Reviewed,
UniProtKB/Swiss-Prot Q29318 (DHSO_PIG)
Last modified
June 16, 2009.
Version 50.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Sorbitol dehydrogenase EC=1.1.1.14 Alternative name(s): L-iditol 2-dehydrogenase | ||
| Gene names |
| ||
| Organism | Sus scrofa (Pig) | ||
| Taxonomic identifier | 9823 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus |
Protein attributes
| Sequence length | 97 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | L-iditol + NAD+ = L-sorbose + NADH. UniProtKB P07846 |
| Cofactor | Binds 1 zinc ion per subunit By similarity. UniProtKB P07846 |
| Subunit structure | Homotetramer By similarity. UniProtKB P07846 |
| Sequence similarities | Belongs to the zinc-containing alcohol dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Metal-binding NAD Zinc |
| Molecular function | Oxidoreductase |
| PTM | Acetylation |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | L-iditol 2-dehydrogenase activity Inferred from electronic annotation. Source: EC zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – ›97 | ›96 | Sorbitol dehydrogenase | PRO_0000160818 | |||||
Sites | |||||||||
| Metal binding | 44 | 1 | Zinc; catalytic By similarity UniProtKB P07846 | ||||||
| Metal binding | 69 | 1 | Zinc; catalytic By similarity UniProtKB P07846 | ||||||
| Metal binding | 70 | 1 | Zinc; catalytic By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||
Experimental info | |||||||||
| Non-terminal residue | 97 | 1 | |||||||
Sequences
References
| [1] | "Evaluation and characterization of a porcine small intestine cDNA library: analysis of 839 clones." Winteroe A.K., Fredholm M., Davies W. Mamm. Genome 7:509-517(1996) [PubMed: 8672129] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Small intestine. |
Cross-references
Sequence databases | |
|---|---|
| F14714 mRNA. Translation: CAA23205.1. | |
3D structure databases | |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | Q29318. |
Enzyme and pathway databases | |
| BRENDA | 1.1.1.14. 249. |
Family and domain databases | |
| InterPro | IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn. IPR002328. ADH_Zn_CS. [Graphical view] |
| PANTHER | PTHR11695. ADH_Sf_Zn. 1 hit. |
| Pfam | PF08240. ADH_N. 1 hit. [Graphical view] |
| PROSITE | PS00059. ADH_ZINC. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DHSO_PIG | ||||||||
| Accession | Primary (citable) accession number: Q29318 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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