A0A5R9BZT0 · A0A5R9BZT0_9LACO
- ProteinAspartate-semialdehyde dehydrogenase
- Geneasd
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids349 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.
Catalytic activity
- L-aspartate 4-semialdehyde + phosphate + NADP+ = 4-phospho-L-aspartate + NADPH + H+
Pathway
Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4.
Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3.
Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 12-15 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 40-41 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 100 | phosphate (UniProtKB | ChEBI) | |||
Active site | 129 | Acyl-thioester intermediate | |||
Binding site | 156 | substrate | |||
Binding site | 159-160 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 246 | substrate | |||
Active site | 253 | Proton acceptor | |||
Binding site | 326 | NADP+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | aspartate-semialdehyde dehydrogenase activity | |
Molecular Function | NAD binding | |
Molecular Function | NADP binding | |
Molecular Function | protein dimerization activity | |
Biological Process | 'de novo' L-methionine biosynthetic process | |
Biological Process | diaminopimelate biosynthetic process | |
Biological Process | isoleucine biosynthetic process | |
Biological Process | lysine biosynthetic process via diaminopimelate | |
Biological Process | threonine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAspartate-semialdehyde dehydrogenase
- EC number
- Short namesASA dehydrogenase ; ASADH
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Lactobacillaceae > Pediococcus
Accessions
- Primary accessionA0A5R9BZT0
Proteomes
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 5-120 | Semialdehyde dehydrogenase NAD-binding | |||
Sequence similarities
Belongs to the aspartate-semialdehyde dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length349
- Mass (Da)38,001
- Last updated2020-02-26 v1
- MD5 Checksum511C3578FB58C2EDCB747B33E83BD263
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
VBTH01000001 EMBL· GenBank· DDBJ | TLQ05742.1 EMBL· GenBank· DDBJ | Genomic DNA |