F9UP74 · F9UP74_LACPL
- ProteinDiaminopimelate decarboxylase
- GenelysA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids441 (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 | 249 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 291-294 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: EPGR | ||||||
Binding site | 294 | substrate | ||||
Sequence: R | ||||||
Binding site | 331 | substrate | ||||
Sequence: R | ||||||
Binding site | 335 | substrate | ||||
Sequence: Y | ||||||
Active site | 362 | Proton donor | ||||
Sequence: C | ||||||
Binding site | 363 | substrate | ||||
Sequence: E | ||||||
Binding site | 391 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 391 | 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 > Bacillota > Bacilli > Lactobacillales > Lactobacillaceae > Lactiplantibacillus
Accessions
- Primary accessionF9UP74
Proteomes
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 67 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 41-298 | Orn/DAP/Arg decarboxylase 2 N-terminal | ||||
Sequence: AIRAEIAAFKQVFEENHVDYQISYASKAFATVAMYQLIAQEHIHCDVVSGGELYTAQQADFPMAAVSFHGNNKSLAELTMALDAGVGTIVVDNFGELRQLTTLTTQRQQPTTIMLRIAPGISAHTHDYISTGQADSKFGFDLDSGQADQAIKAAQAAPYLKLVGIHCHIGSQIFEVNGFEMIVDKLVSEFARWQRELDFYPQIMNVGGGFGVKYTAEDHPLQPTDFVDAIIKETRAQTAAQQVPMLEIWIEPGRSLVA | ||||||
Domain | 299-389 | Orn/DAP/Arg decarboxylase 2 C-terminal | ||||
Sequence: TAGMTLYTIGDEKDIPGIRKYLSVDGGMGDNIRPALYQAKYEAVLAKNPALPAEQVASIAGKYCESGDMLIWNQQLPATAPGDVLAVLDTG |
Sequence similarities
Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length441
- Mass (Da)48,264
- Last updated2011-10-19 v1
- Checksum7B22B6A290EA7A2E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL935263 EMBL· GenBank· DDBJ | CCC79013.1 EMBL· GenBank· DDBJ | Genomic DNA |