A0A922L205 · A0A922L205_DERFA
- ProteinGlycerol-3-phosphate dehydrogenase [NAD(+)]
- GeneGPD1_1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids393 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- NAD+ + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H+ + NADH
Pathway
Lipid metabolism.
Phospholipid metabolism; alpha-glycerophosphate cycle.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 139 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 162 | substrate | ||||
Sequence: K | ||||||
Binding site | 196 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Active site | 247 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 312 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 312-313 | substrate | ||||
Sequence: RN | ||||||
Binding site | 339 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 341 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | glycerol-3-phosphate dehydrogenase (FAD) complex | |
Molecular Function | NAD binding | |
Molecular Function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor | |
Molecular Function | protein homodimerization activity | |
Biological Process | carbohydrate metabolic process | |
Biological Process | glycerol-3-phosphate catabolic process | |
Biological Process | NADH oxidation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlycerol-3-phosphate dehydrogenase [NAD(+)]
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Chelicerata > Arachnida > Acari > Acariformes > Sarcoptiformes > Astigmata > Psoroptidia > Analgoidea > Pyroglyphidae > Dermatophagoidinae > Dermatophagoides
Accessions
- Primary accessionA0A922L205
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-19 | Polar residues | ||||
Sequence: MFVVRSYSSIPSSSSSSND | ||||||
Region | 1-25 | Disordered | ||||
Sequence: MFVVRSYSSIPSSSSSSNDNNKHRH | ||||||
Domain | 57-214 | Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal | ||||
Sequence: GSAIAKIVGKNAHKYPQFETDVRMYVYEEIVDGRKLSEIINEQHENVKYLPGHKLPENIIADPDLEHTVGDADILVFVVPHAFVSRICNTLKGKINPNAIAISLIKGFNELPSGGIELISDVIRHTLGIDTSVLMGANLANEVAEQKFCETTIGCKCP | ||||||
Domain | 236-382 | Glycerol-3-phosphate dehydrogenase NAD-dependent C-terminal | ||||
Sequence: DRYTVEICGALKNVVACAAGFSDGLGYGDNTKAAVIRIGLKEMIRFCKTFYADGLRVSTFFESCGVADLITTCYGGRNRRVSEAFVKTGKTIEELETEMLNGQKLQGYQTCEEVVNMLNLNGYIDRFPLFHAVNLIYKRELPAEKLV |
Sequence similarities
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length393
- Mass (Da)44,206
- Last updated2023-02-22 v1
- Checksum3F7830F8A2925FE4
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A922KVV6 | A0A922KVV6_DERFA | GPD1_1 | 363 | ||
A0A922KY55 | A0A922KY55_DERFA | GPD1_1 | 376 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-19 | Polar residues | ||||
Sequence: MFVVRSYSSIPSSSSSSND |
Keywords
- Technical term