A0A7Y5YNI3 · A0A7Y5YNI3_9PSED

  • Protein
    Diaminopimelate decarboxylase
  • Gene
    lysA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

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
IDPosition(s)Description
Binding site239pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site273-276pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site276substrate
Binding site312substrate
Binding site316substrate
Active site342Proton donor
Binding site343substrate
Binding site370pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site370substrate

GO annotations

AspectTerm
Molecular Functiondiaminopimelate decarboxylase activity
Molecular Functionpyridoxal phosphate binding
Biological Processlysine biosynthetic process via diaminopimelate

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Diaminopimelate decarboxylase
  • EC number
  • Short names
    DAP decarboxylase
    ; DAPDC

Gene names

    • Name
      lysA
    • ORF names
      HNO86_25015

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • C1C7
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas

Accessions

  • Primary accession
    A0A7Y5YNI3

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue60N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain35-280Orn/DAP/Arg decarboxylase 2 N-terminal
Domain281-368Orn/DAP/Arg decarboxylase 2 C-terminal

Sequence similarities

Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    415
  • Mass (Da)
    45,141
  • Last updated
    2021-06-02 v1
  • Checksum
    D181CB26F557852C
MDAFNYRDGELFAEGVALSAIADRFGTPTYVYSRAHIEAQYLAYADALAGMPHLVCFAVKANSNLGVLNVLARLGAGFDIVSRGELERVLAAGGSADKIVFSGVGKTRDDMRRALEVGVHCFNVESTDELERLQVVAAELGVRAPISLRVNPDVDAGTHPYISTGLKENKFGIAIADAEDVYVRAAQLPNLEVVGVDCHIGSQLTTLPPFIDALDRLLGLVDRLSDCGIYLRHIDLGGGLGVRYRDEEPPLAGDYIKAVRERLDGRDLALVFEPGRFIVANAGVLLTQVEYLKHTEHKDFAIVDAAMNDLIRPALYQAWMDVTAVRPRDTAARTYDIVGPICETGDFLAKERELALEEGDLLAVHSAGAYGFVMSSNYNTRGRAAEVLVDGDQAFEVRRRETVAELFAGESLLPE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JABFMP010000039
EMBL· GenBank· DDBJ
NUT78301.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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