A0A0M2UQQ7 · A0A0M2UQQ7_9BACT
- ProteinDiaminopimelate decarboxylase
- GenelysA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids430 (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 | 239 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 273-276 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: EPGR | ||||||
Binding site | 276 | substrate | ||||
Sequence: R | ||||||
Binding site | 313 | substrate | ||||
Sequence: R | ||||||
Binding site | 317 | substrate | ||||
Sequence: Y | ||||||
Active site | 357 | Proton donor | ||||
Sequence: C | ||||||
Binding site | 358 | substrate | ||||
Sequence: E | ||||||
Binding site | 386 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 386 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Planctomycetota > Candidatus Brocadiia > Candidatus Brocadiales > Candidatus Brocadiaceae > Candidatus Brocadia
Accessions
- Primary accessionA0A0M2UQQ7
Proteomes
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 60 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 36-279 | Orn/DAP/Arg decarboxylase 2 N-terminal | ||||
Sequence: AILARYHELKAAFGDVDSLICFSVKSNSNLSLCKILAEAGSGFDVVSGGELFRTIKAGGDPSKIVFAGVGKTDGEIRDALANDIFMFNVESLAELEHIDRLARDVGKVAKVALRINPDIDAKTHAKTTTGKKENKFGIDFTEAEGLIKQSSRYPGIELCGLHVHLGSPIYTVDPYVNALRKIIKLIEKCRDAGLDIEYMNIGGGYCISYTGEEVIRPRDYASKILPLVKEMQCNLLMEPGRFIT | ||||||
Domain | 280-384 | Orn/DAP/Arg decarboxylase 2 C-terminal | ||||
Sequence: GNSGILITRVTYTKETVHGKKFIICDAAMNDLLRPALYDAFHRIWPVTTGIPMPKVEEPEKAAVKKGTELVDIVGPVCESSDVFASKRALPKVGEGDLLAIFSAG |
Sequence similarities
Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length430
- Mass (Da)47,573
- Last updated2015-11-11 v1
- Checksum2F9172289A7FC3DD
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LAQJ01000270 EMBL· GenBank· DDBJ | KKO18428.1 EMBL· GenBank· DDBJ | Genomic DNA |