ID A0A135URQ4_9PEZI Unreviewed; 505 AA.
AC A0A135URQ4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=CSAL01_11375 {ECO:0000313|EMBL:KXH63063.1};
OS Colletotrichum salicis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH63063.1, ECO:0000313|Proteomes:UP000070121};
RN [1] {ECO:0000313|EMBL:KXH63063.1, ECO:0000313|Proteomes:UP000070121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH63063.1,
RC ECO:0000313|Proteomes:UP000070121};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL Submitted (FEB-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXH63063.1}.
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DR EMBL; JFFI01001126; KXH63063.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135URQ4; -.
DR STRING; 1209931.A0A135URQ4; -.
DR OrthoDB; 1700961at2759; -.
DR Proteomes; UP000070121; 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:UP000070121}.
FT DOMAIN 18..108
FT /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase-like N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF20695"
FT DOMAIN 122..322
FT /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase-likw
FT Rift-related"
FT /evidence="ECO:0000259|Pfam:PF01977"
FT DOMAIN 328..464
FT /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF20696"
FT ACT_SITE 286
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03196"
FT BINDING 173..178
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03196"
FT BINDING 173
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03196"
FT BINDING 195..196
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03196"
FT BINDING 196
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03196"
FT BINDING 237
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03196"
FT BINDING 237
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03196"
FT BINDING 395
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03196"
SQ SEQUENCE 505 AA; 56186 MW; A024DD878934D782 CRC64;
MSPSSSQDFP HLNFRSFVEA LKSDGDLVEI NEECDPNLEV GAIIRKVVET DERAPLFNRL
KGQDANGFWR ILGAPNSLRS DPSQRFGRLA RHLGLPPTST MKEILDKMIA AKSSTPIPPV
VSDTGSCKEI RLTPEQFDLT KLPAPMLHQS DGGKYIQTYG MHIVQSPDGK WTNWSIARAM
VYDRNYLVGL VIEPQHIWQI HQMWKKEGRD MPWALVFGVP PAAIMAASMP LPGGLSEAEY
IGSLVGAPLE VVKCDTNGLH VPANSEIVFE GVCSATETAP EGPFGEMHGY VFPGDAHPQP
KYRVDLITHR KDAILPVSNC GRLTDETHTM IGPLAAAEIG FLLKSKGLPI KEAFSPFESQ
VTWVALQVDT EKLRAMKTNA KDFCRSIGDL VFNDKVGYTI HRLVIVGDDI DVYNFKDIIW
AFSTRCRPGL DEYHFEDVLG FPLVPYMSHG NGDIRMGGKV VSDCLMPTEY TTGRDWEAAS
FQESYPVDVQ EKVLQRWESF GFASR
//
