A0A1G7V900 · A0A1G7V900_9GAMM
- ProteinAspartate-semialdehyde dehydrogenase
- Geneasd
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids370 (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 + NADP+ + phosphate = 4-phospho-L-aspartate + H+ + NADPH
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 | 10-13 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: RGMV | ||||||
Binding site | 37-38 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: TS | ||||||
Binding site | 73 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 102 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 135 | Acyl-thioester intermediate | ||||
Sequence: C | ||||||
Binding site | 162 | substrate | ||||
Sequence: Q | ||||||
Binding site | 165-166 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SG | ||||||
Binding site | 241 | substrate | ||||
Sequence: E | ||||||
Binding site | 244 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 268 | substrate | ||||
Sequence: R | ||||||
Active site | 275 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 351 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: Q |
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 > Pseudomonadota > Gammaproteobacteria > Oceanospirillales > Halomonadaceae > Onishia
Accessions
- Primary accessionA0A1G7V900
Proteomes
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-122 | Semialdehyde dehydrogenase NAD-binding | ||||
Sequence: TVGFVGWRGMVGSVLMQRMQEDNEFVGIEPVFFTTSQVGQPGPDIGVDVPPLKDAFDLDALKALDVIVTCQGGDYTEKVYKDLRQTGWKGYWVDAASTLRMADDATIVLDPVNRDVIDAQ |
Sequence similarities
Belongs to the aspartate-semialdehyde dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length370
- Mass (Da)40,192
- Last updated2017-11-22 v1
- Checksum60DEA531B105646F
Keywords
- Technical term