Reviewed,
UniProtKB/Swiss-Prot Q5R5F3 (DHSO_PONAB)
Last modified
November 25, 2008.
Version 29.
History...
Clusters with 100%,
90%,
50% identity |
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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 | Pongo abelii (Sumatran orangutan) | ||
| Taxonomic identifier | 9601 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo |
Protein attributes
| Sequence length | 357 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Catalytic activity | L-iditol + NAD(+) = L-sorbose + NADH. |
| Cofactor | Binds 1 zinc ion per subunit By similarity. |
| Subunit structure | Homotetramer By similarity. |
| 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: InterPro |
| Molecular function | L-iditol 2-dehydrogenase activity Inferred from electronic annotation. Source: EC zinc ion bindingInferred from electronic annotation. Source: InterPro |
| 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 – 357 | 356 | Sorbitol dehydrogenase | PRO_0000301685 | |||||
Sites | |||||||||
| Metal binding | 45 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 70 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 71 | 1 | Zinc; catalytic By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||
Sequences
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References
| [1] | The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney. |
Cross-references
Sequence databases | |
|---|---|
| CR860908 mRNA. Translation: CAH93013.1. | |
| RefSeq | NP_001126780.1. |
3D structure databases | |
| SMR | Q5R5F3. Positions 2-357. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 100173784. |
Phylogenomic databases | |
| HOVERGEN | Q5R5F3. |
Family and domain databases | |
| InterPro | IPR013154. AlcDHase_GroES-like. IPR002085. AlcDHase_SF_Zn. IPR013149. AlcDHase_Zn-bd. IPR002328. AlcDHase_Zn_CS. [Graphical view] |
| PANTHER | PTHR11695. ADH_Sf_Zn. 1 hit. |
| Pfam | PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view] |
| PROSITE | PS00059. ADH_ZINC. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DHSO_PONAB | ||||||||
| Accession | Primary (citable) accession number: Q5R5F3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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