A0A927JDR9 · A0A927JDR9_9ACTN

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.

TypeIDPosition(s)Description
Active site25Schiff-base intermediate with substrate; via pyruvic acid
Binding site57substrate
Active site58Proton donor
Binding site73-75substrate

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
      HT102_12450

Organism names

  • Taxonomic identifier
  • Strain
    • G463
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Hoyosellaceae > Lolliginicoccus

Accessions

  • Primary accession
    A0A927JDR9

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_50381941521-24Aspartate 1-decarboxylase beta chain
Modified residue25Pyruvic acid (Ser)
ChainPRO_503819415125-145Aspartate 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

Features

Showing features for region.

TypeIDPosition(s)Description
Region117-145Disordered

Sequence similarities

Belongs to the PanD family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    145
  • Mass (Da)
    15,311
  • Last updated
    2023-02-22 v1
  • Checksum
    711CD1A44758C32B
MFRTMLKSKIHRATVTQADLHYVGSVTVDADLLDAADLIEGEKVTIVDINNGARLETYVISGERGSGVIGINGAAAHLVHPGDLVILISYGVMEDAEARAYEPRIVFVDEGNAQIELGADPAHAPEGSGLKSPRSPERPVAPNAA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACYWE010000007
EMBL· GenBank· DDBJ
MBD8507295.1
EMBL· GenBank· DDBJ
Genomic DNA

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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