Reviewed,
UniProtKB/Swiss-Prot P49189 (AL9A1_HUMAN)
Last modified
November 25, 2008.
Version 79.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
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 Aldehyde dehydrogenase E3 isozyme Gamma-aminobutyraldehyde dehydrogenase EC=1.2.1.19 R-aminobutyraldehyde dehydrogenase | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
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. Catalyzes the irreversible oxidation of a broad range of aldehydes to the corresponding acids in an NAD-dependent reaction. |
| Catalytic activity | 4-trimethylammoniobutanal + NAD(+) + H(2)O = 4-trimethylammoniobutanoate + NADH. An aldehyde + NAD(+) + H(2)O = an acid + NADH. 4-aminobutanal + NAD(+) + H(2)O = 4-aminobutanoate + NADH. |
| Pathway | |
| Subunit structure | Homotetramer. |
| Subcellular location | CytoplasmBy similarity. |
| Tissue specificity | High expression in adult liver, skeletal muscle, and kidney. Low levels in heart, pancreas, lung and brain. Expressed in all regions of the brain. Expression levels are variable in the different brain areas, with the highest levels in the spinal cord and the lowest in the occipital pole. |
| Developmental stage | Strongly expressed in human embryonic brain (gestational age 12 weeks). |
| Post-translational modification | The N-terminus is blocked. |
| Sequence similarities | Belongs to the aldehyde dehydrogenase family. |
| Biophysicochemical properties | Kinetic parameters: KM=11 µM for 4-aminobutyraldehyde pH dependence: Optimum pH is about 9.4 with propionaldehyde as substrate, and 7.5 with 4-aminobutyraldehyde as substrate. |
Ontologies
Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Coding sequence diversity | Polymorphism |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Acetylation |
| Technical term | Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | cellular aldehyde metabolic process Ref.5 Inferred from direct assay. Source: UniProtKB hormone metabolic process Ref.7Traceable author statement. Source: UniProtKB neurotransmitter biosynthetic process Ref.7Inferred from direct assay. Source: UniProtKB oxidation reduction Ref.7Inferred from direct assay. Source: UniProtKB |
| Cellular component | cytoskeleton Inferred from direct assay. Source: HPA nucleusInferred from direct assay. Source: HPA |
| Molecular function | 4-trimethylammoniobutyraldehyde dehydrogenase activity Inferred from electronic annotation. Source: EC aldehyde dehydrogenase (NAD) activity Ref.7Inferred from direct assay. Source: UniProtKB aminobutyraldehyde dehydrogenase activity Ref.5 Ref.7Inferred from direct assay. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed | ||||||
| Chain | 2 – 494 | 493 | 4-trimethylaminobutyraldehyde dehydrogenase | PRO_0000056485 | |||||
Regions | |||||||||
| Nucleotide binding | 232 – 237 | 6 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 254 | 1 | Proton acceptor By similarity | ||||||
| Active site | 288 | 1 | Nucleophile By similarity | ||||||
| Site | 157 | 1 | Transition state stabilizer By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylserine | ||||||
Natural variations | |||||||||
| Natural variant | 116 | 1 | C → S in allele ALDH9A1*2. | VAR_011304 | |||||
Experimental info | |||||||||
| Sequence conflict | 19 – 25 | 7 | RVEPADA → AGAGGR in AAB18827. Ref.1 | ||||||
| Sequence conflict | 150 | 1 | C → Q AA sequence Ref.6 | ||||||
| Sequence conflict | 159 | 1 | P → W AA sequence Ref.6 | ||||||
| Sequence conflict | 172 | 1 | A → R AA sequence Ref.6 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Human gamma-aminobutyraldehyde dehydrogenase (ALDH9): cDNA sequence, genomic organization, polymorphism, chromosomal localization, and tissue expression." Lin S.W., Chen J.C., Hsu L.C., Hsieh C.-L., Yoshida A. Genomics 34:376-380(1996) [PubMed: 8786138] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-116. Tissue: Liver. |
| [2] | "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], FUNCTION. Tissue: Liver. |
| [3] | "The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. Bentley D.R.Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [4] | Bienvenut W.V., Heiserich L., Gottlieb E. Submitted (MAR-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-15; 247-258; 299-310; 315-326 AND 472-481, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY. Tissue: Colon carcinoma. |
| [5] | "Aldehyde dehydrogenase from adult human brain that dehydrogenates gamma-aminobutyraldehyde: purification, characterization, cloning and distribution." Kikonyogo A., Pietruszko R. Biochem. J. 316:317-324(1996) [PubMed: 8645224] [Abstract] Cited for: PROTEIN SEQUENCE OF 259-274; 353-366; 412-426 AND 434-453, NUCLEOTIDE SEQUENCE [MRNA] OF 29-494, CHARACTERIZATION, TISSUE SPECIFICITY, VARIANT SER-116. Tissue: Brain. |
| [6] | "Human aldehyde dehydrogenase. cDNA cloning and primary structure of the enzyme that catalyzes dehydrogenation of 4-aminobutyraldehyde." Kurys G., Shah P.C., Kikonyogo A., Reed D., Ambroziak W., Pietruszko R. Eur. J. Biochem. 218:311-320(1993) [PubMed: 8269919] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-494, PARTIAL PROTEIN SEQUENCE. |
| [7] | "Human aldehyde dehydrogenase. Purification and characterization of a third isozyme with low Km for gamma-aminobutyraldehyde." Kurys G., Ambroziak W., Pietruszko R. J. Biol. Chem. 264:4715-4721(1989) [PubMed: 2925663] [Abstract] Cited for: CHARACTERIZATION. Tissue: Liver. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| U34252 mRNA. Translation: AAB18827.1. AF172093 mRNA. Translation: AAF43600.1. AL451074 Genomic DNA. Translation: CAH74061.1. Different initiation. U50203 mRNA. Translation: AAB06721.1. X75425 mRNA. Translation: CAA53176.1. | |
| PIR | S39532. G02054. |
| RefSeq | NP_000687.3. |
| UniGene | Hs.2533 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1A4S based on UniProtKB P56533. |
| SMR | P49189. Positions 2-494. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P49189. |
PTM databases | |
| PhosphoSite | P49189. |
2-D gel databases | |
| REPRODUCTION-2DPAGE | IPI00479877. |
Genome annotation databases | |
| Ensembl | ENSG00000143149. Homo sapiens. [Contig view] |
| GeneID | 223. |
| KEGG | hsa:223. |
Organism-specific databases | |
| H-InvDB | HIX0001281. |
| HGNC | HGNC:412. ALDH9A1. |
| HPA | HPA006077. HPA010873. |
| MIM | 602733. gene. |
| PharmGKB | PA24706. |
| GenAtlas | Search... |
| GeneCards | Search... |
Phylogenomic databases | |
| HOGENOM | P49189. |
| HOVERGEN | P49189. |
Gene expression databases | |
| CleanEx | HS_ALDH9A1. |
| GermOnline | ENSG00000143149. Homo sapiens. |
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... |
Other Resources | |
| DrugBank | DB00157. NADH. |
| NextBio | 906. |
| SOURCE | Search... |
Entry information
| Entry name | AL9A1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P49189 Secondary accession number(s): Q5VV90, Q6LCL1, Q9NZT7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 1 Human chromosome 1: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


