A0A853G8X4 · A0A853G8X4_9GAMM
- ProteinDiaminopimelate decarboxylase
- GenelysA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids413 (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
- meso-2,6-diaminoheptanedioate + H+ = L-lysine + CO2
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 | 238 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 270-273 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: EPGR | ||||||
Binding site | 273 | substrate | ||||
Sequence: R | ||||||
Binding site | 309 | substrate | ||||
Sequence: R | ||||||
Binding site | 313 | substrate | ||||
Sequence: Y | ||||||
Active site | 340 | Proton donor | ||||
Sequence: C | ||||||
Binding site | 341 | substrate | ||||
Sequence: E | ||||||
Binding site | 368 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 368 | 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 > sulfur-oxidizing symbionts > Candidatus Vesicomyosocius
Accessions
- Primary accessionA0A853G8X4
Proteomes
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 59 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 35-277 | Orn/DAP/Arg decarboxylase 2 N-terminal | ||||
Sequence: DIEYNWHLFSHAFGIHPHLVCYAVKANSNLAVLSVLAKIGSGFDVVSNGELERVLLAGADASRCVFSGVAKTNIEIKRALEVGIFCFNVESMAEMSRIEQVAKEMSMQAPISLRVNPDVDPKTHPYISTGLKENKFGVDIDDAIPIYKMAYNSPYLKVKGIDCHIGSQLTKISPFLDALDKVLELVAKLGKLNIHVTHLDLGGGVGIKYDNEQTIDINAYISSILDKVGSLKIILEPGRAIVG | ||||||
Domain | 278-366 | Orn/DAP/Arg decarboxylase 2 C-terminal | ||||
Sequence: NAGIFVTKVEFLKQNSDKSFAIIDGAMNDLLRPSFYQAYHQVLPIDENAEGIDAHWDLVGPICETGDFLAKNRRLSLSEGDYLALMSAG |
Sequence similarities
Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length413
- Mass (Da)45,631
- Last updated2021-09-29 v1
- Checksum68263C84A2F36F31