Reviewed,
UniProtKB/Swiss-Prot Q5R8A4 (AL9A1_PONAB)
Last modified
June 16, 2009.
Version 30.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
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 | 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 | 494 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 | 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 |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| 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_0000056488 | |||||
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 | ||||||
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 | |
|---|---|
| CR859849 mRNA. Translation: CAH92006.1. Different initiation. | |
| RefSeq | NP_001126165.1. |
| UniGene | Pab.13036 |
3D structure databases | |
| SMR | Q5R8A4. Positions 2-494. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 100173126. |
Phylogenomic databases | |
| HOVERGEN | Q5R8A4. |
Enzyme and pathway databases | |
| BRENDA | 1.2.1.3. 269192. 1.2.1.47. 269192. |
Family and domain databases | |
| InterPro | 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... |
Entry information
| Entry name | AL9A1_PONAB | ||||||||
| Accession | Primary (citable) accession number: Q5R8A4 | ||||||||
| 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


