Q9I6N5 · P2CDC_PSEAE
- ProteinPyrrole-2-carboxylic acid decarboxylase
- GenehudA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids496 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
- H+ + pyrrole-2-carboxylate = 1H-pyrrole + CO2
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 prenylated FMN (prenyl-FMN) per subunit.
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).
Activity is light sensitive (PubMed:33763291).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
4.3 mM | pyrrole-2-carboxylate |
kcat is 35.8 sec-1 with pyrrole-2-carboxylate as substrate.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 166 | K+ (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 168 | prenyl-FMN (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 170 | prenyl-FMN (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 187 | prenyl-FMN (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 188 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 188 | prenyl-FMN (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 218 | K+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 219 | K+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 221 | K+ (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 229 | K+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 229 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 229 | prenyl-FMN (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 278 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 386 | prenyl-FMN (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Molecular Function | 3-octaprenyl-4-hydroxybenzoate carboxy-lyase activity | |
Molecular Function | metal ion binding | |
Biological Process | catabolic process | |
Biological Process | ubiquinone biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyrrole-2-carboxylic acid decarboxylase
- EC number
- Short namesP2C decarboxylase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionQ9I6N5
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 318 | Decreases activity with pyrrole-2-carboxylic acid, but increases activity with furan-2-carboxylate. | ||||
Sequence: N → C or S | ||||||
Mutagenesis | 318 | No change in activity. | ||||
Sequence: N → D | ||||||
Mutagenesis | 318 | Prevents prenyl-FMN binding. | ||||
Sequence: N → H |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000434525 | 1-496 | Pyrrole-2-carboxylic acid decarboxylase | |||
Sequence: MNRSALDFRHFVDHLRRQGDLVDVHTEVDANLEIGAITRRVYERRAPAPLFHNIRDSLPGARVLGAPAGLRADRARAHSRLALHFGLPEHSGPRDIVAMLRAAMRAEPIAPRRLERGPVQENVWLGEQVDLTRFPVPLLHEQDGGRYFGTYGFHVVQTPDGSWDSWSVGRLMLVDRNTLAGPTIPTQHIGIIREQWRRLGKPTPWAMALGAPPAALAAAGMPLPEGVSEAGYVGALVGEPVEVVRTQTNGLWVPANTEIVLEGEISLDETALEGPMGEYHGYSFPIGKPQPLFHVHALSFRDQPILPICVAGTPPEENHTIWGTMISAQLLDVAQNAGLPVDMVWCSYEAATCWAVLSIDVQRLAALGTDAAAFAARVAETVFGSHAGHLVPKLILVGNDIDVTEIDQVVWALATRAHPLHDHFAFPQIRDFPMVPYLDAEDKARGSGGRLVINCLYPEQFAGQMRAATASFRHAYPTALRRRVEERWSDYGFGDA |
Proteomic databases
Expression
Induction
Repressed by hudR.
Interaction
Structure
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 statusComplete
- Length496
- Mass (Da)54,500
- Last updated2001-03-01 v1
- Checksum6C8EB98074A5CD54
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE004091 EMBL· GenBank· DDBJ | AAG03643.1 EMBL· GenBank· DDBJ | Genomic DNA |