A0A5B9QFD0 · A0A5B9QFD0_9BACT
- Protein6-phosphogluconate dehydrogenase, decarboxylating
- GenegndA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids479 (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+ = CO2 + D-ribulose 5-phosphate + 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 | 11-16 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: GLAVMG | ||||||
Binding site | 34-36 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: NRT | ||||||
Binding site | 76-78 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: VKA | ||||||
Binding site | 104 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 104 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: N | ||||||
Binding site | 130-132 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: SGG | ||||||
Active site | 187 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 190-191 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HN | ||||||
Active site | 194 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 195 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: Y | ||||||
Binding site | 264 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: K | ||||||
Binding site | 291 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 449 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 455 | substrate; ligand shared between dimeric partners | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | NADP binding | |
Molecular Function | phosphogluconate dehydrogenase (decarboxylating) activity | |
Biological Process | D-gluconate metabolic process | |
Biological Process | organic acid catabolic process | |
Biological Process | pentose-phosphate shunt |
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 > Planctomycetota > Planctomycetia > Pirellulales > Lacipirellulaceae > Bythopirellula
Accessions
- Primary accessionA0A5B9QFD0
Proteomes
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 183-471 | 6-phosphogluconate dehydrogenase C-terminal | ||||
Sequence: GHYVKMVHNGIEYGDMQMICEAYFLLTEGLGLSNEELYDVFEDWYQGELNSYLIEITRDIFSVMDDDGGYLVDKIMDRAGAKGTGKWMSQLALDLGVPSTLVTEAVYARCLSAMKEARVRASKVLSGPNPKYSGDKTNFIEQIRDALYASKICSYAQGFVQMQAAAIEHDWPLNFGDCAMLWRGGCIIRAVFLDRIKEAFDADPKLENLLLAPYFQEAVERSQDGWRHVVASAAQLGIPTPAFSAALAYYDGYRRERLPANLLQAQRDYFGAHTFERLDKPGTFHAEWI |
Sequence similarities
Belongs to the 6-phosphogluconate dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length479
- Mass (Da)52,870
- Last updated2019-11-13 v1
- Checksum42E567B3571836E5
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP042913 EMBL· GenBank· DDBJ | QEG36599.1 EMBL· GenBank· DDBJ | Genomic DNA |