Q64442 · DHSO_MOUSE
- ProteinSorbitol dehydrogenase
- GeneSord
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids357 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Polyol dehydrogenase that catalyzes the reversible NAD+-dependent oxidation of various sugar alcohols (By similarity).
Is active with D-sorbitol (D-glucitol) leading to the C2-oxidized product D-fructose (PubMed:6852349).
Is a key enzyme in the polyol pathway that interconverts glucose and fructose via sorbitol, which constitutes an important alternate route for glucose metabolism (By similarity).
May play a role in sperm motility by using sorbitol as an alternative energy source for sperm motility and protein tyrosine phosphorylation (PubMed:18799757).
Has no activity on ethanol. Cannot use NADP+ as the electron acceptor (PubMed:6852349).
Is active with D-sorbitol (D-glucitol) leading to the C2-oxidized product D-fructose (PubMed:6852349).
Is a key enzyme in the polyol pathway that interconverts glucose and fructose via sorbitol, which constitutes an important alternate route for glucose metabolism (By similarity).
May play a role in sperm motility by using sorbitol as an alternative energy source for sperm motility and protein tyrosine phosphorylation (PubMed:18799757).
Has no activity on ethanol. Cannot use NADP+ as the electron acceptor (PubMed:6852349).
Catalytic activity
- H+ + keto-D-fructose + NADH = D-sorbitol + NAD+
Cofactor
Note: Binds 1 zinc ion per subunit.
Activity regulation
Inhibited in vitro by p-hydroxymercuribenzoate, EDTA, l,l0-phenanthroline and N-ethylmaleimide.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1.54 mM | sorbitol | |||||
58.8 μM | NAD+ | |||||
154 mM | fructose | |||||
15 μM | NADH |
pH Dependence
Optimum pH is 9.0 for sorbitol oxidation and 7.5 for D-fructose reduction.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 45 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 51 | substrate | ||||
Sequence: Y | ||||||
Binding site | 70 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 71 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 156 | substrate | ||||
Sequence: E | ||||||
Binding site | 184 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 204 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 209 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 273-275 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: VGM | ||||||
Binding site | 297-299 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: VFR | ||||||
Binding site | 299 | substrate | ||||
Sequence: R | ||||||
Binding site | 300 | substrate | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | extracellular exosome | |
Cellular Component | mitochondrial membrane | |
Cellular Component | mitochondrion | |
Cellular Component | motile cilium | |
Molecular Function | D-sorbitol dehydrogenase (acceptor) activity | |
Molecular Function | D-xylulose reductase activity | |
Molecular Function | identical protein binding | |
Molecular Function | L-iditol 2-dehydrogenase (NAD+) activity | |
Molecular Function | NAD binding | |
Molecular Function | zinc ion binding | |
Biological Process | flagellated sperm motility | |
Biological Process | fructose biosynthetic process | |
Biological Process | glucuronate catabolic process to xylulose 5-phosphate | |
Biological Process | L-xylitol catabolic process | |
Biological Process | response to cadmium ion | |
Biological Process | response to copper ion | |
Biological Process | response to hormone | |
Biological Process | sorbitol catabolic process | |
Biological Process | sorbitol metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSorbitol dehydrogenase
- EC number
- Short namesSDH; SORD
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ64442
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion membrane ; Peripheral membrane protein
Note: Associated with mitochondria of the midpiece and near the plasma membrane in the principal piece of the flagellum. Also found in the epididymosome, secreted by the epididymal epithelium and that transfers proteins from the epididymal fluid to the sperm surface.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000000882 | 2-357 | Sorbitol dehydrogenase | |||
Sequence: AAPAKGENLSLVVHGPGDIRLENYPIPELGPNDVLLKMHSVGICGSDVHYWEHGRIGDFVVKKPMVLGHEAAGTVTKVGELVKHLKPGDRVAIEPGVPREVDEYCKIGRYNLTPTIFFCATPPDDGNLCRFYKHNADFCYKLPDSVTFEEGALIEPLSVGIYACRRGSVSLGNKVLVCGAGPVGMVTLLVAKAMGAAQVVVTDLSASRLTKAKEVGADFTIQVGKETPQEIASKVESLLGSKPEVTIECTGAESSVQTGIYATHSGGTLVIVGMGAEMVNLPLVHAAIREVDIKGVFRYCNTWPMAISMLASKTLNVKPLVTHRFPLEKAVEAFETAKKGVGLKVMIKCDPNDQNP | ||||||
Modified residue | 169 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Testis has the highest level of expression, followed by kidney, liver, and lung. Low levels of expression are also observed in lens, brain, and skeletal muscle. Expressed in sperm flagellum and very low expression in the sperm head.
Developmental stage
Detected early in spermatogenesis. Detected in condensing spermatids (at protein level) and is up-regulated during late spermatogenesis.
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Length357
- Mass (Da)38,249
- Last updated2007-07-10 v3
- ChecksumFDAA462EF1EB6C21
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 49 | in Ref. 1; AAA79043 | ||||
Sequence: V → L | ||||||
Sequence conflict | 259 | in Ref. 1; AAA79043 | ||||
Sequence: T → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U27014 EMBL· GenBank· DDBJ | AAA79043.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK004692 EMBL· GenBank· DDBJ | BAB23478.1 EMBL· GenBank· DDBJ | mRNA | ||
AK015059 EMBL· GenBank· DDBJ | BAB29695.1 EMBL· GenBank· DDBJ | mRNA | ||
AK166988 EMBL· GenBank· DDBJ | BAE39168.1 EMBL· GenBank· DDBJ | mRNA | ||
AK166996 EMBL· GenBank· DDBJ | BAE39175.1 EMBL· GenBank· DDBJ | mRNA | ||
AL844566 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL844573 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC024124 EMBL· GenBank· DDBJ | AAH24124.1 EMBL· GenBank· DDBJ | mRNA | ||
BC030875 EMBL· GenBank· DDBJ | AAH30875.1 EMBL· GenBank· DDBJ | mRNA | ||
BC092291 EMBL· GenBank· DDBJ | AAH92291.1 EMBL· GenBank· DDBJ | mRNA |