A0AAE4ZDG9 · A0AAE4ZDG9_RHOHA
- ProteinDiaminopimelate decarboxylase
- GenelysA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids473 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.
Catalytic activity
- H+ + meso-2,6-diaminoheptanedioate = CO2 + L-lysine
Cofactor
Pathway
Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 283 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 325-328 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: EPGR | ||||||
Binding site | 328 | substrate | ||||
Sequence: R | ||||||
Binding site | 369 | substrate | ||||
Sequence: R | ||||||
Binding site | 373 | substrate | ||||
Sequence: Y | ||||||
Active site | 400 | Proton donor | ||||
Sequence: C | ||||||
Binding site | 401 | substrate | ||||
Sequence: E | ||||||
Binding site | 430 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 430 | substrate | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | diaminopimelate decarboxylase activity | |
Molecular Function | pyridoxal phosphate binding | |
Biological Process | lysine biosynthetic process via diaminopimelate |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDiaminopimelate decarboxylase
- EC number
- Short namesDAP decarboxylase ; DAPDC
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Nocardiaceae > Prescottella
Accessions
- Primary accessionA0AAE4ZDG9
Proteomes
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 97 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-29 | Disordered | ||||
Sequence: MNAHPAGPRHAEIQHAPGLPPRPATASEM | ||||||
Domain | 73-331 | Orn/DAP/Arg decarboxylase 2 N-terminal | ||||
Sequence: DDFRSRCREMARAFGGAERVHYASKAFLSAEIARWVRDEGLSMDVASGGELAVALHAGFPAERITMHGNNKSVAELDAAVAAGVGHIVLDSMVEIERLDEVAARRGVVQDVLIRITVGVEAHTHEFIATAHEDQKFGFSLSGGKAIAAVARVFETGNLRLVGLHSHIGSQIFEVDGFELAAHRVIGLMREIVDRFGAEKTSQLSMVDLGGGLGISYLPSDNPPPVAELAAKLAHIVATESAAAGLPVPTLMVEPGRAIA | ||||||
Domain | 337-428 | Orn/DAP/Arg decarboxylase 2 C-terminal | ||||
Sequence: TLYEVGTIKDVTLDAGATRRYVSVDGGMSDNIRTSLYQAEYDARLVSRDSDGAPVVARVVGKHCESGDIVIRDAWMPDDLGPGDLLAVAATG |
Sequence similarities
Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length473
- Mass (Da)50,302
- Last updated2024-05-29 v1
- Checksum93977D268BD2219A