A0A7X4X369 · A0A7X4X369_9VIBR
- Protein2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase
- GenedapD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids343 (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 | 204 | Mg2+ 2 (UniProtKB | ChEBI); ligand shared between trimeric partners | ||||
Sequence: E | ||||||
Active site | 220 | Acyl-anhydride intermediate | ||||
Sequence: E | ||||||
Binding site | 222 | succinyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 237 | succinyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 240 | succinyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 263 | succinyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 278-279 | succinyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: ES | ||||||
Binding site | 286 | succinyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 303 | succinyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 316-319 | 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 > Pseudomonadota > Gammaproteobacteria > Vibrionales > Vibrionaceae > Vibrio
Accessions
- Primary accessionA0A7X4X369
Proteomes
Subcellular Location
Interaction
Subunit
Homotrimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 131-171 | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase middle | ||||
Sequence: LHNIAWTNEGPIDLPELAERQIDARLAGRSLSVDCVDKFPK |
Sequence similarities
Belongs to the type 2 tetrahydrodipicolinate N-succinyltransferase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length343
- Mass (Da)35,756
- Last updated2021-06-02 v1
- Checksum3ADB664548BDC106