AC   MF_01983;
DC   Protein; auto
c?   <OC:Bacteria>
TR   HAMAP; MF_01983; -; 1; level=0
XX
Names: UbiD_FDC
XX
ID   P2CDC
DE   RecName: Full=Pyrrole-2-carboxylic acid decarboxylase;
DE            Short=P2C decarboxylase;
DE            EC=4.1.1.93;
XX
CC   -!- FUNCTION: Catalyzes the prenyl-FMN-dependent decarboxylation of
CC       pyrrole-2-carboxylate (P2C). Can also catalyze the carboxylation of
CC       pyrrole in the presence of elevated concentrations of CO(2) or
CC       bicarbonate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + pyrrole-2-carboxylate = 1H-pyrrole + CO2;
CC         Xref=Rhea:RHEA:31375, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:19203, ChEBI:CHEBI:27660; EC=4.1.1.93;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + pyrrole-2-carboxylate = 1H-pyrrole + hydrogencarbonate;
CC         Xref=Rhea:RHEA:31379, ChEBI:CHEBI:15377, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:19203, ChEBI:CHEBI:27660; EC=4.1.1.93;
CC   -!- COFACTOR:
CC       Name=prenyl-FMN; Xref=ChEBI:CHEBI:87746;
CC       Note=Binds 1 prenylated FMN (prenyl-FMN) per subunit.;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Note=Binds 1 Mn(2+) per subunit.;
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC       Note=Binds 1 K(+) per subunit.;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the UbiD family. UbiD-like/FDC subfamily.
XX
DR   Pfam; PF01977; UbiD; 1; trigger=no
DR   NCBIfam; TIGR00148; TIGR00148; 1; trigger=no
XX
KW   Aromatic hydrocarbons catabolism
KW   Decarboxylase
KW   FMN
KW   Flavoprotein
KW   Lyase
KW   Manganese
KW   Metal-binding
KW   Potassium
XX
GO   GO:0016831; F:carboxy-lyase activity
XX
FT   From: P2CDC_PSEAE (Q9I6N5)
FT   ACT_SITE        278
FT                   /note="Proton donor"
FT   Condition: E
FT   BINDING         166
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT   Condition: W
FT   BINDING         168
FT                   /ligand="prenyl-FMN"
FT                   /ligand_id="ChEBI:CHEBI:87746"
FT   Condition: V
FT   BINDING         170
FT                   /ligand="prenyl-FMN"
FT                   /ligand_id="ChEBI:CHEBI:87746"
FT   Condition: R
FT   BINDING         187
FT                   /ligand="prenyl-FMN"
FT                   /ligand_id="ChEBI:CHEBI:87746"
FT   Condition: Q
FT   BINDING         188
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   Condition: H
FT   BINDING         188
FT                   /ligand="prenyl-FMN"
FT                   /ligand_id="ChEBI:CHEBI:87746"
FT   Condition: H
FT   BINDING         218
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT   Condition: A
FT   BINDING         219
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT   Condition: A
FT   BINDING         221
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT   Condition: M
FT   BINDING         229
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT   Condition: E
FT   BINDING         229
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   Condition: E
FT   BINDING         229
FT                   /ligand="prenyl-FMN"
FT                   /ligand_id="ChEBI:CHEBI:87746"
FT   Condition: E
FT   BINDING         386
FT                   /ligand="prenyl-FMN"
FT                   /ligand_id="ChEBI:CHEBI:87746"
FT   Condition: H
XX
Size: 485-507;
Related: None;
Template: Q9I6N5; Q03034;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.8 2023/06/01
//