Search Results
Overview
| Uniprot ID | Q00796 |
|---|---|
| Protein Name | Sorbitol dehydrogenase |
| Gene Name | SORD |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 107 | RENDEFCKMGRYNLS |
| 134 | GNLCRFYKHNAAFCY |
| 214 | ATRLSKAKEIGADLV |
| 295 | AIREVDIKGVFRYCN |
| 319 | ASKSVNVKPLVTHRF |
| 330 | THRFPLEKALEAFET |
| 339 | LEAFETFKKGLGLKI |
| 6 | **MAAAAKPNNLSLV |
| 63 | RIGNFIVKKPMVLGH |
| 64 | IGNFIVKKPMVLGHE |
| 78 | EASGTVEKVGSSVKH |
| 84 | EKVGSSVKHLKPGDR |
| 87 | GSSVKHLKPGDRVAI |
Function
Polyol dehydrogenase that catalyzes the reversible NAD(+)-dependent oxidation of various sugar alcohols. Is mostly active with D-sorbitol (D-glucitol), L-threitol, xylitol and ribitol as substrates, leading to the C2-oxidized products D-fructose, L-erythrulose, D-xylulose, and D-ribulose, respectively (PubMed:3365415). Is a key enzyme in the polyol pathway that interconverts glucose and fructose via sorbitol, which constitutes an important alternate route for glucose metabolism. The polyol pathway is believed to be involved in the etiology of diabetic complications, such as diabetic neuropathy and retinopathy, induced by hyperglycemia (PubMed:12962626, PubMed:25105142, PubMed:29966615). May play a role in sperm motility by using sorbitol as an alternative energy source for sperm motility (PubMed:16278369). May have a more general function in the metabolism of secondary alcohols since it also catalyzes the stereospecific oxidation of (2R,3R)-2,3-butanediol. To a lesser extent, can also oxidize L-arabinitol, galactitol and D-mannitol and glycerol in vitro. Oxidizes neither ethanol nor other primary alcohols. Cannot use NADP(+) as the electron acceptor (PubMed:3365415)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005615 | extracellular space |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0031966 | mitochondrial membrane |
| Cellular Component | GO:0031514 | motile cilium |
| Molecular Function | GO:0000721 | (R,R)-butanediol dehydrogenase activity |
| Molecular Function | GO:0030246 | carbohydrate binding |
| Molecular Function | GO:0046526 | D-xylulose reductase activity |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0003939 | L-iditol 2-dehydrogenase (NAD+) activity |
| Molecular Function | GO:0051287 | NAD binding |
| Molecular Function | GO:0050255 | ribitol 2-dehydrogenase (NAD+) activity |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0019640 | D-glucuronate catabolic process to D-xylulose 5-phosphate |
| Biological Process | GO:0030317 | flagellated sperm motility |
| Biological Process | GO:0046370 | fructose biosynthetic process |
| Biological Process | GO:0006006 | glucose metabolic process |
| Biological Process | GO:0006062 | sorbitol catabolic process |
| Biological Process | GO:0051160 | xylitol catabolic process |
| Biological Process | GO:0051164 | xylitol metabolic process |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.