A0A1Q8VMV8 · A0A1Q8VMV8_9ACTO

  • Protein
    Aspartate 1-decarboxylase
  • Gene
    panD
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.

Caution

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

Catalytic activity

Cofactor

pyruvate (UniProtKB | Rhea| CHEBI:15361 )

Note: Binds 1 pyruvoyl group covalently per subunit.

Pathway

Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.

Features

Showing features for active site, binding site.

Type
IDPosition(s)Description
Active site28Schiff-base intermediate with substrate; via pyruvic acid
Binding site60substrate
Active site61Proton donor
Binding site76-78substrate

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionaspartate 1-decarboxylase activity
Biological Processalanine biosynthetic process
Biological Processpantothenate biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      panD
    • ORF names
      BKH15_07460
      , BKH28_07095
      , FK267_13200

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • G53E
    • P6N
    • CCUG 34288
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Actinomycetales > Actinomycetaceae > Actinomyces

Accessions

  • Primary accession
    A0A1Q8VMV8

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_50415036061-27Aspartate 1-decarboxylase beta chain
Modified residue28Pyruvic acid (Ser)
ChainPRO_504150360728-151Aspartate 1-decarboxylase alpha chain

Post-translational modification

Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.

Keywords

Interaction

Subunit

Heterooctamer of four alpha and four beta subunits.

Family & Domains

Sequence similarities

Belongs to the PanD family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    151
  • Mass (Da)
    16,138
  • Last updated
    2017-04-12 v1
  • Checksum
    96F618C92F2CF8AB
MSSRTRTMMTSKIHRATVTQADLDYVGSITVDIDLLEAADLLPGERVDICNCTNGNRLSTYVIPGERGAGEICVNGAAAHLVSPGDVVILIAYSQMSDAEARTYLPRVVFVDEANRIVERGTDPGQIPADSDVARLQGLRPTGIPLAEARA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MSKL01000017
EMBL· GenBank· DDBJ
OLO49437.1
EMBL· GenBank· DDBJ
Genomic DNA
MSKW01000014
EMBL· GenBank· DDBJ
OLO76721.1
EMBL· GenBank· DDBJ
Genomic DNA
VICC01000011
EMBL· GenBank· DDBJ
TQD59006.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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