A0A158K4Q0 · A0A158K4Q0_9BURK
- Protein6-phosphogluconate dehydrogenase, decarboxylating
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids468 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO2, with concomitant reduction of NADP to NADPH.
Catalytic activity
- 6-phospho-D-gluconate + NADP+ = D-ribulose 5-phosphate + CO2 + NADPH
Pathway
Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 3/3.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 10-15 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: GLAVMG | ||||||
Binding site | 33-35 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: NRS | ||||||
Binding site | 74-76 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: VKA | ||||||
Binding site | 102 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 102 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: N | ||||||
Binding site | 128-130 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: SGG | ||||||
Active site | 183 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 186-187 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HN | ||||||
Active site | 190 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 191 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: Y | ||||||
Binding site | 261 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: K | ||||||
Binding site | 288 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 446 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 452 | substrate; ligand shared between dimeric partners | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | NADP binding | |
Molecular Function | phosphogluconate dehydrogenase (decarboxylating) activity | |
Biological Process | D-gluconate catabolic process | |
Biological Process | pentose-phosphate shunt, oxidative branch |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name6-phosphogluconate dehydrogenase, decarboxylating
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Caballeronia
Accessions
- Primary accessionA0A158K4Q0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 179-468 | 6-phosphogluconate dehydrogenase C-terminal | ||||
Sequence: GHFVKMVHNGIEYGDMQLIAESYDVLKRVAGLSNEELHEVYSEWNKGELDSYLIEITTKIFTKKDEETGQHLVDVILDRAAQKGTGKWTSQNALDLGAPLPLITEAVFARVLSSLKDQRVKASKQLSGPSPKFDGDRAAFIESVRRALYLSKIVSYAQGFAQLRAASDEYKWDLHYGEIAKIFRAGCIIRARFLQKITDAYAKDEALANLLLDPYFSDIAAKYQDALRDVVVAAVKAGVPVPAFSSAVAYFDSYRSERLPANLVQAQRDFFGAHTFERVDKKGSFHADWA |
Sequence similarities
Belongs to the 6-phosphogluconate dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length468
- Mass (Da)51,289
- Last updated2017-09-27 v1
- Checksum2557CD146069C7FF