ID VPR_LACPL Reviewed; 493 AA. AC F9USN6; DT 22-FEB-2023, integrated into UniProtKB/Swiss-Prot. DT 19-OCT-2011, sequence version 1. DT 27-MAR-2024, entry version 57. DE RecName: Full=Vinyl phenol reductase {ECO:0000303|PubMed:23065750, ECO:0000303|PubMed:29934329}; DE Short=VPR {ECO:0000303|PubMed:29934329}; DE EC=1.1.1.- {ECO:0000269|PubMed:29934329, ECO:0000305|PubMed:35165440}; DE AltName: Full=4-vinylphenol reductase; GN Name=vprA {ECO:0000303|PubMed:29934329}; GN OrderedLocusNames=lp_3125 {ECO:0000312|EMBL:CCC80166.1}; OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) OS (Lactobacillus plantarum). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactiplantibacillus. OX NCBI_TaxID=220668; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1; RX PubMed=12566566; DOI=10.1073/pnas.0337704100; RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P., RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J., RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M., RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M., RA Siezen R.J.; RT "Complete genome sequence of Lactobacillus plantarum WCFS1."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1; RX PubMed=22156394; DOI=10.1128/jb.06275-11; RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M., RA Kleerebezem M., van Hijum S.A.; RT "Complete resequencing and reannotation of the Lactobacillus plantarum RT WCFS1 genome."; RL J. Bacteriol. 194:195-196(2012). RN [3] RP INDUCTION BY 4-COUMARATE. RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1; RX PubMed=23065750; DOI=10.1002/mnfr.201200384; RA Reveron I., de Las Rivas B., Munoz R., Lopez de Felipe F.; RT "Genome-wide transcriptomic responses of a human isolate of Lactobacillus RT plantarum exposed to p-coumaric acid stress."; RL Mol. Nutr. Food Res. 56:1848-1859(2012). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DISRUPTION PHENOTYPE, AND RP INDUCTION. RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1; RX PubMed=29934329; DOI=10.1128/aem.01064-18; RA Santamaria L., Reveron I., de Felipe F.L., de Las Rivas B., Munoz R.; RT "Ethylphenol Formation by Lactobacillus plantarum: Identification of the RT Enzyme Involved in the Reduction of Vinylphenols."; RL Appl. Environ. Microbiol. 84:e01064-e01064(2018). RN [5] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=35165440; DOI=10.1038/s41586-022-04396-8; RA Needham B.D., Funabashi M., Adame M.D., Wang Z., Boktor J.C., Haney J., RA Wu W.L., Rabut C., Ladinsky M.S., Hwang S.J., Guo Y., Zhu Q., RA Griffiths J.A., Knight R., Bjorkman P.J., Shapiro M.G., Geschwind D.H., RA Holschneider D.P., Fischbach M.A., Mazmanian S.K.; RT "A gut-derived metabolite alters brain activity and anxiety behaviour in RT mice."; RL Nature 602:647-653(2022). CC -!- FUNCTION: Involved in the production of ethylphenols during the CC degradation of hydroxycinnamic acids. Catalyzes the reduction of CC vinylphenols (4-vinylphenol (4-hydroxystyrene), 4-vinylcatechol (3,4- CC dihydroxystyrene), and 4-vinylguaiacol (2-methoxy-4-vinylphenol)) to CC their corresponding ethylphenols (4-ethylphenol, 4-ethylcatechol, and CC 4-ethylguaiacol, respectively) in the presence of NADH. These compounds CC are considered the most important flavor components of fermented soy CC sauce, and, on the other hand, are considered off flavor and CC responsible for sensorial wine and cider alteration (PubMed:29934329). CC The 4-ethylphenol produced by the gut bacteria L.plantarum strain WCFS1 CC can get subsequent sulfation to 4-ethylphenyl sulfate (4EPS) by host CC sulfotransferase (SULT1A1); 4EPS can enter the brain and seems to alter CC brain activity. Therefore, this enzyme likely plays a role in gut CC microbiota-host metabolic interactions (PubMed:35165440). CC {ECO:0000269|PubMed:29934329, ECO:0000269|PubMed:35165440}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4-hydroxystyrene + H(+) + NADH = 4-ethylphenol + NAD(+); CC Xref=Rhea:RHEA:70603, ChEBI:CHEBI:1883, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:49584, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; CC Evidence={ECO:0000269|PubMed:29934329, ECO:0000305|PubMed:35165440}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70604; CC Evidence={ECO:0000269|PubMed:29934329}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3,4-dihydroxystyrene + H(+) + NADH = 4-ethylcatechol + NAD(+); CC Xref=Rhea:RHEA:73955, ChEBI:CHEBI:1390, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:179260; CC Evidence={ECO:0000269|PubMed:29934329}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73956; CC Evidence={ECO:0000305|PubMed:29934329}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-methoxy-4-vinylphenol + H(+) + NADH = 4-ethyl-2- CC methoxyphenol + NAD(+); Xref=Rhea:RHEA:73959, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:42438, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:179252; Evidence={ECO:0000269|PubMed:29934329}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73960; CC Evidence={ECO:0000305|PubMed:29934329}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000269|PubMed:29934329}; CC -!- INDUCTION: Is up-regulated (four-fold) by 4-coumarate (4- CC hydroxycinnamate) (PubMed:23065750, PubMed:29934329). Is also induced CC by its substrate, 4-vinylphenol (PubMed:29934329). CC {ECO:0000269|PubMed:23065750, ECO:0000269|PubMed:29934329}. CC -!- DISRUPTION PHENOTYPE: Mutant lacking this gene is unable to reduce 4- CC vinylphenol to 4-ethylphenol, while its ability to reduce CC hydroxycinnamic acid is not affected. {ECO:0000269|PubMed:29934329}. CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. CC FRD/SDH subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL935263; CCC80166.1; -; Genomic_DNA. DR RefSeq; WP_011102053.1; NC_004567.2. DR RefSeq; YP_004890680.1; NC_004567.2. DR AlphaFoldDB; F9USN6; -. DR SMR; F9USN6; -. DR STRING; 220668.lp_3125; -. DR EnsemblBacteria; CCC80166; CCC80166; lp_3125. DR KEGG; lpl:lp_3125; -. DR PATRIC; fig|220668.9.peg.2613; -. DR eggNOG; COG1053; Bacteria. DR HOGENOM; CLU_011398_4_3_9; -. DR OrthoDB; 9806724at2; -. DR PhylomeDB; F9USN6; -. DR Proteomes; UP000000432; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1. DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1. DR InterPro; IPR003953; FAD-binding_2. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf. DR PANTHER; PTHR43400:SF12; FAD-DEPENDENT OXIDOREDUCTASE 2 FAD BINDING DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR43400; FUMARATE REDUCTASE; 1. DR Pfam; PF00890; FAD_binding_2; 1. DR PRINTS; PR00411; PNDRDTASEI. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1. PE 1: Evidence at protein level; KW FAD; Flavoprotein; Oxidoreductase; Reference proteome. FT CHAIN 1..493 FT /note="Vinyl phenol reductase" FT /id="PRO_0000457668" FT BINDING 19 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P83223" FT BINDING 38 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P83223" FT BINDING 46 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P83223" FT BINDING 50 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P83223" FT BINDING 52 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P83223" FT BINDING 156 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P83223" FT BINDING 224 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P83223" FT BINDING 448 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P83223" FT BINDING 467 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P83223" SQ SEQUENCE 493 AA; 53243 MW; 155C2D0B19B630BD CRC64; MTLAKHDSYD IVVVGTGAAG TAAALEAAQH GASVLLLEKG RHTGGSSNYT EGLFAVDSYL QKAQNINVSA TDVLKEEVDY SKYRADSRIW RRYLDDSANT VQWLKDQGVE YEGVQAMGAG EATWHIYKGM GQAVLHDALQ PQAQKLGVEL LTSTTAITLH QATDGAITGV MIQSAATNET QVINTAAVIL ATGGYLNNPD MMQKLTHYDT RRLIPVSSGK GTGDGLRLAW QAGAQQYGTG MAMLFGGYLK DPSEPSFKYM ASQMETAAGQ QPLLWLNEHG ERFVDEAVVY NFSYAGNALY TQNQVFSILD QGVINKMAQD GNFMGLGVYV RRGEKMTKLQ AEIDAAVAAN KPFIFKANTI EALATKMHLP VDQVTHSIQT YNQYCDNGQD DDFGKNPEYL VKVSQGPFYG FELNVGAFCT MGGLKVTTNN EVLDTTGQPI TGLYAAGNDA AGLTGDTYGP NMPGTCVGYA FYSGRNSGRH AAQYTHQQSI VSH //