P13203 · GLCDH_THEAC
- ProteinGlucose 1-dehydrogenase
- Genegdh
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids361 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the NAD(P)+-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Is also significantly active with galactose as substrate, but not with mannose or glucose 6-phosphate. Can utilize both NAD+ and NADP+ as electron acceptor, with a marked preference for NADP+. Physiologically, may be involved in the degradation of both glucose and galactose through a non-phosphorylative variant of the Entner-Doudoroff pathway.
Catalytic activity
- D-glucose + NAD+ = D-glucono-1,5-lactone + H+ + NADH
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
10 mM | glucose | |||||
0.113 mM | NADP+ |
The KM value for NAD+ is superior to 30 mM, it could not be defined precisely as it was impossible to reach saturation of the enzyme.
Temperature Dependence
Thermostable. Retains full catalytic activity after 9 hours at 55 degrees Celsius, and at 75 degrees Celsius the half-life is approximately 3 hours.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 41 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 43 | substrate | ||||
Sequence: T | ||||||
Binding site | 68 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 69 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 119 | substrate | ||||
Sequence: E | ||||||
Binding site | 156 | substrate | ||||
Sequence: E | ||||||
Binding site | 156 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 160 | substrate | ||||
Sequence: N | ||||||
Binding site | 216-218 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: NRH | ||||||
Binding site | 275-277 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: FGT | ||||||
Binding site | 304-306 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SVD | ||||||
Binding site | 306 | substrate | ||||
Sequence: D | ||||||
Binding site | 349 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | D-glucose binding | |
Molecular Function | galactose 1-dehydrogenase (NADP+) activity | |
Molecular Function | galactose 1-dehydrogenase activity | |
Molecular Function | galactose binding | |
Molecular Function | glucose 1-dehydrogenase (NAD+) activity | |
Molecular Function | glucose 1-dehydrogenase (NADP+) activity | |
Molecular Function | glucose 1-dehydrogenase [NAD(P)+] activity | |
Molecular Function | NAD+ binding | |
Molecular Function | NADP+ binding | |
Molecular Function | zinc ion binding | |
Biological Process | galactose catabolic process via D-galactonate | |
Biological Process | non-phosphorylated glucose catabolic process | |
Biological Process | protein tetramerization |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlucose 1-dehydrogenase
- EC number
- Short namesGDH ; GlcDH
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Candidatus Thermoplasmatota > Thermoplasmata > Thermoplasmatales > Thermoplasmataceae > Thermoplasma
Accessions
- Primary accessionP13203
Proteomes
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 2 | |||||
Sequence: T → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000079889 | 2-361 | Glucose 1-dehydrogenase | |||
Sequence: TEQKAIVTDAPKGGVKYTTIDMPEPEHYDAKLSPVYIGICGTDRGEVAGALSFTYNPEGENFLVLGHEALLRVDDARDNGYIKKGDLVVPLVRRPGKCINCRIGRQDNCSIGDPDKHEAGITGLHGFMRDVIYDDIEYLVKVEDPELGRIAVLTEPLKNVMKAFEVFDVVSKRSIFFGDDSTLIGKRMVIIGSGSEAFLYSFAGVDRGFDVTMVNRHDETENKLKIMDEFGVKFANYLKDMPEKIDLLVDTSGDPTTTFKFLRKVNNNGVVILFGTNGKAPGYPVDGEDIDYIVERNITIAGSVDAAKIHYVQALQSLSNWNRRHPDAMKSIITYEAKPSETNIFFQKPHGEIKTVIKWQ |
Proteomic databases
Interaction
Structure
Family & Domains
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length361
- Mass (Da)40,250
- Last updated2007-01-23 v4
- Checksum4852179202F15208
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 338-361 | in Ref. 1; CAA42450 | ||||
Sequence: AKPSETNIFFQKPHGEIKTVIKWQ → RSRPKPTYSSRNHTER |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X59788 EMBL· GenBank· DDBJ | CAA42450.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL445065 EMBL· GenBank· DDBJ | CAC12026.1 EMBL· GenBank· DDBJ | Genomic DNA |