P00861 · DCDA_ECOLI
- ProteinDiaminopimelate decarboxylase
- GenelysA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids420 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine. Is not active against the DD- or LL-isomers of diaminopimelate.
Catalytic activity
- H+ + meso-2,6-diaminoheptanedioate = CO2 + L-lysine
Cofactor
Activity regulation
Is activated by 2,3-dimercaptopropan-1-ol.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1.7 mM | meso-2,6-diaminoheptanedioate | 6.8 | 37 | |||
1.07 mM | meso-2,6-diaminoheptanedioate | 8 |
pH Dependence
Optimum pH is 6.7-6.8.
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 | 191 | substrate | ||||
Sequence: H | ||||||
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 | protein homodimerization 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
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP00861
- Secondary accessions
Proteomes
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000149923 | 1-420 | Diaminopimelate decarboxylase | |||
Sequence: MPHSLFSTDTDLTAENLLRLPAEFGCPVWVYDAQIIRRQIAALKQFDVVRFAQKACSNIHILRLMREQGVKVDSVSLGEIERALAAGYNPQTHPDDIVFTADVIDQATLERVSELQIPVNAGSVDMLDQLGQVSPGHRVWLRVNPGFGHGHSQKTNTGGENSKHGIWYTDLPAALDVIQRHHLQLVGIHMHIGSGVDYAHLEQVCGAMVRQVIEFGQDLQAISAGGGLSVPYQQGEEAVDTEHYYGLWNAAREQIARHLGHPVKLEIEPGRFLVAQSGVLITQVRSVKQMGSRHFVLVDAGFNDLMRPAMYGSYHHISALAADGRSLEHAPTVETVVAGPLCESGDVFTQQEGGNVETRALPEVKAGDYLVLHDTGAYGASMSSNYNSRPLLPEVLFDNGQARLIRRRQTIEELLALELL | ||||||
Modified residue | 54 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Proteomic databases
Expression
Induction
Up-regulated by LysR. Repressed in the presence of lysine.
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P00861 | cpxR P0AE88 | 4 | EBI-553837, EBI-550918 |
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length420
- Mass (Da)46,177
- Last updated1986-07-21 v1
- Checksum0A26ABCFAF8462B5
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J01614 EMBL· GenBank· DDBJ | AAA83861.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U29581 EMBL· GenBank· DDBJ | AAB40485.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC75877.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE76907.1 EMBL· GenBank· DDBJ | Genomic DNA |