A0A0S6TZ18 · A0A0S6TZ18_CLOBO

Function

function

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

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.

1127102030405060708090100110120
TypeIDPosition(s)Description
Active site25Schiff-base intermediate with substrate; via pyruvic acid
Binding site57substrate
Active site58Proton donor
Binding site73-75substrate

GO annotations

AspectTerm
Cellular Componentcytoplasm
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
      CBO05C_0587

Organism names

Accessions

  • Primary accession
    A0A0S6TZ18

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_50140010771-24Aspartate 1-decarboxylase beta chain
Modified residue25Pyruvic acid (Ser)
ChainPRO_501400107925-127Aspartate 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
    127
  • Mass (Da)
    14,288
  • Last updated
    2016-02-17 v1
  • Checksum
    3446E0CC32845847
MTITMLKSKIHRATITEANLNYVGSITIDKNLMDKANILEYEKVQIVDIDNGSRFETYVIAGEKNSGVICLNGAAARMVQKGDKIIIMSYCDLTIDEAKKFNPTVLFVDNTNIIEKLTNYERHGEII

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DF384213
EMBL· GenBank· DDBJ
GAE00897.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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