PCPB_SPHCR
ID PCPB_SPHCR Reviewed; 538 AA.
AC P42535; Q8KMS8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Pentachlorophenol 4-monooxygenase;
DE EC=1.14.13.50 {ECO:0000269|PubMed:22482720, ECO:0000269|PubMed:25238136};
DE AltName: Full=Pentachlorophenol hydroxylase;
GN Name=pcpB;
OS Sphingobium chlorophenolicum.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=46429;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-14.
RC STRAIN=ATCC 39723 / DSM 6824 / L-1;
RX PubMed=7678243; DOI=10.1128/jb.175.2.411-416.1993;
RA Orser C.S., Lange C.C., Xun L., Zahrt T.C., Schneider B.J.;
RT "Cloning, sequence analysis, and expression of the Flavobacterium
RT pentachlorophenol-4-monooxygenase gene in Escherichia coli.";
RL J. Bacteriol. 175:411-416(1993).
RN [2]
RP SEQUENCE REVISION TO 536, FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 39723 / DSM 6824 / L-1;
RX PubMed=12169590; DOI=10.1128/jb.184.17.4672-4680.2002;
RA Cai M., Xun L.;
RT "Organization and regulation of pentachlorophenol-degrading genes in
RT Sphingobium chlorophenolicum ATCC 39723.";
RL J. Bacteriol. 184:4672-4680(2002).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=22482720; DOI=10.1021/bi300261p;
RA Hlouchova K., Rudolph J., Pietari J.M., Behlen L.S., Copley S.D.;
RT "Pentachlorophenol hydroxylase, a poorly functioning enzyme required for
RT degradation of pentachlorophenol by Sphingobium chlorophenolicum.";
RL Biochemistry 51:3848-3860(2012).
RN [4]
RP CATALYTIC ACTIVITY, AND REACTION MECHANISM.
RX PubMed=25238136; DOI=10.1021/bi5010427;
RA Rudolph J., Erbse A.H., Behlen L.S., Copley S.D.;
RT "A radical intermediate in the conversion of pentachlorophenol to
RT tetrachlorohydroquinone by Sphingobium chlorophenolicum.";
RL Biochemistry 53:6539-6549(2014).
CC -!- FUNCTION: Dechlorination of pentachlorophenol to
CC tetrachlorobenzoquinone. Removes also hydrogen and nitro, amino, and
CC cyano groups from benzene ring at the para position in relation to the
CC hydroxyl of phenol. {ECO:0000269|PubMed:12169590,
CC ECO:0000269|PubMed:22482720}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 + pentachlorophenol = 2,3,5,6-tetrachloro-
CC 1,4-benzoquinone + chloride + H2O + NADP(+); Xref=Rhea:RHEA:18685,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17996, ChEBI:CHEBI:36703, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58217, ChEBI:CHEBI:58349; EC=1.14.13.50;
CC Evidence={ECO:0000269|PubMed:22482720, ECO:0000269|PubMed:25238136};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,3,5,6-tetrachlorophenol + NADPH + O2 = 2,3,5,6-
CC tetrachlorohydroquinone + H2O + NADP(+); Xref=Rhea:RHEA:11440,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:57994, ChEBI:CHEBI:58349, ChEBI:CHEBI:59815;
CC EC=1.14.13.50; Evidence={ECO:0000269|PubMed:22482720,
CC ECO:0000269|PubMed:25238136};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:22482720};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 mM for pentachlorophenol {ECO:0000269|PubMed:22482720};
CC KM=5.6 mM for 2,3,5,6-tetrachlorophenol
CC {ECO:0000269|PubMed:22482720};
CC Note=kcat is 0.024 sec(-1) with pentachlorophenol as substrate. kcat
CC is 0.32 sec(-1) with 2,3,5,6-tetrachlorophenol as substrate.
CC {ECO:0000269|PubMed:22482720};
CC -!- PATHWAY: Xenobiotic degradation; pentachlorophenol degradation.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22482720}.
CC -!- INDUCTION: By polychlorinated phenols. {ECO:0000269|PubMed:12169590}.
CC -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; U12290; AAF15368.2; -; Genomic_DNA.
DR AlphaFoldDB; P42535; -.
DR SMR; P42535; -.
DR BindingDB; P42535; -.
DR eggNOG; COG0654; Bacteria.
DR BioCyc; MetaCyc:PCPBFLAVO-MON; -.
DR BRENDA; 1.14.13.50; 7700.
DR SABIO-RK; P42535; -.
DR UniPathway; UPA00691; -.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0018677; F:pentachlorophenol monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0019338; P:pentachlorophenol catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Direct protein sequencing; FAD;
KW Flavoprotein; Monooxygenase; NADP; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7678243"
FT CHAIN 2..538
FT /note="Pentachlorophenol 4-monooxygenase"
FT /id="PRO_0000214044"
FT BINDING 16..45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 288..298
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
SQ SEQUENCE 538 AA; 59992 MW; CB545A9A1DCE8AB9 CRC64;
MSTYPINAPG QSADAAVLIV GGGPTGLIAA NELLRRGVSC RMIDRLPVAH QTSKSCTIHA
RSMEMMEHIG IAARYIETGV RSNGFTFNFE NTDANALLDF SVLPGRYPFI TIYNQNETER
VLRHDLEATY SFQPEWGTQL LALNQDENGI RADLRLKDGT KQTISPRWVI GADGVRSRVR
ECLGIAYEGE DYEENVLQMM DVGIQDFEAG DDWIHYFIGQ DKFVFVTKLP GSNYRVIISD
LGGANKSNLE ETREAFQGYL SSFDDHATLD EPRWATKWRV WKRMATAYRK GNVFLAGDAA
HCHSPSGGSG MNVGMQDAFN LGWKIAMVER GEAKPDLLDT YHTERTPVAQ QLLEGTHAMH
EIIMGHGKGL TDRIELTQAP GWHDAATYRV SGMSYNYRDQ LVSFNDDRLA GPSAGDRIPD
AELAPRIRLF DLVRNTRPTL LVAPATEAEV AEAEKLRDLI REQWPLVKPV LVRPQGSEES
IEGDVHVDSY GQLKREWGDN AKGWAALLRP DNYIHARAGL DRGDLLVQAI DAMLVRCA
