ID F0XKQ3_GROCL Unreviewed; 482 AA.
AC F0XKQ3;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=CMQ_8261 {ECO:0000313|EMBL:EFX01795.1};
OS Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS (Graphiocladiella clavigera).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Grosmannia.
OX NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN [1] {ECO:0000313|EMBL:EFX01795.1, ECO:0000313|Proteomes:UP000007796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
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; GL629788; EFX01795.1; -; Genomic_DNA.
DR RefSeq; XP_014171277.1; XM_014315802.1.
DR AlphaFoldDB; F0XKQ3; -.
DR STRING; 655863.F0XKQ3; -.
DR GeneID; 25981897; -.
DR eggNOG; ENOG502QR5I; Eukaryota.
DR HOGENOM; CLU_023348_0_0_1; -.
DR InParanoid; F0XKQ3; -.
DR OrthoDB; 1700961at2759; -.
DR Proteomes; UP000007796; 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, ECO:0000313|EMBL:EFX01795.1};
KW Manganese {ECO:0000256|HAMAP-Rule:MF_03196};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03196};
KW Reference proteome {ECO:0000313|Proteomes:UP000007796}.
FT DOMAIN 16..104
FT /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase-like N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF20695"
FT DOMAIN 120..286
FT /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase-likw
FT Rift-related"
FT /evidence="ECO:0000259|Pfam:PF01977"
FT DOMAIN 304..440
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 371
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03196"
SQ SEQUENCE 482 AA; 52704 MW; 8F54B1BA0750F12A CRC64;
MSPNALPSMD FRTFVDALKA DGDIVEINEE CDPFLEVSAI IRRVVESDEK APLFNNVKGQ
NENGLWRILG GPNSLRSDPA TRYGRVARHL NLPPTASMKD ILGALTAAKS RPPIPPTVVE
TGPCKEYKLT GDQIDLNALP SPQLHKGDGG KYVQTYGMHI VQSPDGTWTN WSIARAMVND
KNSLAGLVAL PQHIAQIREM WKAKGQDMPW ALAFGVPPAA IMAASMPLPD GVSEAEYVGS
LVGASLEVVK CESNGLYVPA NSEIVFEGTC SVTEMVPEGP FGEMHGKDAI MPVSSCGRLT
DETHTMIGPL AAVEIGFLLK SNDFPVKEVF APFESQATWV AIQIDGEKLR ALKTDAETFA
RKVGDLVFRN KAGATIHRLL LVGDDIDVYN FKDVIWAYTT RCRPGMDEYY FEDVLGFALI
PYMLHGNGPA WRGGKAVSDC LLPSEYKNGP DWETADFAHS FPIEIQERVN SRWEALGFGC
SK
//