A0A517XKZ6 · A0A517XKZ6_9BACT
- ProteinAspartate-semialdehyde dehydrogenase
- Geneasd2
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids338 (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 | 11-14 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 39-40 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 99 | phosphate (UniProtKB | ChEBI) | |||
Active site | 129 | Acyl-thioester intermediate | |||
Binding site | 156 | substrate | |||
Binding site | 159-160 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 181 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 210 | substrate | |||
Binding site | 236 | substrate | |||
Active site | 243 | Proton acceptor | |||
Binding site | 315 | 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 > Planctomycetota > Planctomycetia > Gemmatales > Gemmataceae > Urbifossiella
Accessions
- Primary accessionA0A517XKZ6
Proteomes
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length338
- Mass (Da)35,390
- Last updated2019-10-16 v1
- ChecksumB5BA42BB10D5CD71
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP036273 EMBL· GenBank· DDBJ | QDU18181.1 EMBL· GenBank· DDBJ | Genomic DNA |