Reviewed,
UniProtKB/Swiss-Prot Q2XQV4 (ALDH2_PIG)
Last modified
November 4, 2008.
Version 24.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Aldehyde dehydrogenase, mitochondrial EC=1.2.1.3 Alternative name(s): ALDH class 2 ALDH-E2 | ||
| 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 | 521 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)
| Function | Is capable of converting retinaldehyde to retinoic acid By similarity. |
| Catalytic activity | An aldehyde + NAD(+) + H(2)O = an acid + NADH. |
| Pathway | Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | Mitochondrion matrixBy similarity. |
| Sequence similarities | Belongs to the aldehyde dehydrogenase family. |
Ontologies
Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Acetylation |
Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | aldehyde dehydrogenase (NAD) activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 21 | 21 | Mitochondrion By similarity | ||||||
| Chain | 22 – 521 | 500 | Aldehyde dehydrogenase, mitochondrial | PRO_0000312492 | |||||
Regions | |||||||||
| Nucleotide binding | 266 – 271 | 6 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 289 | 1 | Proton acceptor By similarity | ||||||
| Active site | 323 | 1 | Nucleophile By similarity | ||||||
| Site | 190 | 1 | Transition state stabilizer By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 22 | 1 | N-acetylserine By similarity | ||||||
| Modified residue | 372 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| [1] | Ji Y., Bennett B.M. Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| DQ266356 mRNA. Translation: ABB70228.1. | |
| RefSeq | NP_001038076.1. |
| UniGene | Ssc.11147 |
3D structure databases | |
| SMR | Q2XQV4. Positions 28-521. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 733685. |
| KEGG | ssc:733685. |
Phylogenomic databases | |
| HOVERGEN | Q2XQV4. |
Family and domain databases | |
| InterPro | IPR016160. Ald_DHase_CS. IPR016162. Ald_DHase_N. IPR015590. Aldehyde_DHase. [Graphical view] |
| Gene3D | G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit. |
| PANTHER | PTHR11699. Aldehyde_dehyd. 1 hit. |
| Pfam | PF00171. Aldedh. 1 hit. [Graphical view] |
| PROSITE | PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ALDH2_PIG | ||||||||
| Accession | Primary (citable) accession number: Q2XQV4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


