YQJG_ECOLI
ID YQJG_ECOLI Reviewed; 328 AA.
AC P42620; Q2M9A4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Glutathionyl-hydroquinone reductase YqjG;
DE Short=GS-HQR;
DE EC=1.8.5.7 {ECO:0000269|PubMed:20388120, ECO:0000269|PubMed:22686328, ECO:0000269|PubMed:22955277};
GN Name=yqjG; OrderedLocusNames=b3102, JW3073;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=20388120; DOI=10.1042/bj20091863;
RA Xun L., Belchik S.M., Xun R., Huang Y., Zhou H., Sanchez E., Kang C.,
RA Board P.G.;
RT "S-Glutathionyl-(chloro)hydroquinone reductases: a novel class of
RT glutathione transferases.";
RL Biochem. J. 428:419-427(2010).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND KINETIC
RP PARAMETERS.
RX PubMed=22686328; DOI=10.1021/bi300477z;
RA Lam L.K., Zhang Z., Board P.G., Xun L.;
RT "Reduction of benzoquinones to hydroquinones via spontaneous reaction with
RT glutathione and enzymatic reaction by S-glutathionyl-hydroquinone
RT reductases.";
RL Biochemistry 51:5014-5021(2012).
RN [5] {ECO:0007744|PDB:3R3E}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, AND
RP SUBUNIT.
RC STRAIN=K12;
RA Branch M.C., Cook P.D., Harp J.M., Armstrong R.N.;
RT "Crystal structure analysis of YqjG from Escherichia coli.";
RL Submitted (MAR-2012) to the PDB data bank.
RN [6] {ECO:0007744|PDB:4G0I, ECO:0007744|PDB:4G0K, ECO:0007744|PDB:4G0L}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH
RP GLUTATHIONE AND GS-MENADIONE, FUNCTION, CATALYTIC ACTIVITY, KINETIC
RP PARAMETERS, REACTION MECHANISM, ACTIVE SITES, SUBUNIT, AND MUTAGENESIS OF
RP CYS-63; TYR-195; TYR-253 AND TYR-296.
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 use a variety of GS-HQs as substrates, such as GS-p-hydroquinone
CC (GS-HQ), GS-hydroxy-p-hydroquinone (GS-HHQ), GS-methyl-p-hydroquinone
CC (GS-MHQ), GS-menadiol, and GS-trichloro-p-hydroquinone (GS-TriCH). Also
CC displays GSH-dependent disulfide-bond reduction activity toward HED (2-
CC hydroxyethyl disulfide), and is able to catalyze DMA (dimethylarsinate)
CC reduction. Exhibits no GSH transferase activity with 1-chloro-2,4-
CC dinitrobenzene (CDNB). {ECO:0000269|PubMed:20388120,
CC ECO:0000269|PubMed:22686328, ECO:0000269|PubMed:22955277}.
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:20388120, ECO:0000269|PubMed:22686328,
CC ECO:0000269|PubMed:22955277};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=840 uM for glutathione {ECO:0000269|PubMed:22686328,
CC ECO:0000269|PubMed:22955277};
CC KM=70 uM for GS-methyl-p-hydroquinone {ECO:0000269|PubMed:22686328,
CC ECO:0000269|PubMed:22955277};
CC KM=390 uM for GS-p-hydroquinone {ECO:0000269|PubMed:22686328,
CC ECO:0000269|PubMed:22955277};
CC KM=35 uM for GS-hydroxy-p-hydroquinone {ECO:0000269|PubMed:22686328,
CC ECO:0000269|PubMed:22955277};
CC KM=4 uM for GS-menadiol {ECO:0000269|PubMed:22686328,
CC ECO:0000269|PubMed:22955277};
CC KM=341 uM for GS-p-hydroquinone {ECO:0000269|PubMed:22686328,
CC ECO:0000269|PubMed:22955277};
CC Vmax=10.8 umol/min/mg enzyme for the reduction of glutathionyl-para-
CC hydroquinone {ECO:0000269|PubMed:22686328,
CC ECO:0000269|PubMed:22955277};
CC Note=kcat is 15, 14, 7.2 and 4.9 sec(-1) for the reduction of GS-MHQ,
CC GS-HQ, GS-HHQ and GS-menadiol, respectively.
CC {ECO:0000269|PubMed:22686328};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22955277, ECO:0000269|Ref.5}.
CC -!- MISCELLANEOUS: The reaction mechanism of reduction of GS-HQs is
CC believed to involve a redox-active Cys that attacks the sulfhydryl of
CC GS-hydroquinone, forming protein-glutathione mixed disulfide bond and
CC releasing the hydroquinone. A GSH comes in to regenerate the protein
CC and release GS-SG to complete the reaction.
CC {ECO:0000269|PubMed:22955277}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Xi-class GSH transferase
CC family. {ECO:0000305}.
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DR EMBL; U18997; AAA57906.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76137.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77152.1; -; Genomic_DNA.
DR PIR; C65099; C65099.
DR RefSeq; NP_417573.1; NC_000913.3.
DR RefSeq; WP_000531213.1; NZ_LN832404.1.
DR PDB; 3R3E; X-ray; 2.20 A; A/B=1-328.
DR PDB; 4G0I; X-ray; 2.05 A; A/B=1-328.
DR PDB; 4G0K; X-ray; 2.56 A; A/B=1-328.
DR PDB; 4G0L; X-ray; 2.62 A; A/B=1-328.
DR PDBsum; 3R3E; -.
DR PDBsum; 4G0I; -.
DR PDBsum; 4G0K; -.
DR PDBsum; 4G0L; -.
DR AlphaFoldDB; P42620; -.
DR SMR; P42620; -.
DR BioGRID; 4260937; 21.
DR BioGRID; 851931; 3.
DR DIP; DIP-12888N; -.
DR IntAct; P42620; 13.
DR STRING; 511145.b3102; -.
DR jPOST; P42620; -.
DR PaxDb; P42620; -.
DR PRIDE; P42620; -.
DR EnsemblBacteria; AAC76137; AAC76137; b3102.
DR EnsemblBacteria; BAE77152; BAE77152; BAE77152.
DR GeneID; 947615; -.
DR KEGG; ecj:JW3073; -.
DR KEGG; eco:b3102; -.
DR PATRIC; fig|511145.12.peg.3198; -.
DR EchoBASE; EB2602; -.
DR eggNOG; COG0435; Bacteria.
DR HOGENOM; CLU_037263_0_1_6; -.
DR InParanoid; P42620; -.
DR OMA; PWANRAI; -.
DR PhylomeDB; P42620; -.
DR BioCyc; EcoCyc:G7616-MON; -.
DR BioCyc; MetaCyc:G7616-MON; -.
DR BRENDA; 1.8.5.7; 2026.
DR PRO; PR:P42620; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0016672; F:oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor; IDA:EcoCyc.
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; IPR040079; Glutathione_S-Trfase.
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; SFLDS00019; Glutathione_Transferase_(cytos; 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; Reference proteome.
FT CHAIN 1..328
FT /note="Glutathionyl-hydroquinone reductase YqjG"
FT /id="PRO_0000169436"
FT DOMAIN 172..296
FT /note="GST C-terminal"
FT REGION 203..311
FT /note="Dimerization"
FT ACT_SITE 63
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:22955277"
FT ACT_SITE 195
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:22955277"
FT BINDING 96
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:22955277, ECO:0000269|Ref.5"
FT BINDING 130..133
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:22955277, ECO:0000269|Ref.5"
FT BINDING 148..149
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:22955277, ECO:0000269|Ref.5"
FT SITE 253
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000305"
FT SITE 296
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000305"
FT MUTAGEN 63
FT /note="C->A: Loss of GS-hydroquinone reductase activity."
FT /evidence="ECO:0000269|PubMed:22955277"
FT MUTAGEN 195
FT /note="Y->F: 46-fold reduction in GS-hydroquinone reductase
FT activity."
FT /evidence="ECO:0000269|PubMed:22955277"
FT MUTAGEN 253
FT /note="Y->F: 55-fold reduction in GS-hydroquinone reductase
FT activity."
FT /evidence="ECO:0000269|PubMed:22955277"
FT MUTAGEN 296
FT /note="Y->F: 22-fold reduction in GS-hydroquinone reductase
FT activity."
FT /evidence="ECO:0000269|PubMed:22955277"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:4G0I"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:4G0L"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:4G0I"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:4G0I"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:4G0I"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:4G0I"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:4G0I"
FT HELIX 64..75
FT /evidence="ECO:0007829|PDB:4G0I"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:4G0I"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:4G0I"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:4G0L"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:4G0I"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:4G0I"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:4G0I"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:4G0I"
FT TURN 139..142
FT /evidence="ECO:0007829|PDB:4G0I"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:4G0I"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:4G0I"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:4G0I"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:4G0I"
FT HELIX 176..189
FT /evidence="ECO:0007829|PDB:4G0I"
FT TURN 190..193
FT /evidence="ECO:0007829|PDB:4G0I"
FT HELIX 194..198
FT /evidence="ECO:0007829|PDB:4G0I"
FT HELIX 203..223
FT /evidence="ECO:0007829|PDB:4G0I"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:4G0I"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:4G0I"
FT HELIX 237..249
FT /evidence="ECO:0007829|PDB:4G0I"
FT TURN 250..257
FT /evidence="ECO:0007829|PDB:4G0I"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:4G0I"
FT HELIX 268..278
FT /evidence="ECO:0007829|PDB:4G0I"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:4G0I"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:4G0I"
FT HELIX 289..299
FT /evidence="ECO:0007829|PDB:4G0I"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:4G0I"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:4G0I"
SQ SEQUENCE 328 AA; 37386 MW; D1C675FD1F861D1D CRC64;
MGQLIDGVWH DTWYDTKSTG GKFQRSASAF RNWLTADGAP GPTGTGGFIA EKDRYHLYVS
LACPWAHRTL IMRKLKGLEP FISVSVVNPL MLENGWTFDD SFPGATGDTL YQNEFLYQLY
LHADPHYSGR VTVPVLWDKK NHTIVSNESA EIIRMFNTAF DALGAKAGDY YPPALQTKID
ELNGWIYDTV NNGVYKAGFA TSQEAYDEAV AKVFESLARL EQILGQHRYL TGNQLTEADI
RLWTTLVRFD PVYVTHFKCD KHRISDYLNL YGFLRDIYQM PGIAETVNFD HIRNHYFRSH
KTINPTGIIS IGPWQDLDEP HGRDVRFG
