ID X0BC97_FUSOX Unreviewed; 503 AA.
AC X0BC97;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Ferulic acid decarboxylase 1 {ECO:0000256|HAMAP-Rule:MF_03196};
DE EC=4.1.1.102 {ECO:0000256|HAMAP-Rule:MF_03196};
DE AltName: Full=Phenacrylate decarboxylase {ECO:0000256|HAMAP-Rule:MF_03196};
GN Name=FDC1 {ECO:0000256|HAMAP-Rule:MF_03196};
GN ORFNames=FOQG_15695 {ECO:0000313|EMBL:EXK79770.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK79770.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK79770.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK79770.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|HAMAP-Rule:MF_03196}.
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 Evidence={ECO:0000256|HAMAP-Rule:MF_03196};
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03196};
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 Evidence={ECO:0000256|HAMAP-Rule:MF_03196};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03196};
CC -!- COFACTOR:
CC Name=prenyl-FMN; Xref=ChEBI:CHEBI:87746;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03196};
CC Note=Binds 1 prenylated FMN (prenyl-FMN) per subunit.
CC {ECO:0000256|HAMAP-Rule:MF_03196};
CC -!- SUBUNIT: Homodimer. May form higher order oligomers.
CC {ECO:0000256|HAMAP-Rule:MF_03196}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03196}.
CC -!- SIMILARITY: Belongs to the UbiD family. UbiD-like/FDC subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03196}.
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DR EMBL; JH658461; EXK79770.1; -; Genomic_DNA.
DR AlphaFoldDB; X0BC97; -.
DR eggNOG; ENOG502QR5I; Eukaryota.
DR HOGENOM; CLU_023348_0_0_1; -.
DR Proteomes; UP000030663; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046281; P:cinnamic acid catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0033494; P:ferulate metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.5.4570; -; 1.
DR Gene3D; 3.40.1670.10; UbiD C-terminal domain-like; 1.
DR HAMAP; MF_01983; UbiD_FDC; 1.
DR InterPro; IPR032903; FDC-like.
DR InterPro; IPR002830; UbiD.
DR InterPro; IPR049381; UbiD-like_C.
DR InterPro; IPR049383; UbiD-like_N.
DR InterPro; IPR048304; UbiD_Rift_dom.
DR NCBIfam; TIGR00148; UbiD family decarboxylase; 1.
DR PANTHER; PTHR30108; 3-OCTAPRENYL-4-HYDROXYBENZOATE CARBOXY-LYASE-RELATED; 1.
DR PANTHER; PTHR30108:SF17; FERULIC ACID DECARBOXYLASE 1; 1.
DR Pfam; PF01977; UbiD; 1.
DR Pfam; PF20696; UbiD_C; 1.
DR Pfam; PF20695; UbiD_N; 1.
DR SUPFAM; SSF50475; FMN-binding split barrel; 1.
DR SUPFAM; SSF143968; UbiD C-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03196};
KW Decarboxylase {ECO:0000256|HAMAP-Rule:MF_03196};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_03196};
KW Manganese {ECO:0000256|HAMAP-Rule:MF_03196};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03196};
KW Reference proteome {ECO:0000313|Proteomes:UP000030663}.
FT DOMAIN 15..105
FT /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase-like N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF20695"
FT DOMAIN 120..319
FT /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase-likw
FT Rift-related"
FT /evidence="ECO:0000259|Pfam:PF01977"
FT DOMAIN 325..460
FT /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF20696"
FT ACT_SITE 283
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03196"
FT BINDING 170..175
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03196"
FT BINDING 170
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03196"
FT BINDING 192..193
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03196"
FT BINDING 193
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03196"
FT BINDING 234
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03196"
FT BINDING 234
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03196"
FT BINDING 392
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03196"
SQ SEQUENCE 503 AA; 56038 MW; 985C6B43C7419FEE CRC64;
MPSKTLPHMD FRSYVEALEA DGDLVSITEE CDPHLEVGAI IRKVVENNDK APLFNKLKGQ
DENGFWRILG APNSLRSDPK QRYGRLARHL GLPTDSSMKV ILDKMIAAKT TPPIPPTVVE
TGPCKEHILT PDQFDLTKLP APLLHQSDGG KYIQTYGMHI VQSPDGKWTN WSIARAMVYD
RNHLAGLVIK PQHLYQIHEM WKKEGRDMPW ALAFGVPPAA IMASSMPLPD GLSEAEYIGS
LVGSSLDVIK CETNGLYVPA NSEIVFEGTC SITETAPEGP FGEMHGYVFP GDAHPWPKYT
VDLITHRKDA ILPVSNCGRL TDETHTMIGP LAAAEIGFLL KSKGLPIKEA FSPFESQVTW
VALQVDTQKL REMKTTSEKF CREIGDIIFN HKVGYTIHRL VIVGDDINVY DFKDVIWAFC
TRCRPGMDEY FFEDVAGFPL IPYMSHGNGA PNRGGKVVSD SLLPVEYTTG KNWEAADFEN
SFPEEIKDRV CSRWQTLGFS SAK
//
