Reviewed,
UniProtKB/Swiss-Prot P83402 (AL7A1_ACASC)
Last modified
November 25, 2008.
Version 31.
History...
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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: Alpha-aminoadipic semialdehyde dehydrogenase Short name=Alpha-AASA dehydrogenase EC=1.2.1.31 Alternative name(s): Delta1-piperideine-6-carboxylate dehydrogenease Short name=P6c dehydrogenase Aldehyde dehydrogenase family 7 member A1 Antiquitin-1 | ||
| Gene names |
| ||
| Organism | Acanthopagrus schlegeli (Black porgy) | ||
| Taxonomic identifier | 72011 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Neoteleostei › Acanthomorpha › Acanthopterygii › Percomorpha › Perciformes › Percoidei › Sparidae › Acanthopagrus |
Protein attributes
| Sequence length | 18 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | L-2-aminoadipate 6-semialdehyde + NAD(P)(+) + H(2)O = L-2-aminoadipate + NAD(P)H. |
| Subunit structure | Homotetramer. |
| Sequence similarities | Belongs to the aldehyde dehydrogenase family. |
| Biophysicochemical properties | Kinetic parameters: KM=2.0 mM for acetaldehyde Vmax=1.3 µmol/min/mg enzyme pH dependence: Optimum pH is 9-10. |
Ontologies
Keywords | |
|---|---|
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | cellular aldehyde metabolic process Ref.1 Inferred from direct assay. Source: UniProtKB oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | L-aminoadipate-semialdehyde dehydrogenase activity Inferred from electronic annotation. Source: EC aldehyde dehydrogenase (NAD) activity Ref.1Inferred from direct assay. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
References
| [1] | "First purification of the antiquitin protein and demonstration of its enzymatic activity." Tang W.-K., Cheng C.H.K., Fong W.-P. FEBS Lett. 516:183-186(2002) [PubMed: 11959129] [Abstract] Cited for: PROTEIN SEQUENCE, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT. Tissue: Liver. |
Cross-references
3D structure databases | |
|---|---|
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | P83402. |
Family and domain databases | |
| InterPro | IPR016160. Ald_DHase_CS. [Graphical view] |
| PROSITE | PS00070. ALDEHYDE_DEHYDR_CYS. Partial match. PS00687. ALDEHYDE_DEHYDR_GLU. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AL7A1_ACASC | ||||||||
| Accession | Primary (citable) accession number: P83402 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||

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