ACDA_CLOS1
ID ACDA_CLOS1 Reviewed; 377 AA.
AC J7TF92;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=3-(aryl)acrylate reductase {ECO:0000305};
DE EC=1.3.8.15 {ECO:0000269|PubMed:29168502};
GN Name=acdA {ECO:0000303|PubMed:29168502};
GN ORFNames=CLOSPO_00312 {ECO:0000312|EMBL:EDU39257.1};
OS Clostridium sporogenes (strain ATCC 15579).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=471871;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15579;
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J., Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H.,
RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R.,
RA Wilson R.K.;
RT "Draft genome sequence of Clostridium sporogenes ATCC 15579.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=ATCC 15579;
RX PubMed=29168502; DOI=10.1038/nature24661;
RA Dodd D., Spitzer M.H., Van Treuren W., Merrill B.D., Hryckowian A.J.,
RA Higginbottom S.K., Le A., Cowan T.M., Nolan G.P., Fischbach M.A.,
RA Sonnenburg J.L.;
RT "A gut bacterial pathway metabolizes aromatic amino acids into nine
RT circulating metabolites.";
RL Nature 551:648-652(2017).
CC -!- FUNCTION: Essential for the reductive metabolism of L-phenylalanine, L-
CC tyrosine and L-tryptophan (PubMed:29168502). Catalyzes the reduction of
CC phenylacrylic acid to phenylpropionic acid, 4-hydroxy-phenylacrylic
CC acid to 4-hydroxy-phenylpropionic acid, and indoleacrylic acid to
CC indolepropionic acid (PubMed:29168502). {ECO:0000269|PubMed:29168502}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-phenylpropanoate + H(+) + oxidized [electron-transfer
CC flavoprotein] = (E)-cinnamate + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:59996, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:15669, ChEBI:CHEBI:51057,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=1.3.8.15;
CC Evidence={ECO:0000269|PubMed:29168502};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:59998;
CC Evidence={ECO:0000269|PubMed:29168502};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxidized [electron-transfer flavoprotein] + phloretate
CC = (E)-4-coumarate + reduced [electron-transfer flavoprotein];
CC Xref=Rhea:RHEA:59992, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC ChEBI:CHEBI:12876, ChEBI:CHEBI:15378, ChEBI:CHEBI:16331,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=1.3.8.15;
CC Evidence={ECO:0000269|PubMed:29168502};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:59994;
CC Evidence={ECO:0000269|PubMed:29168502};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-(1H-indol-3-yl)propanoate + H(+) + oxidized [electron-
CC transfer flavoprotein] = (E)-3-(indol-3-yl)acrylate + reduced
CC [electron-transfer flavoprotein]; Xref=Rhea:RHEA:60104, Rhea:RHEA-
CC COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:82916,
CC ChEBI:CHEBI:131929; EC=1.3.8.15;
CC Evidence={ECO:0000269|PubMed:29168502};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:60106;
CC Evidence={ECO:0000269|PubMed:29168502};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:H6LGM6};
CC -!- PATHWAY: Amino-acid degradation. {ECO:0000269|PubMed:29168502}.
CC -!- DISRUPTION PHENOTYPE: Mutants are deficient in reductive metabolism of
CC phenylalanine, tyrosine and tryptophan, and exhibit growth defects when
CC cultured with amino acids as the sole carbon source.
CC {ECO:0000269|PubMed:29168502}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; ABKW02000002; EDU39257.1; -; Genomic_DNA.
DR RefSeq; WP_003483287.1; NZ_DS981517.1.
DR EnsemblBacteria; EDU39257; EDU39257; CLOSPO_00312.
DR HOGENOM; CLU_018204_0_2_9; -.
DR BioCyc; MetaCyc:MON-20595; -.
DR BRENDA; 1.3.8.15; 1517.
DR Proteomes; UP000006610; Unassembled WGS sequence.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006569; P:tryptophan catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Oxidoreductase; Phenylalanine catabolism;
KW Tryptophan catabolism; Tyrosine catabolism.
FT CHAIN 1..377
FT /note="3-(aryl)acrylate reductase"
FT /id="PRO_0000454348"
FT ACT_SITE 361
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P15651"
FT BINDING 121..130
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P15651"
FT BINDING 154..156
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P15651"
FT BINDING 266
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P15651"
FT BINDING 277
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P15651"
FT BINDING 334..338
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P15651"
FT BINDING 363..365
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P15651"
SQ SEQUENCE 377 AA; 41328 MW; BC238F2BC3850065 CRC64;
MFFTEQHELI RKLARDFAEQ EIEPIADEVD KTAEFPKEIV KKMAQNGFFG IKMPKEYGGA
GADNRAYVTI MEEISRASGV AGIYLSSPNS LLGTPFLLVG TDEQKEKYLK PMIRGEKTLA
FALTEPGAGS DAGAVATTAR EEGDYYILNG RKTFITGAPI SDNIIVFAKT DMSKGTKGIT
TFIVDSKQEG VSFGKPEDKM GMIGCPTSDI ILENVKVHKS DILGELNKGF ITAMKTLSVG
RIGVAAQALG IAQAAVDEAV KYAKQRKQFN RPIAKFQAIQ FKLANMETKL NAAKLLVYNA
AYKMDCGEKA DKEASMAKYF AAESAIQIVN DALQIHGGYG YIKDYKIERL YRDVRVIAIY
EGTSEVQQMV IASNLLK
