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Database: UniProt
Entry: F0XKQ3_GROCL
LinkDB: F0XKQ3_GROCL
Original site: F0XKQ3_GROCL 
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
//
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