FDC1_ASPNC
ID FDC1_ASPNC Reviewed; 500 AA.
AC A2QHE5;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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, ECO:0000269|PubMed:26083743};
DE AltName: Full=Phenacrylate decarboxylase {ECO:0000255|HAMAP-Rule:MF_03196};
GN Name=fdc1 {ECO:0000255|HAMAP-Rule:MF_03196}; ORFNames=An03g06590;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
RN [2]
RP CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=26083743; DOI=10.1038/nature14559;
RA White M.D., Payne K.A., Fisher K., Marshall S.A., Parker D., Rattray N.J.,
RA Trivedi D.K., Goodacre R., Rigby S.E., Scrutton N.S., Hay S., Leys D.;
RT "UbiX is a flavin prenyltransferase required for bacterial ubiquinone
RT biosynthesis.";
RL Nature 522:502-506(2015).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.01 ANGSTROMS) IN COMPLEX WITH PRFMN AND MANGANESE,
RP FUNCTION, ACTIVE SITE, AND MUTAGENESIS OF ARG-173; GLU-277 AND GLU-282.
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 ECO:0000269|PubMed:26083754}.
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, ECO:0000269|PubMed:26083743};
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:26083743, 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 -!- INTERACTION:
CC A2QHE5; A2QHE5: fdc1; NbExp=2; IntAct=EBI-16161677, EBI-16161677;
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; AM270061; CAK38415.1; -; Genomic_DNA.
DR RefSeq; XP_001390534.1; XM_001390497.1.
DR PDB; 4ZA4; X-ray; 1.22 A; A=1-500.
DR PDB; 4ZA5; X-ray; 1.10 A; A=1-500.
DR PDB; 4ZA7; X-ray; 1.10 A; A=1-500.
DR PDB; 4ZA8; X-ray; 1.06 A; A=1-500.
DR PDB; 4ZA9; X-ray; 1.01 A; A=1-500.
DR PDB; 4ZAA; X-ray; 1.24 A; A=1-500.
DR PDB; 4ZAB; X-ray; 1.16 A; A=1-500.
DR PDB; 6EV3; X-ray; 1.30 A; A=1-500.
DR PDB; 6EV4; X-ray; 1.14 A; A=1-500.
DR PDB; 6EV5; X-ray; 1.28 A; A=1-500.
DR PDB; 6EV6; X-ray; 1.10 A; A=1-500.
DR PDB; 6EV7; X-ray; 1.06 A; A=1-500.
DR PDB; 6EV8; X-ray; 1.03 A; A=1-500.
DR PDB; 6EV9; X-ray; 1.64 A; A=1-500.
DR PDB; 6EVA; X-ray; 1.64 A; A=1-500.
DR PDB; 6EVB; X-ray; 1.13 A; A=1-500.
DR PDB; 6EVC; X-ray; 1.18 A; A=1-500.
DR PDB; 6EVD; X-ray; 1.19 A; A=1-500.
DR PDB; 6R2P; X-ray; 1.26 A; A=1-500.
DR PDB; 6R2R; X-ray; 1.13 A; A=1-500.
DR PDB; 6R2T; X-ray; 1.29 A; A=1-500.
DR PDB; 6R2Z; X-ray; 1.08 A; A=1-500.
DR PDB; 6R30; X-ray; 1.12 A; A=1-500.
DR PDB; 6R32; X-ray; 1.21 A; A=1-500.
DR PDB; 6R33; X-ray; 1.01 A; A=1-500.
DR PDB; 6R34; X-ray; 1.10 A; A=1-500.
DR PDB; 6R3F; X-ray; 1.25 A; A=1-500.
DR PDB; 6R3G; X-ray; 1.13 A; A=1-500.
DR PDB; 6R3I; X-ray; 1.14 A; A=1-500.
DR PDB; 6R3J; X-ray; 1.39 A; A=1-500.
DR PDB; 6R3L; X-ray; 1.24 A; A=1-500.
DR PDB; 6R3N; X-ray; 1.02 A; A=1-500.
DR PDB; 6R3O; X-ray; 1.13 A; A=1-500.
DR PDB; 6TIH; X-ray; 1.02 A; AAA=1-500.
DR PDB; 6TIJ; X-ray; 1.12 A; AAA=1-500.
DR PDB; 6TIL; X-ray; 1.42 A; AAA=1-500.
DR PDB; 6TIN; X-ray; 1.28 A; AAA=1-500.
DR PDB; 6TIO; X-ray; 1.54 A; AAA=1-500.
DR PDB; 7NF3; X-ray; 1.10 A; A=1-500.
DR PDB; 7NF4; X-ray; 1.69 A; A/B=1-500.
DR PDBsum; 4ZA4; -.
DR PDBsum; 4ZA5; -.
DR PDBsum; 4ZA7; -.
DR PDBsum; 4ZA8; -.
DR PDBsum; 4ZA9; -.
DR PDBsum; 4ZAA; -.
DR PDBsum; 4ZAB; -.
DR PDBsum; 6EV3; -.
DR PDBsum; 6EV4; -.
DR PDBsum; 6EV5; -.
DR PDBsum; 6EV6; -.
DR PDBsum; 6EV7; -.
DR PDBsum; 6EV8; -.
DR PDBsum; 6EV9; -.
DR PDBsum; 6EVA; -.
DR PDBsum; 6EVB; -.
DR PDBsum; 6EVC; -.
DR PDBsum; 6EVD; -.
DR PDBsum; 6R2P; -.
DR PDBsum; 6R2R; -.
DR PDBsum; 6R2T; -.
DR PDBsum; 6R2Z; -.
DR PDBsum; 6R30; -.
DR PDBsum; 6R32; -.
DR PDBsum; 6R33; -.
DR PDBsum; 6R34; -.
DR PDBsum; 6R3F; -.
DR PDBsum; 6R3G; -.
DR PDBsum; 6R3I; -.
DR PDBsum; 6R3J; -.
DR PDBsum; 6R3L; -.
DR PDBsum; 6R3N; -.
DR PDBsum; 6R3O; -.
DR PDBsum; 6TIH; -.
DR PDBsum; 6TIJ; -.
DR PDBsum; 6TIL; -.
DR PDBsum; 6TIN; -.
DR PDBsum; 6TIO; -.
DR PDBsum; 7NF3; -.
DR PDBsum; 7NF4; -.
DR AlphaFoldDB; A2QHE5; -.
DR SMR; A2QHE5; -.
DR DIP; DIP-61587N; -.
DR PaxDb; A2QHE5; -.
DR EnsemblFungi; CAK38415; CAK38415; An03g06590.
DR GeneID; 4980646; -.
DR KEGG; ang:ANI_1_1576034; -.
DR VEuPathDB; FungiDB:An03g06590; -.
DR HOGENOM; CLU_023348_0_0_1; -.
DR Proteomes; UP000006706; Chromosome 6R.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0009074; P:aromatic amino acid family catabolic process; IDA:UniProtKB.
DR GO; GO:0046281; P:cinnamic acid catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0033494; P:ferulate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0018966; P:styrene metabolic process; IDA:UniProtKB.
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; Reference proteome.
FT CHAIN 1..500
FT /note="Ferulic acid decarboxylase 1"
FT /id="PRO_0000434529"
FT ACT_SITE 282
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03196,
FT ECO:0000305|PubMed:26083754"
FT BINDING 168..173
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 168
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 190..191
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 191
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 233
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 233
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03196"
FT BINDING 391
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03196,
FT ECO:0000269|PubMed:26083754"
FT MUTAGEN 173
FT /note="R->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:26083754"
FT MUTAGEN 277
FT /note="E->Q: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:26083754"
FT MUTAGEN 282
FT /note="E->Q: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:26083754"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:4ZA9"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:4ZA9"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:4ZA9"
FT HELIX 35..46
FT /evidence="ECO:0007829|PDB:4ZA9"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:4ZA9"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:4ZA9"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:4ZA9"
FT TURN 78..81
FT /evidence="ECO:0007829|PDB:4ZA9"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:4ZA9"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:4ZA9"
FT HELIX 96..104
FT /evidence="ECO:0007829|PDB:4ZA9"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:4ZA9"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:4ZA9"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:4ZA9"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:4ZA9"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:4ZA9"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:4ZA9"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:4ZA9"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:4ZA9"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:4ZA9"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:4ZA9"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:4ZA9"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:4ZA9"
FT HELIX 217..223
FT /evidence="ECO:0007829|PDB:4ZA9"
FT HELIX 233..241
FT /evidence="ECO:0007829|PDB:4ZA9"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:4ZA9"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:4ZA9"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:4ZA9"
FT STRAND 262..277
FT /evidence="ECO:0007829|PDB:4ZA9"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:7NF4"
FT STRAND 293..305
FT /evidence="ECO:0007829|PDB:4ZA9"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:4ZA9"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:4ZA9"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:4ZA9"
FT HELIX 327..341
FT /evidence="ECO:0007829|PDB:4ZA9"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:4ZA9"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:4ZA9"
FT STRAND 359..364
FT /evidence="ECO:0007829|PDB:4ZA9"
FT HELIX 366..372
FT /evidence="ECO:0007829|PDB:4ZA9"
FT HELIX 376..388
FT /evidence="ECO:0007829|PDB:4ZA9"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:4ZA9"
FT STRAND 398..402
FT /evidence="ECO:0007829|PDB:4ZA9"
FT HELIX 411..421
FT /evidence="ECO:0007829|PDB:4ZA9"
FT TURN 424..427
FT /evidence="ECO:0007829|PDB:4ZA9"
FT STRAND 428..431
FT /evidence="ECO:0007829|PDB:4ZA9"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:4ZA9"
FT HELIX 441..444
FT /evidence="ECO:0007829|PDB:4ZA9"
FT STRAND 446..448
FT /evidence="ECO:0007829|PDB:4ZA9"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:6EV5"
FT STRAND 455..459
FT /evidence="ECO:0007829|PDB:4ZA9"
FT HELIX 463..466
FT /evidence="ECO:0007829|PDB:4ZA9"
FT STRAND 473..476
FT /evidence="ECO:0007829|PDB:7NF4"
FT HELIX 477..480
FT /evidence="ECO:0007829|PDB:4ZA9"
FT HELIX 483..496
FT /evidence="ECO:0007829|PDB:4ZA9"
SQ SEQUENCE 500 AA; 55201 MW; D07ABD3734A181B9 CRC64;
MSAQPAHLCF RSFVEALKVD NDLVEINTPI DPNLEAAAIT RRVCETNDKA PLFNNLIGMK
NGLFRILGAP GSLRKSSADR YGRLARHLAL PPTASMREIL DKMLSASDMP PIPPTIVPTG
PCKENSLDDS EFDLTELPVP LIHKSDGGKY IQTYGMHIVQ SPDGTWTNWS IARAMVHDKN
HLTGLVIPPQ HIWQIHQMWK KEGRSDVPWA LAFGVPPAAI MASSMPIPDG VTEAGYVGAM
TGSSLELVKC DTNDLYVPAT SEIVLEGTLS ISETGPEGPF GEMHGYIFPG DTHLGAKYKV
NRITYRNNAI MPMSSCGRLT DETHTMIGSL AAAEIRKLCQ QNDLPITDAF APFESQVTWV
ALRVDTEKLR AMKTTSEGFR KRVGDVVFNH KAGYTIHRLV LVGDDIDVYE GKDVLWAFST
RCRPGMDETL FEDVRGFPLI PYMGHGNGPA HRGGKVVSDA LMPTEYTTGR NWEAADFNQS
YPEDLKQKVL DNWTKMGFSN
