UniProtKB - P42620 (YQJG_ECOLI)
Protein
Glutathionyl-hydroquinone reductase YqjG
Gene
yqjG
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes glutathione (GSH)-dependent reduction of glutathionyl-hydroquinones (GS-HQs) to the corresponding hydroquinones. Can use a variety of GS-HQs as substrates, such as GS-p-hydroquinone (GS-HQ), GS-hydroxy-p-hydroquinone (GS-HHQ), GS-methyl-p-hydroquinone (GS-MHQ), GS-menadiol, and GS-trichloro-p-hydroquinone (GS-TriCH). Also displays GSH-dependent disulfide-bond reduction activity toward HED (2-hydroxyethyl disulfide), and is able to catalyze DMA (dimethylarsinate) reduction. Exhibits no GSH transferase activity with 1-chloro-2,4-dinitrobenzene (CDNB).3 Publications
Miscellaneous
The reaction mechanism of reduction of GS-HQs is believed to involve a redox-active Cys that attacks the sulfhydryl of GS-hydroquinone, forming protein-glutathione mixed disulfide bond and releasing the hydroquinone. A GSH comes in to regenerate the protein and release GS-SG to complete the reaction.1 Publication
Catalytic activityi
- 2-(glutathione-S-yl)-hydroquinone + glutathione = glutathione disulfide + hydroquinone3 PublicationsEC:1.8.5.73 Publications
Kineticsi
kcat is 15, 14, 7.2 and 4.9 sec(-1) for the reduction of GS-MHQ, GS-HQ, GS-HHQ and GS-menadiol, respectively.1 Publication
- KM=840 µM for glutathione2 Publications
- KM=70 µM for GS-methyl-p-hydroquinone2 Publications
- KM=390 µM for GS-p-hydroquinone2 Publications
- KM=35 µM for GS-hydroxy-p-hydroquinone2 Publications
- KM=4 µM for GS-menadiol2 Publications
- KM=341 µM for GS-p-hydroquinone2 Publications
- Vmax=10.8 µmol/min/mg enzyme for the reduction of glutathionyl-para-hydroquinone2 Publications
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 63 | Nucleophile1 Publication | 1 | |
Binding sitei | 96 | Glutathione2 Publications | 1 | |
Active sitei | 195 | Proton donor/acceptor1 Publication | 1 | |
Sitei | 253 | Lowers pKa of active site CysCurated | 1 | |
Sitei | 296 | Lowers pKa of active site CysCurated | 1 |
GO - Molecular functioni
- glutathione transferase activity Source: GO_Central
- oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor Source: EcoCyc
GO - Biological processi
- glutathione metabolic process Source: InterPro
Keywordsi
Molecular function | Oxidoreductase |
Enzyme and pathway databases
BioCyci | EcoCyc:G7616-MONOMER MetaCyc:G7616-MONOMER |
Names & Taxonomyi
Protein namesi | Recommended name: Glutathionyl-hydroquinone reductase YqjG (EC:1.8.5.73 Publications)Short name: GS-HQR |
Gene namesi | Name:yqjG Ordered Locus Names:b3102, JW3073 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 63 | C → A: Loss of GS-hydroquinone reductase activity. 1 Publication | 1 | |
Mutagenesisi | 195 | Y → F: 46-fold reduction in GS-hydroquinone reductase activity. 1 Publication | 1 | |
Mutagenesisi | 253 | Y → F: 55-fold reduction in GS-hydroquinone reductase activity. 1 Publication | 1 | |
Mutagenesisi | 296 | Y → F: 22-fold reduction in GS-hydroquinone reductase activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000169436 | 1 – 328 | Glutathionyl-hydroquinone reductase YqjGAdd BLAST | 328 |
Proteomic databases
jPOSTi | P42620 |
PaxDbi | P42620 |
PRIDEi | P42620 |
Interactioni
Subunit structurei
Homodimer.
2 PublicationsProtein-protein interaction databases
BioGRIDi | 4260937, 21 interactors 851931, 3 interactors |
DIPi | DIP-12888N |
IntActi | P42620, 13 interactors |
STRINGi | 511145.b3102 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P42620 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 172 – 296 | GST C-terminalAdd BLAST | 125 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 130 – 133 | Glutathione binding2 Publications | 4 | |
Regioni | 148 – 149 | Glutathione binding2 Publications | 2 | |
Regioni | 203 – 311 | DimerizationAdd BLAST | 109 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0435, Bacteria |
HOGENOMi | CLU_037263_0_1_6 |
InParanoidi | P42620 |
PhylomeDBi | P42620 |
Family and domain databases
InterProi | View protein in InterPro IPR010987, Glutathione-S-Trfase_C-like IPR036282, Glutathione-S-Trfase_C_sf IPR040079, Glutathione_S-Trfase IPR004045, Glutathione_S-Trfase_N IPR016639, GST_Omega/GSH IPR036249, Thioredoxin-like_sf |
PANTHERi | PTHR32419, PTHR32419, 1 hit |
Pfami | View protein in Pfam PF13409, GST_N_2, 1 hit |
PIRSFi | PIRSF015753, GST, 1 hit |
SFLDi | SFLDS00019, Glutathione_Transferase_(cytos, 1 hit SFLDG01206, Xi.1, 1 hit |
SUPFAMi | SSF47616, SSF47616, 1 hit SSF52833, SSF52833, 1 hit |
PROSITEi | View protein in PROSITE PS50405, GST_CTER, 1 hit |
i Sequence
Sequence statusi: Complete.
P42620-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MGQLIDGVWH DTWYDTKSTG GKFQRSASAF RNWLTADGAP GPTGTGGFIA
60 70 80 90 100
EKDRYHLYVS LACPWAHRTL IMRKLKGLEP FISVSVVNPL MLENGWTFDD
110 120 130 140 150
SFPGATGDTL YQNEFLYQLY LHADPHYSGR VTVPVLWDKK NHTIVSNESA
160 170 180 190 200
EIIRMFNTAF DALGAKAGDY YPPALQTKID ELNGWIYDTV NNGVYKAGFA
210 220 230 240 250
TSQEAYDEAV AKVFESLARL EQILGQHRYL TGNQLTEADI RLWTTLVRFD
260 270 280 290 300
PVYVTHFKCD KHRISDYLNL YGFLRDIYQM PGIAETVNFD HIRNHYFRSH
310 320
KTINPTGIIS IGPWQDLDEP HGRDVRFG
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U18997 Genomic DNA Translation: AAA57906.1 U00096 Genomic DNA Translation: AAC76137.1 AP009048 Genomic DNA Translation: BAE77152.1 |
PIRi | C65099 |
RefSeqi | NP_417573.1, NC_000913.3 WP_000531213.1, NZ_LN832404.1 |
Genome annotation databases
EnsemblBacteriai | AAC76137; AAC76137; b3102 BAE77152; BAE77152; BAE77152 |
GeneIDi | 57728229 947615 |
KEGGi | ecj:JW3073 eco:b3102 |
PATRICi | fig|511145.12.peg.3198 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U18997 Genomic DNA Translation: AAA57906.1 U00096 Genomic DNA Translation: AAC76137.1 AP009048 Genomic DNA Translation: BAE77152.1 |
PIRi | C65099 |
RefSeqi | NP_417573.1, NC_000913.3 WP_000531213.1, NZ_LN832404.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3R3E | X-ray | 2.20 | A/B | 1-328 | [»] | |
4G0I | X-ray | 2.05 | A/B | 1-328 | [»] | |
4G0K | X-ray | 2.56 | A/B | 1-328 | [»] | |
4G0L | X-ray | 2.62 | A/B | 1-328 | [»] | |
SMRi | P42620 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4260937, 21 interactors 851931, 3 interactors |
DIPi | DIP-12888N |
IntActi | P42620, 13 interactors |
STRINGi | 511145.b3102 |
Proteomic databases
jPOSTi | P42620 |
PaxDbi | P42620 |
PRIDEi | P42620 |
Genome annotation databases
EnsemblBacteriai | AAC76137; AAC76137; b3102 BAE77152; BAE77152; BAE77152 |
GeneIDi | 57728229 947615 |
KEGGi | ecj:JW3073 eco:b3102 |
PATRICi | fig|511145.12.peg.3198 |
Organism-specific databases
EchoBASEi | EB2602 |
Phylogenomic databases
eggNOGi | COG0435, Bacteria |
HOGENOMi | CLU_037263_0_1_6 |
InParanoidi | P42620 |
PhylomeDBi | P42620 |
Enzyme and pathway databases
BioCyci | EcoCyc:G7616-MONOMER MetaCyc:G7616-MONOMER |
Miscellaneous databases
PROi | PR:P42620 |
Family and domain databases
InterProi | View protein in InterPro IPR010987, Glutathione-S-Trfase_C-like IPR036282, Glutathione-S-Trfase_C_sf IPR040079, Glutathione_S-Trfase IPR004045, Glutathione_S-Trfase_N IPR016639, GST_Omega/GSH IPR036249, Thioredoxin-like_sf |
PANTHERi | PTHR32419, PTHR32419, 1 hit |
Pfami | View protein in Pfam PF13409, GST_N_2, 1 hit |
PIRSFi | PIRSF015753, GST, 1 hit |
SFLDi | SFLDS00019, Glutathione_Transferase_(cytos, 1 hit SFLDG01206, Xi.1, 1 hit |
SUPFAMi | SSF47616, SSF47616, 1 hit SSF52833, SSF52833, 1 hit |
PROSITEi | View protein in PROSITE PS50405, GST_CTER, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | YQJG_ECOLI | |
Accessioni | P42620Primary (citable) accession number: P42620 Secondary accession number(s): Q2M9A4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1995 |
Last sequence update: | November 1, 1995 | |
Last modified: | April 7, 2021 | |
This is version 141 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families