A0A7I6H9J8 · A0A7I6H9J8_ECOHS
- ProteinDiaminopimelate decarboxylase
- GenelysA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids420 (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 | 227 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 268-271 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: EPGR | ||||||
Binding site | 271 | substrate | ||||
Sequence: R | ||||||
Binding site | 307 | substrate | ||||
Sequence: R | ||||||
Binding site | 311 | substrate | ||||
Sequence: Y | ||||||
Active site | 342 | Proton donor | ||||
Sequence: C | ||||||
Binding site | 343 | substrate | ||||
Sequence: E | ||||||
Binding site | 378 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 378 | 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 > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionA0A7I6H9J8
Proteomes
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 54 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 33-275 | Orn/DAP/Arg decarboxylase 2 N-terminal | ||||
Sequence: AQIIRRQIAALKQFDVVRFAQKACSNIHILRLMREQGVKVDSVSLGEIERALAAGYNPQTHPDDIVFTADVIDQATLERVSELQIPVNAGSVDMLDQLGQVSPGHRVWLRVNPGFGHGHSQKTNTGGENSKHGIWYTDLPAALDVIQRHHLQLVGIHMHIGSGVDYAHLEQVCGAMVRQVIEFGQDLQAISAGGGLSVPYQQGEEAVDTEHYYGLWNAAREQIARHLGHPVKLEIEPGRFLVA | ||||||
Domain | 276-376 | Orn/DAP/Arg decarboxylase 2 C-terminal | ||||
Sequence: QSGVLITQVRSVKQMGSRHFVLVDAGFNDLMRPAMYGSYHHISALAADGRSLEHAPTVETVVAGPLCESGDVFTQQEGGNVETRALPEVKAGDYLVLHDTG |
Sequence similarities
Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length420
- Mass (Da)46,177
- Last updated2021-04-07 v1
- Checksum0A26ABCFAF8462B5
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000802 EMBL· GenBank· DDBJ | ABV07226.1 EMBL· GenBank· DDBJ | Genomic DNA |