway |
|
EC number |
1.2.1.59: With NAD(+) or NADP(+) 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 O09452
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O09452-F1 | Predicted | AlphaFoldDB |
No variants for O09452
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O09452 | |||||
No associated diseases with O09452
3 regional properties for O09452
Functions
| Description | ||
|---|---|---|
| EC Number | 1.2.1.59 | With NAD(+) or NADP(+) 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 |
|---|---|
| chloroplast | A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity | Catalysis of the reaction: D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+. |
| glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity | Catalysis of the reaction: phosphate + NADP+ + glyceraldehyde-3-phosphate = NADPH + 3-phospho-D-glyceroyl-phosphate. |
| NAD binding | Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH. |
| NADP binding | Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| 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. |
| 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 |
| MAYFKAVAYL | AALASAAAFN | PGSSFVPRLN | APATQPKAAK | MTGPTMQAVP | CGINGFGRIG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RLVARIMIKD | PETKLLQVNA | GSATPDYMAY | QFKYDSIHGR | YQGDVVVDGD | DLVIDGQRVI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TTRARDPKDI | GWAKTGVEYL | CESTGVFLTA | EKAQPHIDAG | VKKVIFSAPA | KDDSLTVVMG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VNAEDYKGQT | DFISCASCTT | NGLAPLVKCI | NDKWGIEEGL | MTTIHAMTAT | QAVVDSSSRK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DWRGGRAASG | NIIPSSTGAA | KAVAKVIPAV | KGKLTGMAFR | VPTIDVSVVD | LTCRLAKDAT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| YEEICAEVKR | RANGDMKGFL | GYTDEPLVST | DFETEPISST | FDAEAGISLN | PRFVKLVAWY |
| 370 | 380 | ||||
| DNEWGYSNRV | KDLMVHVAKV | DAKVKA |