FDC1_CANDC
ID FDC1_CANDC Reviewed; 513 AA.
AC B9WJ66;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Ferulic acid decarboxylase 1 {ECO:0000255|HAMAP-Rule:MF_03196, ECO:0000303|PubMed:26083754};
DE EC=4.1.1.102 {ECO:0000255|HAMAP-Rule:MF_03196};
DE AltName: Full=Phenacrylate decarboxylase {ECO:0000255|HAMAP-Rule:MF_03196};
GN Name=FDC1 {ECO:0000250|UniProtKB:Q03034, ECO:0000255|HAMAP-Rule:MF_03196};
GN ORFNames=CD36_64160;
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(2009).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.46 ANGSTROMS) IN COMPLEX WITH PRFMN AND MANGANESE.
RX PubMed=26083754; DOI=10.1038/nature14560;
RA Payne K.A., White M.D., Fisher K., Khara B., Bailey S.S., Parker D.,
RA Rattray N.J., Trivedi D.K., Goodacre R., Beveridge R., Barran P.,
RA Rigby S.E., Scrutton N.S., Hay S., Leys D.;
RT "New cofactor supports alpha,beta-unsaturated acid decarboxylation via 1,3-
RT dipolar cycloaddition.";
RL Nature 522:497-501(2015).
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:0000255|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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_03196};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03196,
CC ECO:0000269|PubMed:26083754};
CC -!- COFACTOR:
CC Name=prenyl-FMN; Xref=ChEBI:CHEBI:87746;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03196,
CC ECO:0000269|PubMed:26083754};
CC Note=Binds 1 prenylated FMN (prenyl-FMN) per subunit.
CC {ECO:0000255|HAMAP-Rule:MF_03196, ECO:0000269|PubMed:26083754};
CC -!- SUBUNIT: Homodimer. May form higher order oligomers.
CC {ECO:0000255|HAMAP-Rule:MF_03196}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03196}.
CC -!- SIMILARITY: Belongs to the UbiD family. UbiD-like/FDC subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03196}.
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DR EMBL; FM992693; CAX41287.1; -; Genomic_DNA.
DR RefSeq; XP_002421128.1; XM_002421083.1.
DR PDB; 4ZAD; X-ray; 2.46 A; A/B=1-513.
DR PDBsum; 4ZAD; -.
DR AlphaFoldDB; B9WJ66; -.
DR SMR; B9WJ66; -.
DR DIP; DIP-61588N; -.
DR STRING; 42374.XP_002421128.1; -.
DR EnsemblFungi; CAX41287; CAX41287; CD36_64160.
DR GeneID; 8048688; -.
DR KEGG; cdu:CD36_64160; -.
DR CGD; CAL0000166139; Cd36_64160.
DR VEuPathDB; FungiDB:CD36_64160; -.
DR eggNOG; ENOG502QR5I; Eukaryota.
DR HOGENOM; CLU_023348_0_0_1; -.
DR OrthoDB; 588541at2759; -.
DR Proteomes; UP000002605; Chromosome 6.
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 HAMAP; MF_01983; UbiD_FDC; 1.
DR InterPro; IPR002830; UbiD.
DR InterPro; IPR032903; UbiD/Fdc1.
DR PANTHER; PTHR30108; PTHR30108; 1.
DR Pfam; PF01977; UbiD; 1.
DR TIGRFAMs; TIGR00148; TIGR00148; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Decarboxylase; Flavoprotein; FMN; Lyase;
KW Manganese; Metal-binding.
FT CHAIN 1..513
FT /note="Ferulic acid decarboxylase 1"
FT /id="PRO_0000434530"
FT ACT_SITE 289
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03196"
FT BINDING 174..179
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03196,
FT ECO:0000269|PubMed:26083754"
FT BINDING 174
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03196,
FT ECO:0000269|PubMed:26083754"
FT BINDING 196..197
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03196,
FT ECO:0000269|PubMed:26083754"
FT BINDING 197
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03196"
FT BINDING 240
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03196,
FT ECO:0000269|PubMed:26083754"
FT BINDING 240
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03196"
FT BINDING 405
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03196,
FT ECO:0000269|PubMed:26083754"
FT TURN 5..7
FT /evidence="ECO:0007829|PDB:4ZAD"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:4ZAD"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:4ZAD"
FT HELIX 34..45
FT /evidence="ECO:0007829|PDB:4ZAD"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:4ZAD"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:4ZAD"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:4ZAD"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:4ZAD"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:4ZAD"
FT HELIX 99..108
FT /evidence="ECO:0007829|PDB:4ZAD"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:4ZAD"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:4ZAD"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:4ZAD"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:4ZAD"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:4ZAD"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:4ZAD"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:4ZAD"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:4ZAD"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:4ZAD"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:4ZAD"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:4ZAD"
FT HELIX 197..207
FT /evidence="ECO:0007829|PDB:4ZAD"
FT STRAND 213..221
FT /evidence="ECO:0007829|PDB:4ZAD"
FT HELIX 224..230
FT /evidence="ECO:0007829|PDB:4ZAD"
FT HELIX 240..247
FT /evidence="ECO:0007829|PDB:4ZAD"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:4ZAD"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:4ZAD"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:4ZAD"
FT STRAND 269..284
FT /evidence="ECO:0007829|PDB:4ZAD"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:4ZAD"
FT STRAND 300..312
FT /evidence="ECO:0007829|PDB:4ZAD"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:4ZAD"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:4ZAD"
FT HELIX 329..332
FT /evidence="ECO:0007829|PDB:4ZAD"
FT HELIX 334..347
FT /evidence="ECO:0007829|PDB:4ZAD"
FT HELIX 352..355
FT /evidence="ECO:0007829|PDB:4ZAD"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:4ZAD"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:4ZAD"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:4ZAD"
FT HELIX 376..381
FT /evidence="ECO:0007829|PDB:4ZAD"
FT HELIX 386..399
FT /evidence="ECO:0007829|PDB:4ZAD"
FT TURN 401..409
FT /evidence="ECO:0007829|PDB:4ZAD"
FT STRAND 412..417
FT /evidence="ECO:0007829|PDB:4ZAD"
FT HELIX 425..434
FT /evidence="ECO:0007829|PDB:4ZAD"
FT TURN 438..441
FT /evidence="ECO:0007829|PDB:4ZAD"
FT STRAND 442..445
FT /evidence="ECO:0007829|PDB:4ZAD"
FT HELIX 455..458
FT /evidence="ECO:0007829|PDB:4ZAD"
FT HELIX 462..465
FT /evidence="ECO:0007829|PDB:4ZAD"
FT STRAND 470..476
FT /evidence="ECO:0007829|PDB:4ZAD"
FT HELIX 478..481
FT /evidence="ECO:0007829|PDB:4ZAD"
FT HELIX 493..495
FT /evidence="ECO:0007829|PDB:4ZAD"
FT HELIX 498..506
FT /evidence="ECO:0007829|PDB:4ZAD"
FT HELIX 508..511
FT /evidence="ECO:0007829|PDB:4ZAD"
SQ SEQUENCE 513 AA; 57668 MW; 630227105CDE9406 CRC64;
MSLNPALKFR DFIQVLKNEG DLIEIDTEVD PNLEVGAITR KAYENKLAAP LFNNLKQDPE
NIDPKNLFRI LGCPGGLRGF GNDHARIALH LGLDSQTPMK EIIDFLVANR NPKKYIPPVL
VPNDQSPHKK HHLTKEQIDL TKLPVPLLHH GDGGKFIQTY GMWVLQTPDK SWTNWSIARG
MVHDSKSITG LVINPQHVKQ VSDAWVAAGK GDKIPFALCF GVPPAAILVS SMPIPDGATE
AEYIGGLCNQ AVPVVKCETN DLEVPADCEM VFEGYLDRDT LVREGPFGEM HGYCFPKDHH
TQPLYRVNHI SYRDQAIMPI SNPGLCTDET HTLIGGLVSA ETKYLISQHP VLSKIVEDVF
TPYEAQALWL AVKINTHELV KLKTNAKELS NLVGDFLFRS KECYKVCSIL HEIILVGDDI
DIFDFKQLIW AYTTRHTPVQ DQLYFDDVKP FALAPFASQG PLIKTRQGGK CVTTCIFPKQ
FTDPDFEFVT CNFNGYPEEV KNKISQNWDK YYK
