A0A1B4ZDL9 · A0A1B4ZDL9_9ACTN
- Protein2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase
- GenedapD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids327 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the conversion of the cyclic tetrahydrodipicolinate (THDP) into the acyclic N-succinyl-L-2-amino-6-oxopimelate using succinyl-CoA.
Catalytic activity
- (S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = (S)-2-succinylamino-6-oxoheptanedioate + CoA
Pathway
Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 175 | Mg2+ 1 (UniProtKB | ChEBI); ligand shared between trimeric partners | ||||
Sequence: D | ||||||
Binding site | 192 | Mg2+ 2 (UniProtKB | ChEBI); ligand shared between trimeric partners | ||||
Sequence: E | ||||||
Active site | 208 | Acyl-anhydride intermediate | ||||
Sequence: E | ||||||
Binding site | 210 | succinyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 225 | succinyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 228 | succinyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 251 | succinyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 266-267 | succinyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: EA | ||||||
Binding site | 274 | succinyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 286 | succinyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 299-302 | succinyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: RRNS |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase activity | |
Molecular Function | magnesium 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 name2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces
Accessions
- Primary accessionA0A1B4ZDL9
Subcellular Location
Interaction
Subunit
Homotrimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 119-159 | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase middle | ||||
Sequence: LANVAWTSLGPVAVDDVEKVRLNARAEGLHLQVTSIDKFPR |
Sequence similarities
Belongs to the type 2 tetrahydrodipicolinate N-succinyltransferase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length327
- Mass (Da)33,642
- Last updated2016-11-02 v1
- Checksum17CBD8641DB63715