A0A432Q9D5 · A0A432Q9D5_9BACT

  • 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 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
      DSY50_04505

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MAG 32
  • Taxonomic lineage
    Bacteria > Thermodesulfobacteriota > Desulfobulbia > Desulfobulbales > Desulfobulbaceae > Desulfobulbus

Accessions

  • Primary accession
    A0A432Q9D5

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_50196233981-24Aspartate 1-decarboxylase beta chain
Modified residue25Pyruvic acid (Ser)
ChainPRO_501962339925-120Aspartate 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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    120
  • Mass (Da)
    13,088
  • Last updated
    2019-05-08 v1
  • Checksum
    5223C43187039954
MQRIMLKAKIHRATITEADLNYDGSLTIDSNLMEAVGIIPFEQVKVYNVNNGERFDTYAIAGKAGSGVIGLNGAAARKGHVGDLIIIVTYGSYDDSELADYAPAILLCDEKNRIKKRITI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QNYC01000116
EMBL· GenBank· DDBJ
RUM35521.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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