{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q47914","uniProtkbId":"PCPD_SPHCR","entryAudit":{"firstPublicDate":"2018-06-20","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2002-10-01","entryVersion":136,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Sphingobium chlorophenolicum","taxonId":46429,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingobiaceae","Sphingobium"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12486067"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19325743"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"23676275"}],"value":"Tetrachlorobenzoquinone reductase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12486067"}],"value":"TCBQ reductase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23676275"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19325743"}],"value":"1.1.1.404"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12169590"}],"value":"pcpD"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12486067"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19325743"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23676275"}],"value":"Reductase involved in the degradation of pentachlorophenol (PCP), a general biocide and a major environmental pollutant (PubMed:12486067, PubMed:19325743). It catalyzes the reduction of tetrachlorobenzoquinone (TCBQ) to tetrachlorohydroquinone (TCHQ) (PubMed:12486067, PubMed:19325743, PubMed:23676275). The enzyme can use NADH or NADPH, but it is 550-fold more reactive with NADH (PubMed:19325743, PubMed:23676275). It has broad substrate specificity and can reduce the small molecule 2,6-dichloroindophenol (DCIP) and the protein cytochrome c (PubMed:23676275)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2,3,5,6-tetrachlorohydroquinone + NAD(+) + H(+) = 2,3,5,6-tetrachloro-1,4-benzoquinone + NADH","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:51888"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:36703"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:57994"}],"ecNumber":"1.1.1.404","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23676275"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19325743"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:51890"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23676275"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19325743"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"FMN","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23676275"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19325743"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58210"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"[2Fe-2S] cluster","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19325743"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23676275"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:190135"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19325743"}],"value":"Binds 1 [2Fe-2S] cluster."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19325743"}],"value":"The activity is stimulated by tetrachlorohydroquinone (TCHQ) at low concentrations but inhibited at high concentrations (PubMed:19325743). However, inhibition by TCHQ might not happen in vivo because TCHQ is unlikely to accumulate to high concentrations in cells (PubMed:19325743). Is inhibited by pentachlorophenol (PCP) in a concentration-dependent manner, due to competitive binding of PCP to the active site of PcpD (PubMed:19325743)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":11.5,"unit":"uM","substrate":"NADH (with 90 uM cytochrome c)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23676275"}]},{"constant":1.21,"unit":"mM","substrate":"NADPH (with 90 uM cytochrome c)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23676275"}]},{"constant":17.6,"unit":"uM","substrate":"cytochrome c (with 100 uM NADH)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23676275"}]},{"constant":38.3,"unit":"uM","substrate":"2,6-dichloroindophenol (DCIP) (with 100 uM NADH)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23676275"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23676275"}],"value":"kcat is 20.1 sec(-1) with NADH as substrate (with 90 uM cytochrome c) (PubMed:23676275). kcat is 3.7 sec(-1) with NADPH as substrate (with 90 uM cytochrome c) (PubMed:23676275). kcat is 9.1 sec(-1) with cytochrome c as substrate (with 100 uM NADH) (PubMed:23676275). kcat is 14.1 sec(-1) with 2,6-dichloroindophenol (DCIP) as substrate (with 100 uM NADH) (PubMed:23676275)."}]}},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19325743"}],"value":"Optimum pH is 7.0 (PubMed:19325743). It maintains more than 70% of its optimal activity even at pH 5.0 (PubMed:19325743). PcpD loses its activity quickly in basic solutions, retaining less than 20% of its optimal activity at pH 8.0 (PubMed:19325743)."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12486067"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19325743"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23676275"}],"value":"Xenobiotic degradation; pentachlorophenol degradation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19325743"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23676275"}],"value":"Homotrimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12486067"}],"value":"Expression is induced in the presence of pentachlorophenol"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12486067"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23676275"}],"value":"Lack of the gene affects the ability of S.chlorophenolicum to degrade pentachlorophenol (PCP) at high concentrations, but not at low concentrations (PubMed:12486067). It does not affect the ability of the mutant to remove tetrachlorophenol from the medium (PubMed:12486067). Deletion of the gene results in increased sensitivity to phenols that are degraded via a benzoquinone intermediate (PubMed:23676275)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the PDR/VanB family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":324,"modifier":"EXACT"}},"description":"Tetrachlorobenzoquinone reductase","featureId":"PRO_0000444444"},{"type":"Domain","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"FAD-binding FR-type","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00716"}]},{"type":"Domain","location":{"start":{"value":238,"modifier":"EXACT"},"end":{"value":324,"modifier":"EXACT"}},"description":"2Fe-2S ferredoxin-type","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00465"}]},{"type":"Binding site","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00465"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":278,"modifier":"EXACT"},"end":{"value":278,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00465"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":281,"modifier":"EXACT"},"end":{"value":281,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00465"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":311,"modifier":"EXACT"},"end":{"value":311,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00465"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}}],"keywords":[{"id":"KW-0001","category":"Ligand","name":"2Fe-2S"},{"id":"KW-0058","category":"Biological process","name":"Aromatic hydrocarbons catabolism"},{"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"id":"KW-0288","category":"Ligand","name":"FMN"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0520","category":"Ligand","name":"NAD"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"}],"references":[{"referenceNumber":1,"citation":{"id":"12169590","citationType":"journal article","authors":["Cai M.","Xun L."],"citationCrossReferences":[{"database":"PubMed","id":"12169590"},{"database":"DOI","id":"10.1128/jb.184.17.4672-4680.2002"}],"title":"Organization and regulation of pentachlorophenol-degrading genes in Sphingobium chlorophenolicum ATCC 39723.","publicationDate":"2002","journal":"J. Bacteriol.","firstPage":"4672","lastPage":"4680","volume":"184"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 39723 / DSM 6824 / L-1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAA68938.2"}]},{"referenceNumber":2,"citation":{"id":"7678243","citationType":"journal article","authors":["Orser C.S.","Lange C.C.","Xun L.","Zahrt T.C.","Schneider B.J."],"citationCrossReferences":[{"database":"PubMed","id":"7678243"},{"database":"DOI","id":"10.1128/jb.175.2.411-416.1993"}],"title":"Cloning, sequence analysis, and expression of the Flavobacterium pentachlorophenol-4-monooxygenase gene in Escherichia coli.","publicationDate":"1993","journal":"J. Bacteriol.","firstPage":"411","lastPage":"416","volume":"175"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-187"],"referenceComments":[{"value":"ATCC 39723 / DSM 6824 / L-1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAA68938.2"}]},{"referenceNumber":3,"citation":{"id":"12486067","citationType":"journal article","authors":["Dai M.","Rogers J.B.","Warner J.R.","Copley S.D."],"citationCrossReferences":[{"database":"PubMed","id":"12486067"},{"database":"DOI","id":"10.1128/jb.185.1.302-310.2003"}],"title":"A previously unrecognized step in pentachlorophenol degradation in Sphingobium chlorophenolicum is catalyzed by tetrachlorobenzoquinone reductase (PcpD).","publicationDate":"2003","journal":"J. 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REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":1,"SUBUNIT":1,"INDUCTION":1,"DISRUPTION PHENOTYPE":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":2,"Binding site":4},"uniParcId":"UPI00000B98D5"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9ZBB0","uniProtkbId":"PCPA_SPHCR","entryAudit":{"firstPublicDate":"2026-11-04","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1999-05-01","entryVersion":89,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Sphingobium chlorophenolicum","taxonId":46429,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingobiaceae","Sphingobium"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10600501"}],"value":"2,6-dichloro-p-hydroquinone 1,2-dioxygenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10600501"}],"value":"2,6-DiCH 1,2-dioxygenase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10526172"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10600501"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23489289"}],"value":"1.13.11.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10387005"}],"value":"2,6-dichlorohydroquinone 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It catalyzes the ring-opening of 2,6-dichlorohydroquinone (DiCH) to form 2-chloromaleylacetate (2-CMA) (PubMed:10526172, PubMed:10600501, PubMed:23489289). Cleavage of the benzene ring leads to the formation of an unstable intermediate, 2,6-dichloro-4-hydroxy-6-oxohexa-2,4-dienoate, which can spontaneously react with water, yielding 2-chloromaleylacetate (2-CMA) (PubMed:10526172, PubMed:10600501). In vitro, the enzyme can also catalyze the conversion of hydroquinone (HQ) and chlorohydroquinone (CHQ) to gamma-hydroxymuconic-semialdehyde and maleylacetate, respectively (PubMed:10526172). Another study shows that it cannot oxidize 2,5-DiCH, 6-chlorohydroxyquinol, hydroxyquinol, 2-chloro-p-hydroquinone, catechol, and 4-fluorocatechol (PubMed:10600501)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2,6-dichlorohydroquinone + O2 = (2E,4E)-2,6-dichloro-4-hydroxy-6-oxohexa-2,4-dienoate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:87599"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:141024"},{"database":"ChEBI","id":"CHEBI:747817"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10526172"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10600501"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23489289"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:87600"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10526172"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10600501"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Fe(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10387005"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10600501"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23489289"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29033"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23489289"}],"value":"Binds 1 Fe(2+) ion."}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"maximumVelocities":[{"velocity":3492.0,"unit":"nmol/min/mg","enzyme":"enzyme","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10600501"}]}],"michaelisConstants":[{"constant":13.5,"unit":"uM","substrate":"2,6-dichlorohydroquinone","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10600501"}]},{"constant":6.7,"unit":"uM","substrate":"2,6-dichlorohydroquinone","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23489289"}]},{"constant":242.0,"unit":"uM","substrate":"hydroquinone","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23489289"}]},{"constant":4.6,"unit":"uM","substrate":"Fe(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10600501"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10600501"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23489289"}],"value":"kcat is 2.1 sec(-1) with 2,6-dichlorohydroquinone as substrate (PubMed:10600501). kcat is 1.8 sec(-1) with 2,6-dichlorohydroquinone as substrate (PubMed:23489289). kcat is 0.28 sec(-1) with hydroquinone as substrate (PubMed:23489289)."}]}},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10600501"}],"value":"Optimum pH is 6.7 (PubMed:10600501). The enzyme is active from pH 6.3 to 8.0 (PubMed:10600501)."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12169590"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"10387005"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"10526172"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"10600501"}],"value":"Xenobiotic degradation; pentachlorophenol degradation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23489289"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12169590"}],"value":"Expression increases from the basal level after pentachlorophenol induction"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23489289"}],"value":"A tight hydrophobic pocket provides p-hydroquinones access to the Fe(II) center (PubMed:23489289). The p-hydroxyl group is essential for the substrate-binding, thus phenols and catechols, lacking a p-hydroxyl group, do not bind to PcpA (PubMed:23489289)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the extradiol ring-cleavage dioxygenase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":320,"modifier":"EXACT"}},"description":"2,6-dichloro-p-hydroquinone 1,2-dioxygenase","featureId":"PRO_0000465192"},{"type":"Domain","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":136,"modifier":"EXACT"}},"description":"VOC 1","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01163"}]},{"type":"Domain","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":280,"modifier":"EXACT"}},"description":"VOC 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reductase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19242755"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29273747"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12169590"}],"value":"1.3.1.32"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Chloromaleylacetate reductase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29273747"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12169590"}],"value":"1.3.1.-"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12169590"}],"value":"pcpE"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12169590"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19242755"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29273747"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12169590"}],"value":"Reductase involved in the degradation of pentachlorophenol (PCP), a general biocide and a major environmental pollutant (PubMed:12169590, PubMed:19242755). It catalyzes two consecutive reductive reactions, the reductive dehalogenation of 2-chloromaleylacetate (2-CMA) to maleylacetate (MA) and the subsequent reduction of MA to 3-oxoadipate (3-OXO) (Probable). The enzyme can use either NADH or NADPH, however it shows a strong preference for NADH over NADPH for the first reaction, the reduction of 2-CMA to MA (PubMed:29273747). The reduction of MA to 3-OXO is the rate-limiting step for PcpE catalysis (PubMed:29273747). PcpE exhibits an extremely low but detectable level of alcohol dehalogenase activity toward ethanol, supporting the notion that it is evolved from an iron-containing alcohol dehydrogenase (PubMed:29273747)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-chloromaleylacetate + NADH = maleylacetate + chloride + NAD(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:87507"},{"database":"ChEBI","id":"CHEBI:16468"},{"database":"ChEBI","id":"CHEBI:17996"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:231622"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29273747"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12169590"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:87508"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29273747"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12169590"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3-oxoadipate + NAD(+) = maleylacetate + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16981"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15775"},{"database":"ChEBI","id":"CHEBI:16468"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.3.1.32","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19242755"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29273747"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12169590"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:16983"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19242755"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29273747"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12169590"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3-oxoadipate + NADP(+) = maleylacetate + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16985"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15775"},{"database":"ChEBI","id":"CHEBI:16468"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.3.1.32","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29273747"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:16987"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29273747"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29273747"}],"value":"Inhibited by pentachlorophenol (PCP) in a concentration-dependent manner"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":0.09,"unit":"mM","substrate":"maleylacetate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19242755"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29273747"}]},{"constant":0.09,"unit":"mM","substrate":"2-chloromaleylacetate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29273747"}]},{"constant":0.13,"unit":"mM","substrate":"NADH (with 2-chloromaleylacetate as cosubstrate)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29273747"}]},{"constant":0.44,"unit":"mM","substrate":"NADH (with maleylacetate as cosubstrate)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29273747"}]},{"constant":0.67,"unit":"mM","substrate":"NADPH (with 2-chloromaleylacetate as cosubstrate)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29273747"}]},{"constant":0.52,"unit":"mM","substrate":"NADPH (with maleylacetate as cosubstrate)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29273747"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19242755"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29273747"}],"value":"kcat is 1.2 sec(-1) with maleylacetate as substrate (PubMed:19242755, PubMed:29273747). kcat is 17.6 sec(-1) with 2-chloromaleylacetate as substrate (PubMed:29273747). kcat is 143.7 sec(-1) with NADH as substrate (with 2-chloromaleylacetate as cosubstrate) (PubMed:29273747). kcat is 1.2 sec(-1) with NADH as substrate (with maleylacetate as cosubstrate) (PubMed:29273747). kcat is 29.7 sec(-1) with NADPH as substrate (with 2-chloromaleylacetate as cosubstrate) (PubMed:29273747). kcat is 0.7 sec(-1) with NADPH as substrate (with maleylacetate as cosubstrate) (PubMed:29273747)."}]}},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19242755"}],"value":"Optimum pH is 7.0 (PubMed:19242755). 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The enzyme is rather non-specific and exhibits poor catalytic efficiency (PubMed:22482720)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"pentachlorophenol + NADPH + O2 + H(+) = 2,3,5,6-tetrachloro-1,4-benzoquinone + chloride + NADP(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18685"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:17996"},{"database":"ChEBI","id":"CHEBI:36703"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58217"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.14.13.50","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22482720"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25238136"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:18686"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22482720"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2,3,5,6-tetrachlorophenol + NADPH + O2 = 2,3,5,6-tetrachlorohydroquinone + NADP(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11440"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:57994"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:59815"}],"ecNumber":"1.14.13.50","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22482720"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22482720"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}]},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":5.6,"unit":"uM","substrate":"2,3,5,6-tetrachlorophenol","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22482720"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22482720"}],"value":"kcat is 0.024 sec(-1) with pentachlorophenol as substrate (PubMed:22482720). kcat is 0.32 sec(-1) with 2,3,5,6-tetrachlorophenol as substrate (PubMed:22482720)."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12169590"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12486067"}],"value":"Xenobiotic degradation; pentachlorophenol degradation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22482720"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12169590"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7678243"}],"value":"Expression is induced by pentachlorophenol (PubMed:12169590, PubMed:7678243). It can also be induced by several other polychlorinated phenols such as 2,3,5,6-tetrachlorophenol (TeCP), TriCP and DiCP (PubMed:12169590)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25238136"}],"value":"After product formation, the strongly oxidizing tetrachlorobenzoquinone (TCBQ) abstracts an electron from a donor at the active site, possibly a cysteine residue, resulting in an unreactive diradical intermediate that traps the enzyme and greatly slows completion of the catalytic cycle (PubMed:25238136). TCBQ reductase, the second enzyme in the degradation pathway, rescues the stalled hydroxylase through two rapid one-electron transfer reactions (PubMed:25238136). This interaction restores productive catalysis and allows efficient degradation of PCP (PubMed:25238136)"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12486067"}],"value":"It was originally thought that the first step in the pentachlorophenol (PCP) degradation pathway in S.chlorophenolicum involved the conversion of PCP to tetrachlorohydroquinone. It has now been shown that PCP is actually converted by PcpB to tetrachlorobenzoquinone, which is subsequently reduced to tetrachlorohydroquinone by PcpD"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the PheA/TfdB FAD monooxygenase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7678243"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":538,"modifier":"EXACT"}},"description":"Pentachlorophenol 4-monooxygenase","featureId":"PRO_0000214044"},{"type":"Binding site","location":{"start":{"value":25,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q5YTV5"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q5YTV5"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":45,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q5YTV5"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":54,"modifier":"EXACT"},"end":{"value":54,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q5YTV5"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":115,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q5YTV5"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q5YTV5"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":312,"modifier":"EXACT"},"end":{"value":312,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q5YTV5"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}}],"keywords":[{"id":"KW-0058","category":"Biological process","name":"Aromatic hydrocarbons catabolism"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0274","category":"Ligand","name":"FAD"},{"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"id":"KW-0503","category":"Molecular function","name":"Monooxygenase"},{"id":"KW-0521","category":"Ligand","name":"NADP"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"}],"references":[{"referenceNumber":1,"citation":{"id":"7678243","citationType":"journal article","authors":["Orser C.S.","Lange C.C.","Xun L.","Zahrt T.C.","Schneider B.J."],"citationCrossReferences":[{"database":"PubMed","id":"7678243"},{"database":"DOI","id":"10.1128/jb.175.2.411-416.1993"}],"title":"Cloning, sequence analysis, and expression of the Flavobacterium pentachlorophenol-4-monooxygenase gene in Escherichia coli.","publicationDate":"1993","journal":"J. 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