PCPF_SPHCR
ID PCPF_SPHCR Reviewed; 313 AA.
AC Q8KN33;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Glutathionyl-hydroquinone reductase PcpF {ECO:0000305};
DE Short=GS-HQR {ECO:0000305};
DE EC=1.8.5.7 {ECO:0000269|PubMed:18820023};
GN Name=pcpF {ECO:0000303|PubMed:18820023};
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=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 [2]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP CYS-53 AND CYS-248.
RC STRAIN=ATCC 39723 / DSM 6824 / L-1;
RX PubMed=18820023; DOI=10.1128/jb.00489-08;
RA Huang Y., Xun R., Chen G., Xun L.;
RT "Maintenance role of a glutathionyl-hydroquinone lyase (PcpF) in
RT pentachlorophenol degradation by Sphingobium chlorophenolicum ATCC 39723.";
RL J. Bacteriol. 190:7595-7600(2008).
RN [3] {ECO:0007744|PDB:4FQU}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS), AND SUBUNIT.
RX PubMed=22955277; DOI=10.1074/jbc.m112.395541;
RA Green A.R., Hayes R.P., Xun L., Kang C.;
RT "Structural understanding of GSH-dependent reduction mechanism of
RT glutathionyl-hydroquinone reductases.";
RL J. Biol. Chem. 287:35838-35848(2012).
CC -!- FUNCTION: Catalyzes glutathione (GSH)-dependent reduction of
CC glutathionyl-hydroquinones (GS-HQs) to the corresponding hydroquinones.
CC Can act on halogenated substrates such as GS-2,6-dichloro-p-
CC hydroquinone (GS-DiCH) and GS-trichloro-p-hydroquinone (GS-TriCH).
CC Involved in the degradation of pentachlorophenol (PCP), a toxic
CC pollutant. {ECO:0000269|PubMed:18820023}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(glutathione-S-yl)-hydroquinone + glutathione = glutathione
CC disulfide + hydroquinone; Xref=Rhea:RHEA:51936, ChEBI:CHEBI:17594,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:134616; EC=1.8.5.7;
CC Evidence={ECO:0000269|PubMed:18820023};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22955277}.
CC -!- DISRUPTION PHENOTYPE: Disruption mutant does not have GS-hydroquinone
CC lyase activity, is more sensitive to PCP toxicity and has a
CC significantly decreased PCP degradation rate.
CC {ECO:0000269|PubMed:18820023}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Xi-class GSH transferase
CC family. {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; AF512952; AAM96671.1; -; Genomic_DNA.
DR PDB; 4FQU; X-ray; 3.00 A; A/B/C/D/E/F/G/H=1-313.
DR PDBsum; 4FQU; -.
DR AlphaFoldDB; Q8KN33; -.
DR SMR; Q8KN33; -.
DR eggNOG; COG0435; Bacteria.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR016639; GST_Omega/GSH.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR32419; PTHR32419; 1.
DR Pfam; PF13409; GST_N_2; 1.
DR PIRSF; PIRSF015753; GST; 1.
DR SFLD; SFLDG01206; Xi.1; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Oxidoreductase.
FT CHAIN 1..313
FT /note="Glutathionyl-hydroquinone reductase PcpF"
FT /id="PRO_0000441028"
FT DOMAIN 161..285
FT /note="GST C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00685"
FT ACT_SITE 53
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P42620"
FT ACT_SITE 184
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P42620"
FT BINDING 86
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P42620"
FT BINDING 119..122
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P42620"
FT BINDING 137..138
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P42620"
FT MUTAGEN 53
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18820023"
FT MUTAGEN 248
FT /note="C->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:18820023"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:4FQU"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:4FQU"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:4FQU"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:4FQU"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:4FQU"
FT HELIX 54..65
FT /evidence="ECO:0007829|PDB:4FQU"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:4FQU"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:4FQU"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:4FQU"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:4FQU"
FT HELIX 106..112
FT /evidence="ECO:0007829|PDB:4FQU"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:4FQU"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:4FQU"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:4FQU"
FT HELIX 138..146
FT /evidence="ECO:0007829|PDB:4FQU"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:4FQU"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:4FQU"
FT HELIX 165..178
FT /evidence="ECO:0007829|PDB:4FQU"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:4FQU"
FT HELIX 182..187
FT /evidence="ECO:0007829|PDB:4FQU"
FT HELIX 192..212
FT /evidence="ECO:0007829|PDB:4FQU"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:4FQU"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:4FQU"
FT HELIX 226..238
FT /evidence="ECO:0007829|PDB:4FQU"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:4FQU"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:4FQU"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:4FQU"
FT HELIX 257..268
FT /evidence="ECO:0007829|PDB:4FQU"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:4FQU"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:4FQU"
FT HELIX 278..287
FT /evidence="ECO:0007829|PDB:4FQU"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:4FQU"
SQ SEQUENCE 313 AA; 35382 MW; 6894D38FDBE6CBBC CRC64;
MGLLIDGVWR DAWYDTKSSG GRFVRKESQY RGGLDAGFRG EPGRYHLYAG FACPWAHRVL
IMRALKGLEE MISVSMVNAY MGENGWTFLP GDDVVPDSIN GADYLYQVYT AADPTYTGRV
TIPILWDKVE KRILNNESSE IIRILNSAFD DVGALPGDYY PAEFRPEIDR INARVYETLN
NGVYRSGFAT TQEAYEEAFY PLFDTLDWLE EHLTGREWLV GDRLTEADIR LFPTLVRFDA
IYHGHFKCNL RRIADYPNLS RLVGKLASHE RVAPTINLRH AKAHYYGSHP SVNPTGIVPV
GPAQPLPGLT LQS
