A0A263NWF7 · A0A263NWF7_9PSED
- ProteinSuccinyl-diaminopimelate desuccinylase
- GenedapE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids383 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls.
Catalytic activity
- H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-diaminoheptanedioate + succinate
Cofactor
Co2+ (UniProtKB | Rhea| CHEBI:48828 )
Note: Binds 2 Zn2+ or Co2+ ions per subunit.
Pathway
Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 3/3.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 73 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 75 | |||||
Sequence: D | ||||||
Binding site | 107 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 107 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 141 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 142 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 170 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 356 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | cobalt ion binding | |
Molecular Function | succinyl-diaminopimelate desuccinylase activity | |
Molecular Function | zinc ion binding | |
Biological Process | diaminopimelate biosynthetic process | |
Biological Process | lysine biosynthetic process via diaminopimelate |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSuccinyl-diaminopimelate desuccinylase
- EC number
- Short namesSDAP desuccinylase
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionA0A263NWF7
Proteomes
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 183-290 | Peptidase M20 dimerisation | ||||
Sequence: NGRRGSLGATLTVRGVQGHVAYPHLAKNPIHLAAPALAELAAEHWDDGNTFFPPTSFQISNLNSGTGATNVIPGDLTAVFNFRFSTESTVEGLQQRVAAILDKHGLDW |
Sequence similarities
Belongs to the peptidase M20A family. DapE subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length383
- Mass (Da)41,012
- Last updated2017-12-20 v1
- Checksum1C1C00B9B1E2758A