AC   MF_01636;
DC   Protein; auto
TR   HAMAP; MF_01636; -; 1; level=0
XX
Names: UbiD
XX
ID   UBID
DE   RecName: Full=3-octaprenyl-4-hydroxybenzoate carboxy-lyase;
DE            EC=4.1.1.98;
DE   AltName: Full=Polyprenyl p-hydroxybenzoate decarboxylase;
GN   Name=ubiD;
XX
CC   -!- FUNCTION: Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy
CC       benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone
CC       biosynthesis.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 4-hydroxy-3-(all-trans-polyprenyl)benzoate + H(+) = a 2-(all-
CC         trans-polyprenyl)phenol + CO2; Xref=Rhea:RHEA:41680, Rhea:RHEA-
CC         COMP:9514, Rhea:RHEA-COMP:9516, ChEBI:CHEBI:1269, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:78396; EC=4.1.1.98;
CC   -!- COFACTOR:
CC       Name=prenylated FMN; Xref=ChEBI:CHEBI:87746;
CC       Note=Binds 1 prenylated FMN per subunit.;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC   -!- SUBUNIT: Homohexamer.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the UbiD family.
XX
DR   Pfam; PF01977; UbiD; 1; trigger=no
DR   NCBIfam; TIGR00148; TIGR00148; 1; trigger=no
XX
KW   Decarboxylase
KW   Lyase
KW   Manganese
KW   Membrane
KW   Metal-binding
KW   Cell membrane
KW   Ubiquinone biosynthesis
KW   Flavoprotein
KW   FMN
XX
GO   GO:0008694; F:4-hydroxy-3-polyprenylbenzoate decarboxylase activity
GO   GO:0006744; P:ubiquinone biosynthetic process
GO   GO:0005886; C:plasma membrane
XX
FT   From: UBID_ECOLI (P0AAB4)
FT   BINDING         178..180
FT                   /ligand="prenyl-FMN"
FT                   /ligand_id="ChEBI:CHEBI:87746"
FT   Condition: [IV]-Y-R
FT   BINDING         192..194
FT                   /ligand="prenyl-FMN"
FT                   /ligand_id="ChEBI:CHEBI:87746"
FT   Condition: R-W-L
FT   BINDING         197..198
FT                   /ligand="prenyl-FMN"
FT                   /ligand_id="ChEBI:CHEBI:87746"
FT   Condition: R-G
FT   ACT_SITE        290
FT                   /note="Proton donor"
FT   Condition: D
FT   BINDING         175
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   Condition: N
FT   BINDING         241
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   Condition: E
XX
Size: 487-522;
Related: None;
Template: P0AAB4;
Scope:
 Bacteria; Pseudomonadota
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Version: 33
# Last updated date: 2025-09-18
# Created date: 2006-11-15
//