Reviewed,
UniProtKB/Swiss-Prot P83049 (XYL2_PIG)
Last modified
November 4, 2008.
Version 25.
History...
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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: D-xylulose reductase EC=1.1.1.9 Alternative name(s): Xylitol dehydrogenase Short name=XDH |
| 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 | 134 AA. |
| Sequence status | Fragments. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | Xylitol + NAD(+) = D-xylulose + NADH. |
| Enzyme regulation | Activated by calcium and inhibited by zinc. |
| Sequence similarities | Belongs to the zinc-containing alcohol dehydrogenase family. |
Ontologies
Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Xylose metabolism |
| Ligand | Metal-binding NAD Zinc |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | D-xylose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | D-xylulose reductase 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – ›134 | ›134 | D-xylulose reductase | PRO_0000160882 | |||||
Experimental info | |||||||||
| Non-adjacent residues | 21 – 22 | 2 | |||||||
| Non-adjacent residues | 37 – 38 | 2 | |||||||
| Non-adjacent residues | 44 – 45 | 2 | |||||||
| Non-adjacent residues | 55 – 56 | 2 | |||||||
| Non-adjacent residues | 68 – 69 | 2 | |||||||
| Non-adjacent residues | 76 – 77 | 2 | |||||||
| Non-adjacent residues | 80 – 81 | 2 | |||||||
| Non-adjacent residues | 92 – 93 | 2 | |||||||
| Non-adjacent residues | 110 – 111 | 2 | |||||||
| Non-adjacent residues | 128 – 129 | 2 | |||||||
| Non-terminal residue | 134 | 1 | |||||||
Sequences
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References
| [1] | "Xylitol:NAD 2-oxidoreductase (D-xylulose reductase EC 1.1.1.9) from porcine kidney. Purification and properties." Schweiger M., Wissler J.H., Amselgruber W.M. Submitted (JUL-2001) to UniProtKB Cited for: PROTEIN SEQUENCE, COFACTOR, ENZYME REGULATION. Tissue: Kidney. |
Cross-references
3D structure databases | |
|---|---|
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | P83049. |
Family and domain databases | |
| InterPro | IPR002328. AlcDHase_Zn_CS. [Graphical view] |
| PROSITE | PS00059. ADH_ZINC. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | XYL2_PIG | ||||||||
| Accession | Primary (citable) accession number: P83049 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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