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Reviewed, UniProtKB/Swiss-Prot P07846 (DHSO_SHEEP)

Last modified June 16, 2009. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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)
Taxonomic identifier9940 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Caprinae › Ovis

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Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

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Ontologies

Keywords
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionL-iditol 2-dehydrogenase activity

Inferred from direct assay. Source: UniProtKB

zinc ion binding

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 354354Sorbitol dehydrogenase
PRO_0000160819

Sites

Metal binding431Zinc; catalytic By similarity
Metal binding671Zinc; catalytic By similarity
Metal binding681Zinc; catalytic By similarity

Amino acid modifications

Modified residue11N-acetylalanine

Secondary structure

1 ..................................................................... 354
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P07846-1 [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

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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: 6705798] [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: 6368230] [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: 2936393] [Abstract]
Cited for: 3D-STRUCTURE MODELING.

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Cross-references

Sequence databases

PIRS10065.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1SDGmodel-A1-347[»]
SMRP07846. Positions 1-354.
ModBaseSearch...

Phylogenomic databases

HOVERGENP07846.

Enzyme and pathway databases

BRENDA1.1.1.14. 271.

Family and domain databases

InterProIPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR002328. ADH_Zn_CS.
[Graphical view]
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

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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: June 16, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents