AC   MF_03196;
DC   Protein; auto
c?   <OC:Eukaryota>
TR   HAMAP; MF_01983; -; 1; level=0
XX
Names: UbiD_FDC_euk
XX
ID   FDC1
DE   RecName: Full=Ferulic acid decarboxylase 1;
DE            EC=4.1.1.102;
DE   AltName: Full=Phenacrylate decarboxylase;
GN   Name=FDC1;
XX
CC   -!- FUNCTION: Catalyzes the reversible decarboxylation of aromatic
CC       carboxylic acids like ferulic acid, p-coumaric acid or cinnamic acid,
CC       producing the corresponding vinyl derivatives 4-vinylphenol, 4-
CC       vinylguaiacol, and styrene, respectively, which play the role of aroma
CC       metabolites.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-4-coumarate + H(+) = 4-hydroxystyrene + CO2;
CC         Xref=Rhea:RHEA:33227, ChEBI:CHEBI:1883, ChEBI:CHEBI:12876,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526; EC=4.1.1.102;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-cinnamate + H(+) = CO2 + styrene; Xref=Rhea:RHEA:46920,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15669, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:27452; EC=4.1.1.102;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-ferulate + H(+) = 2-methoxy-4-vinylphenol + CO2;
CC         Xref=Rhea:RHEA:33807, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:29749, ChEBI:CHEBI:42438; EC=4.1.1.102;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC   -!- COFACTOR:
CC       Name=prenyl-FMN; Xref=ChEBI:CHEBI:87746;
CC       Note=Binds 1 prenylated FMN (prenyl-FMN) per subunit.;
CC   -!- SUBUNIT: Homodimer. May form higher order oligomers.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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   Cytoplasm
KW   Decarboxylase
KW   Lyase
KW   Manganese
KW   Metal-binding
XX
GO   GO:0005737; C:cytoplasm
GO   GO:0016831; F:carboxy-lyase activity
GO   GO:0046281; P:cinnamic acid catabolic process
GO   GO:0033494; P:ferulate metabolic process
XX
FT   From: FDC1_YEAST (Q03034)
FT   BINDING         170..175
FT                   /ligand="prenyl-FMN"
FT                   /ligand_id="ChEBI:CHEBI:87746"
FT   Condition: [SN]-W-[SA]-[IV]-x-R
FT   BINDING         192..193
FT                   /ligand="prenyl-FMN"
FT                   /ligand_id="ChEBI:CHEBI:87746"
FT   Condition: Q-[HD]
FT   ACT_SITE        285
FT                   /note="Proton donor"
FT   Condition: E
FT   BINDING         170
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   Condition: N
FT   BINDING         193
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   Condition: H
FT   BINDING         236
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   Condition: E
FT   BINDING         236
FT                   /ligand="prenyl-FMN"
FT                   /ligand_id="ChEBI:CHEBI:87746"
FT   Condition: E
FT   BINDING         394
FT                   /ligand="prenyl-FMN"
FT                   /ligand_id="ChEBI:CHEBI:87746"
FT   Condition: K
XX
Size: 494-549;
Related: None;
Template: Q03034; Q9I6N5;
Scope:
 Eukaryota; Fungi
 Eukaryota; Oomycota
Fusion:
 Nter: None
 Cter: None
Duplicate: in ASPFN, ASPKW, ASPNA, ASPNC, ASPOR, BYSSN, COLGC, FUSC1, FUSC4,
 FUSO4, FUSOF, GIBF5, GIBM7, GIBZA, HYPAI, HYPVG, MACPH, METRA, PENEN
Plasmid: None
Comments: None
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# Revision 1.11 2023/06/01
//