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P07846 (DHSO_SHEEP) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sorbitol dehydrogenase

EC=1.1.1.14
Alternative name(s):
L-iditol 2-dehydrogenase
Gene names
Name:SORD
OrganismOvis aries (Sheep) [Reference proteome]
Taxonomic identifier9940 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis

Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Converts sorbitol to fructose. Part of the polyol pathway that plays an important role in sperm physiology. May play a role in the sperm motility by providing an energetic source for sperm By similarity.

Catalytic activity

L-iditol + NAD+ = L-sorbose + NADH.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Homotetramer. Ref.4

Subcellular location

Mitochondrion membrane; Peripheral membrane protein. Cell projectionciliumflagellum. 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 By similarity.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 354354Sorbitol dehydrogenase
PRO_0000160819

Sites

Metal binding431Zinc; catalytic
Metal binding671Zinc; catalytic
Metal binding681Zinc; catalytic
Binding site491Substrate
Binding site1531Substrate
Binding site2961Substrate
Binding site2971Substrate

Amino acid modifications

Modified residue11N-acetylalanine

Secondary structure

......................................................... 354
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07846 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: D5FE56BC06F87389

FASTA35437,831
        10         20         30         40         50         60 
AKPAAENLSL VVHGPGDLRL ENYPIPEPGP NEVLLKMHSV GICGSDVHYW QGRIGDFVVK 

        70         80         90        100        110        120 
KPMVLGHEAS GTVVKVGSLV RHLQPGDRVA IQPGAPRQTD EFCKIGRYNL SPTIFFCATP 

       130        140        150        160        170        180 
PDDGNLCRFY KHNANFCYKL PDNVTFEEGA LIEPLSVGIH ACRRAGVTLG NKVLVCGAGP 

       190        200        210        220        230        240 
IGLVNLLAAK AMGAAQVVVT DLSASRLSKA KEVGADFILE ISNESPEEIA KKVEGLLGSK 

       250        260        270        280        290        300 
PEVTIECTGV ETSIQAGIYA THSGGTLVLV GLGSEMTSVP LVHAATREVD IKGVFRYCNT 

       310        320        330        340        350 
WPMAISMLAS KSVNVKPLVT HRFPLEKALE AFETSKKGLG LKVMIKCDPS DQNP 

« Hide

References

[1]"Sorbitol dehydrogenase. The primary structure of the sheep-liver enzyme."
Jeffery J., Cederlund E., Joernvall H.
Eur. J. Biochem. 140:7-16(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Liver.
[2]"Extensive variations and basic features in the alcohol dehydrogenase-sorbitol dehydrogenase family."
Joernvall H., von Bahr-Lindstroem H., Jeffery J.
Eur. J. Biochem. 140:17-23(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: SIMILARITY TO ZINC ALCOHOL DEHYDROGENASES.
[3]"Molecular aspects of functional differences between alcohol and sorbitol dehydrogenases."
Eklund H., Horjales E., Joernvall H., Branden C.I., Jeffery J.
Biochemistry 24:8005-8012(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[4]"X-ray crystal structure and small-angle X-ray scattering of sheep liver sorbitol dehydrogenase."
Yennawar H., Moller M., Gillilan R., Yennawar N.
Acta Crystallogr. D 67:440-446(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, SUBUNIT, ZINC-BINDING SITES, SUBSTRATE-BINDING SITES, ENZYME MECHANISM.

Cross-references

Sequence databases

PIRS10065.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SDGmodel-A1-347[»]
3QE3X-ray1.90A1-354[»]
ProteinModelPortalP07846.
SMRP07846. Positions 1-354.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL1075154.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG005484.

Enzyme and pathway databases

SABIO-RKP07846.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11695. PTHR11695. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. SSF50129. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07846.

Entry information

Entry nameDHSO_SHEEP
AccessionPrimary (citable) accession number: P07846
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: July 9, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references