Q9I6N5 · P2CDC_PSEAE

Function

function

Catalyzes the prenyl-FMN-dependent decarboxylation of pyrrole-2-carboxylate (P2C) (PubMed:33763291).
Can also catalyze the carboxylation of pyrrole in the presence of elevated concentrations of CO2 or bicarbonate (PubMed:33763291).
Can accept a modest range of heteroaromatic compounds such as 3-methylpyrrole-2-carboxylate, indole-3-carboxylate and furan-2-carboxylate, and shows very low activity with thiophene-2-carboxylate (PubMed:33763291).
Attenuates the virulence of P.aeruginosa in a Drosophila model when overexpressed (PubMed:18591226).

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
prenyl-FMN (UniProtKB | Rhea| CHEBI:87746 )

Note: Binds 1 prenylated FMN (prenyl-FMN) per subunit.
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds 1 Mn2+ per subunit (PubMed:23671667, PubMed:33763291).
Can also use Mg2+, with lower efficiency (PubMed:33763291).
K+ (UniProtKB | Rhea| CHEBI:29103 )

Note: Binds 1 K+ per subunit.

Activity regulation

Imidazole acts as a reversible inhibitor via the formation of an imidazole-prenyl-FMN adduct (PubMed:33763291).
Activity is light sensitive (PubMed:33763291).

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
4.3 mMpyrrole-2-carboxylate
kcat is 35.8 sec-1 with pyrrole-2-carboxylate as substrate.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site166K+ (UniProtKB | ChEBI)
Binding site168prenyl-FMN (UniProtKB | ChEBI)
Binding site170prenyl-FMN (UniProtKB | ChEBI)
Binding site187prenyl-FMN (UniProtKB | ChEBI)
Binding site188Mn2+ (UniProtKB | ChEBI)
Binding site188prenyl-FMN (UniProtKB | ChEBI)
Binding site218K+ (UniProtKB | ChEBI)
Binding site219K+ (UniProtKB | ChEBI)
Binding site221K+ (UniProtKB | ChEBI)
Binding site229K+ (UniProtKB | ChEBI)
Binding site229Mn2+ (UniProtKB | ChEBI)
Binding site229prenyl-FMN (UniProtKB | ChEBI)
Active site278Proton donor
Binding site386prenyl-FMN (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Molecular Function3-octaprenyl-4-hydroxybenzoate carboxy-lyase activity
Molecular Functionmetal ion binding
Biological Processcatabolic process
Biological Processubiquinone biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Pyrrole-2-carboxylic acid decarboxylase
  • EC number
  • Short names
    P2C decarboxylase
  • Alternative names
    • Ferulic acid decarboxylase-like protein
    • Homologous to UbiD protein A
    • UbiD-like decarboxylase

Gene names

    • Name
      hudA
    • Ordered locus names
      PA0254

Organism names

Accessions

  • Primary accession
    Q9I6N5

Proteomes

Organism-specific databases

Subcellular Location

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis318Decreases activity with pyrrole-2-carboxylic acid, but increases activity with furan-2-carboxylate.
Mutagenesis318No change in activity.
Mutagenesis318Prevents prenyl-FMN binding.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004345251-496Pyrrole-2-carboxylic acid decarboxylase

Proteomic databases

Expression

Induction

Repressed by hudR.

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Domain

Consists of three domains: an N-terminal alpha/beta domain, a split beta-barrel with a similar fold of a family of flavin reductases and a C-terminal alpha/beta domain with a topology characteristic for the UbiD protein family.

Sequence similarities

Belongs to the UbiD family. UbiD-like/FDC subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    496
  • Mass (Da)
    54,500
  • Last updated
    2001-03-01 v1
  • Checksum
    6C8EB98074A5CD54
MNRSALDFRHFVDHLRRQGDLVDVHTEVDANLEIGAITRRVYERRAPAPLFHNIRDSLPGARVLGAPAGLRADRARAHSRLALHFGLPEHSGPRDIVAMLRAAMRAEPIAPRRLERGPVQENVWLGEQVDLTRFPVPLLHEQDGGRYFGTYGFHVVQTPDGSWDSWSVGRLMLVDRNTLAGPTIPTQHIGIIREQWRRLGKPTPWAMALGAPPAALAAAGMPLPEGVSEAGYVGALVGEPVEVVRTQTNGLWVPANTEIVLEGEISLDETALEGPMGEYHGYSFPIGKPQPLFHVHALSFRDQPILPICVAGTPPEENHTIWGTMISAQLLDVAQNAGLPVDMVWCSYEAATCWAVLSIDVQRLAALGTDAAAFAARVAETVFGSHAGHLVPKLILVGNDIDVTEIDQVVWALATRAHPLHDHFAFPQIRDFPMVPYLDAEDKARGSGGRLVINCLYPEQFAGQMRAATASFRHAYPTALRRRVEERWSDYGFGDA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE004091
EMBL· GenBank· DDBJ
AAG03643.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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