P32816 · GLDA_GEOSE
- ProteinGlycerol dehydrogenase
- GenegldA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids370 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone). Allows microorganisms to utilize glycerol as a source of carbon under anaerobic conditions. Is also able to use various diols as substrates, such as propan-1,2-diol, butan-2,3-diol, ethan-1,2-diol, and 3-mercapto-1,2-dihydroxypropane.
Catalytic activity
- glycerol + NAD+ = dihydroxyacetone + H+ + NADH
- H+ + hydroxyacetone + NADH = (S)-propane-1,2-diol + NAD+
Cofactor
Note: Binds 1 zinc ion per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
3.8 mM | glycerol | |||||
121 μM | NAD+ |
pH Dependence
Optimum pH is 6.0-8.5.
Pathway
Polyol metabolism; glycerol fermentation; glycerone phosphate from glycerol (oxidative route): step 1/2.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 39 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 96 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 97 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 118 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 121 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 123 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 127 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 129 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 133 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 173 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 173 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 256 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 256 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 274 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | glycerol dehydrogenase (NAD+) activity | |
Molecular Function | metal ion binding | |
Biological Process | anaerobic glycerol catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlycerol dehydrogenase
- EC number
- Short namesGDH; GLDH; GlyDH
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Geobacillus
Accessions
- Primary accessionP32816
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 97 | Loss of activity. | ||||
Sequence: K → H | ||||||
Mutagenesis | 305 | No effect on affinity for substrates. | ||||
Sequence: S → C |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000087826 | 1-370 | Glycerol dehydrogenase | |||
Sequence: MAAERVFISPAKYVQGKNVITKIANYLEGIGNKTVVIADEIVWKIAGHTIVNELKKGNIAAEEVVFSGEASRNEVERIANIARKAEAAIVIGVGGGKTLDTAKAVADELDAYIVIVPTAASTDAPTSALSVIYSDDGVFESYRFYKKNPDLVLVDTKIIANAPPRLLASGIADALATWVEARSVIKSGGKTMAGGIPTIAAEAIAEKCEQTLFKYGKLAYESVKAKVVTPALEAVVEANTLLSGLGFESGGLAAAHAIHNGFTALEGEIHHLTHGEKVAFGTLVQLALEEHSQQEIERYIELYLSLDLPVTLEDIKLKDASREDILKVAKAATAEGETIHNAFNVTADDVADAIFAADQYAKAYKEKHRK |
Interaction
Subunit
Homooctamer.
Structure
Sequence
- Sequence statusComplete
- Length370
- Mass (Da)39,501
- Last updated1993-10-01 v1
- ChecksumE5D93264B1670F25
Keywords
- Technical term