Reviewed,
UniProtKB/Swiss-Prot Q43839 (G6PDC_SOLTU)
Last modified
November 25, 2008.
Version 61.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Glucose-6-phosphate 1-dehydrogenase, chloroplastic Short name=G6PD EC=1.1.1.49 |
| Organism | Solanum tuberosum (Potato) |
| Taxonomic identifier | 4113 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum |
Protein attributes
| Sequence length | 577 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis which are involved in membrane synthesis and cell division. May be involved in nitrite reduction. |
| Catalytic activity | D-glucose 6-phosphate + NADP(+) = D-glucono-1,5-lactone 6-phosphate + NADPH. |
| Enzyme regulation | Regulated by metabolites. Post-translationally inactivated by cysteine-mediated redox modification via the ferredoxin-thioredoxin system in the light and this avoids futile cycles with photosynthetic CO2 fixation. Ref.2 |
| Pathway | |
| Subunit structure | Homodimer. |
| Subcellular location | |
| Tissue specificity | Green tissues, leaves and chloroplasts. |
| Sequence similarities | Belongs to the glucose-6-phosphate dehydrogenase family. |
Ontologies
Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Glucose metabolism |
| Cellular component | Chloroplast Plastid |
| Domain | Transit peptide |
| Ligand | NADP |
| Molecular function | Oxidoreductase |
Gene Ontology (GO) | |
| Biological process | glucose metabolic process Inferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | chloroplast Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | binding Inferred from electronic annotation. Source: InterPro glucose-6-phosphate dehydrogenase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 63 | 63 | Chloroplast Potential | ||||||||
| Chain | 64 – 577 | 514 | Glucose-6-phosphate 1-dehydrogenase, chloroplastic | PRO_0000010440 | |||||||
Sites | |||||||||||
| Active site | 326 | 1 | Proton acceptor By similarity | ||||||||
| Binding site | 131 | 1 | NADP By similarity | ||||||||
| Binding site | 264 | 1 | Substrate By similarity | ||||||||
| Binding site | 268 | 1 | Substrate By similarity | ||||||||
| Binding site | 427 | 1 | Substrate By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 149 ↔ 157 | Redox modulation Ref.2 | |||||||||
Experimental info | |||||||||||
| Mutagenesis | 119 | 1 | C → S: No effect on redox regulation Ref.2 | ||||||||
| Mutagenesis | 149 | 1 | C → S: Abolishes redox regulation Ref.2 | ||||||||
| Mutagenesis | 157 | 1 | C → S: Abolishes redox regulation Ref.2 | ||||||||
| Mutagenesis | 168 | 1 | C → S: No effect on redox regulation Ref.2 | ||||||||
| Mutagenesis | 194 | 1 | C → S: No effect on redox regulation Ref.2 | ||||||||
| Mutagenesis | 216 | 1 | C → S: No effect on redox regulation Ref.2 | ||||||||
Sequences
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References
| [1] | "Molecular characterization of the plastidic glucose-6-phosphate dehydrogenase from potato in comparison to its cytosolic counterpart." von Schaewen A., Langenkaemper G., Graeve K., Wenderoth I., Scheibe R. Plant Physiol. 109:1327-1335(1995) [PubMed: 8539293] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Desiree. Tissue: Green leaf. |
| [2] | "Identification of the cysteine residues involved in redox modification of plant plastidic glucose-6-phosphate dehydrogenase." Wenderoth I., Scheibe R., von Schaewen A. J. Biol. Chem. 272:26985-26990(1997) [PubMed: 9341136] [Abstract] Cited for: ENZYME REGULATION, DISULFIDE BOND, MUTAGENESIS OF CYS-119; CYS-149; CYS-157; CYS-168; CYS-194 AND CYS-216. |
Cross-references
Sequence databases | |
|---|---|
| X83923 mRNA. Translation: CAA58775.1. | |
| PIR | T07375. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1QKI based on UniProtKB P11413. |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR001282. Glc-6-P_DHase. IPR016040. NAD(P)-bd. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| PANTHER | PTHR23429. G6PDH. 1 hit. |
| Pfam | PF02781. G6PD_C. 1 hit. PF00479. G6PD_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF000110. G6PD. 1 hit. |
| PRINTS | PR00079. G6PDHDRGNASE. |
| ProDom | PD001129. G6PD. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR00871. zwf. 1 hit. |
| PROSITE | PS00069. G6P_DEHYDROGENASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | G6PDC_SOLTU | ||||||||
| Accession | Primary (citable) accession number: Q43839 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


