Reviewed,
UniProtKB/Swiss-Prot Q9JLJ2 (AL9A1_MOUSE)
Last modified
January 19, 2010.
Version 71.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 4-trimethylaminobutyraldehyde dehydrogenase Short name=TMABADH EC=1.2.1.47 Alternative name(s): Aldehyde dehydrogenase family 9 member A1 EC=1.2.1.3 | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 494 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Converts gamma-trimethylaminobutyraldehyde into gamma-butyrobetaine By similarity. |
| Catalytic activity | 4-trimethylammoniobutanal + NAD+ + H2O = 4-trimethylammoniobutanoate + NADH. An aldehyde + NAD+ + H2O = an acid + NADH. |
| Pathway | |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the aldehyde dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Acetylation |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | carnitine metabolic process Ref.1 Inferred from direct assay. Source: MGI oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytosol Ref.1 Inferred from direct assay. Source: MGI mitochondrionInferred from direct assay. Source: MGI |
| Molecular function | 4-trimethylammoniobutyraldehyde dehydrogenase activity Inferred from electronic annotation. Source: EC aldehyde dehydrogenase (NAD) activityInferred from electronic annotation. Source: EC |
| 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 – 494 | 493 | 4-trimethylaminobutyraldehyde dehydrogenase | PRO_0000056486 | |||||
Regions | |||||||||
| Nucleotide binding | 232 – 237 | 6 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 254 | 1 | Potential | ||||||
| Active site | 288 | 1 | Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylserine By similarity | ||||||
| Modified residue | 298 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Molecular and biochemical characterization of rat gamma-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis." Vaz F.M., Fouchier S.W., Ofman R., Sommer M., Wanders R.J.A. J. Biol. Chem. 275:7390-7394(2000) [PubMed: 10702312] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver. |
| [2] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary tumor. |
| [3] | Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 39-59; 74-82; 88-101; 228-239; 247-274; 317-338; 348-366; 412-426 AND 472-494, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF170919 mRNA. Translation: AAF43599.1. BC003297 mRNA. Translation: AAH03297.1. |
| IPI | IPI00124372. |
| RefSeq | NP_064377.2. |
| UniGene | Mm.330055 Mm.474999 |
3D structure databases | |
| SMR | Q9JLJ2. Positions 2-492. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q9JLJ2. |
PTM databases | |
| PhosphoSite | Q9JLJ2. |
2-D gel databases | |
| REPRODUCTION-2DPAGE | Q9JLJ2. |
Proteomic databases | |
| PRIDE | Q9JLJ2. |
Genome annotation databases | |
| Ensembl | ENSMUST00000028004; ENSMUSP00000028004; ENSMUSG00000026687; Mus musculus. [Genome view] |
| GeneID | 56752. |
| KEGG | mmu:56752. |
| NMPDR | fig|10090.3.peg.1427. |
| UCSC | uc007dkx.1. mouse. |
Organism-specific databases | |
| CTD | 56752. |
| MGI | MGI:1861622. Aldh9a1. |
Phylogenomic databases | |
| HOVERGEN | Q9JLJ2. |
| InParanoid | Q9JLJ2. |
| PhylomeDB | Q9JLJ2. |
Enzyme and pathway databases | |
| BRENDA | 1.2.1.3. 244. 1.2.1.47. 244. |
Gene expression databases | |
| ArrayExpress | Q9JLJ2. |
| Bgee | Q9JLJ2. |
| CleanEx | MM_ALDH9A1. |
| Genevestigator | Q9JLJ2. |
| GermOnline | ENSMUSG00000026687. Mus musculus. |
Family and domain databases | |
| InterPro | IPR016161. Ald_DH/histidinol_DH. IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH. [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... |
Other Resources | |
| SOURCE | Search... |
Entry information
| Entry name | AL9A1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q9JLJ2 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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