A0A1Q8Q3A0 · A0A1Q8Q3A0_9BACI
- ProteinGlucose-6-phosphate 1-dehydrogenase
- Genezwf
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids478 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
Catalytic activity
- D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH + H+
Pathway
Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 7-14 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: GATGDLAK | ||||||
Binding site | 41 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 84-85 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: DV | ||||||
Binding site | 147 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 177 | substrate | ||||
Sequence: H | ||||||
Binding site | 181 | substrate | ||||
Sequence: K | ||||||
Binding site | 215 | substrate | ||||
Sequence: E | ||||||
Binding site | 234 | substrate | ||||
Sequence: D | ||||||
Active site | 239 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 338 | substrate | ||||
Sequence: K | ||||||
Binding site | 343 | substrate | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | glucose-6-phosphate dehydrogenase activity | |
Molecular Function | NADP binding | |
Biological Process | glucose metabolic process | |
Biological Process | pentose-phosphate shunt, oxidative branch |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlucose-6-phosphate 1-dehydrogenase
- EC number
- Short namesG6PD
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Domibacillus
Accessions
- Primary accessionA0A1Q8Q3A0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-186 | Glucose-6-phosphate dehydrogenase NAD-binding | ||||
Sequence: VLFGATGDLAKRKIFPALYNLFMDGKMPDSFSIVGVGRREWSDQTFQSHVEESVHTFSRRIINDASNMKTFLQAFRYSPLDVTKSDEYQSLLETVQQQEKNLSIPENRLFYLSVSPEFVDAITSNIKQSGLGTVKGWKRLIVEKPFGHDLTSARELNEKLSRTFEEEEMYRIDHYLGKPMVQN | ||||||
Domain | 192-472 | Glucose-6-phosphate dehydrogenase C-terminal | ||||
Sequence: YTNPLLRAIWNKDHIVNVQITASEVVGVEERAGYYDRAGAIRDMVQNHMLQMVMMTAMQISKKGAEEVNDEKRKVMESLRPLQKEDVAANVIRGQYGPGEIKGEPVTAYENEPGVSPSSKNDTFIAARLWIDNDFWAGVPFYIRTGKRMQEKSTRIVVEFKNPLSAETAPNRLTIDISPSEGVSLQLNMKNPLNNQIEPVSIDFSANAKDVPEAYELLLFGALRGDPTFFAHWKEVELSWEWVQPILDAFEEDLVPLHLYRSGSMGPEASYQLLQEDGFKW |
Sequence similarities
Belongs to the glucose-6-phosphate dehydrogenase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length478
- Mass (Da)54,610
- Last updated2017-04-12 v1
- Checksum7CE198147C1993D0