PCPC_SPHCR
ID PCPC_SPHCR Reviewed; 248 AA.
AC Q03520; Q8KN34;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Tetrachloro-P-hydroquinone reductive dehalogenase;
DE EC=1.21.4.5 {ECO:0000269|PubMed:1459949, ECO:0000269|PubMed:8931562};
GN Name=pcpC;
OS Sphingobium chlorophenolicum.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=46429;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 39723 / DSM 6824 / L-1;
RX PubMed=8478329; DOI=10.1128/jb.175.9.2640-2644.1993;
RA Orser C.S., Dutton J., Lange C.C., Jablonski P.E., Xun L., Hargis M.;
RT "Characterization of a Flavobacterium glutathione S-transferase gene
RT involved reductive dechlorination.";
RL J. Bacteriol. 175:2640-2644(1993).
RN [2]
RP SEQUENCE REVISION TO 78-79 AND 180, AND FUNCTION.
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 PROTEIN SEQUENCE OF 2-19, CATALYTIC ACTIVITY, SUBUNIT, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 39723 / DSM 6824 / L-1;
RX PubMed=1459949; DOI=10.1128/jb.174.24.8003-8007.1992;
RA Xun L., Topp E., Orser C.S.;
RT "Purification and characterization of a tetrachloro-p-hydroquinone
RT reductive dehalogenase from a Flavobacterium sp.";
RL J. Bacteriol. 174:8003-8007(1992).
RN [4]
RP CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-14 AND CYS-157, AND REACTION
RP MECHANISM.
RC STRAIN=ATCC 39723 / DSM 6824 / L-1;
RX PubMed=8931562; DOI=10.1021/bi961730f;
RA McCarthy D.L., Navarrete S., Willett W.S., Babbitt P.C., Copley S.D.;
RT "Exploration of the relationship between tetrachlorohydroquinone
RT dehalogenase and the glutathione S-transferase superfamily.";
RL Biochemistry 35:14634-14642(1996).
CC -!- FUNCTION: Sequential reduction of tetrachloro-p-hydroquinone to
CC monochlorophenol, using glutathione as the reducing agent.
CC {ECO:0000269|PubMed:12169590}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,6-dichlorohydroquinone + chloride + glutathione disulfide +
CC H(+) = 2,3,6-trichlorohydroquinone + 2 glutathione;
CC Xref=Rhea:RHEA:56832, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:141023,
CC ChEBI:CHEBI:141024; EC=1.21.4.5;
CC Evidence={ECO:0000269|PubMed:1459949, ECO:0000269|PubMed:8931562};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,3,6-trichlorohydroquinone + chloride + glutathione disulfide
CC = 2,3,5,6-tetrachlorohydroquinone + 2 glutathione;
CC Xref=Rhea:RHEA:56828, ChEBI:CHEBI:17996, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:57994, ChEBI:CHEBI:58297, ChEBI:CHEBI:141023;
CC EC=1.21.4.5; Evidence={ECO:0000269|PubMed:1459949,
CC ECO:0000269|PubMed:8931562};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6-7. {ECO:0000269|PubMed:1459949};
CC -!- PATHWAY: Xenobiotic degradation; pentachlorophenol degradation.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1459949}.
CC -!- INDUCTION: Constitutively expressed.
CC -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR EMBL; AF512952; AAM96673.1; -; Genomic_DNA.
DR AlphaFoldDB; Q03520; -.
DR SMR; Q03520; -.
DR eggNOG; COG0625; Bacteria.
DR BioCyc; MetaCyc:PCPCFLAVO-MON; -.
DR BRENDA; 1.21.4.5; 7700.
DR UniPathway; UPA00691; -.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:InterPro.
DR GO; GO:0052690; F:trichloro-p-hydroquinone reductive dehalogenase activity; IEA:RHEA.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0019338; P:pentachlorophenol catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR044617; TCHQD.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR45374; PTHR45374; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Direct protein sequencing;
KW Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1459949"
FT CHAIN 2..248
FT /note="Tetrachloro-P-hydroquinone reductive dehalogenase"
FT /id="PRO_0000185991"
FT DOMAIN 2..84
FT /note="GST N-terminal"
FT DOMAIN 133..248
FT /note="GST C-terminal"
FT MUTAGEN 14
FT /note="C->S: Produces 2,3,5-trichloro-6-S-
FT glutathionylhydroquinone and dichloro-S-
FT glutathionylhydroquinone, but no 2,6-dichlorohydroquinone."
FT /evidence="ECO:0000269|PubMed:8931562"
FT MUTAGEN 157
FT /note="C->S: No effect."
FT /evidence="ECO:0000269|PubMed:8931562"
SQ SEQUENCE 248 AA; 28246 MW; A6B4A59A65F8AC77 CRC64;
MPEVSLYNYT MSICSMKTRL AMEEFGVDYD DKQVDIGFAL ENFEPDYVRL NEKAVVPTLV
VGDRVVTNSY NIVLEAAKLG KVGIPADPVE NKAALDWFQK GDQVNFQVIT YGHKGVPRGD
ELLIARRERA KEYAEKYPEL RSIYQAAHDR IVEHGNCAYD ADTVAQAEVD LQKRLDELDA
HLADKPFIAG SNYSIADIMW TVLLARIEML NMTAWISERP NLLAYYQRMK ARRSFETARV
MPNWKGGI
