Q1Q7I9 · Q1Q7I9_KUEST

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.

1120102030405060708090100110120
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
      KsCSTR_40810
      , KSMBR1_3042
      , kusta0045

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • Kuenenia_mbr1_ru-nijmegen
    • CSTR1
  • Taxonomic lineage
    Bacteria > Planctomycetota > Candidatus Brocadiia > Candidatus Brocadiales > Candidatus Brocadiaceae > Candidatus Kuenenia

Accessions

  • Primary accession
    Q1Q7I9

Proteomes

    • Identifier
    • Component
      Chromosome Kuenenia_stuttgartiensis_MBR1

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_50150246401-24Aspartate 1-decarboxylase beta chain
Modified residue25Pyruvic acid (Ser)
ChainPRO_501502464125-120Aspartate 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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    120
  • Mass (Da)
    13,336
  • Last updated
    2006-05-16 v1
  • Checksum
    E78719A04D26D111
MLREMCKSKIHGATVTETNLEYNGSITIDKSLLTAVDILHYERVQVLNINNGTRVETYVIEGEQDSGIICLNGAAARWAQPGDRVIIIAYCLINNKDAIGWKPKIILVDAKNKLIKNLPT

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CT030148
EMBL· GenBank· DDBJ
CAJ70790.1
EMBL· GenBank· DDBJ
Genomic DNA
CP049055
EMBL· GenBank· DDBJ
QII13460.1
EMBL· GenBank· DDBJ
Genomic DNA
LT934425
EMBL· GenBank· DDBJ
SOH05520.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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