MULTISPECIES: glutathionyl-hydroquinone reductase YqjG [Enterobacteriaceae]
Protein Classification
glutathione S-transferase family protein( domain architecture ID 11418207)
glutathione S-transferase family protein similar to Saccharomyces cerevisiae glutathione S-transferase omega-like proteins and Escherichia coli glutathionyl-hydroquinone reductase
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| ECM4 | COG0435 | Glutathionyl-hydroquinone reductase [Energy production and conversion]; |
1-328 | 0e+00 | ||||||
Glutathionyl-hydroquinone reductase [Energy production and conversion]; : Pssm-ID: 440204 [Multi-domain] Cd Length: 321 Bit Score: 652.19 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||
| ECM4 | COG0435 | Glutathionyl-hydroquinone reductase [Energy production and conversion]; |
1-328 | 0e+00 | ||||||
Glutathionyl-hydroquinone reductase [Energy production and conversion]; Pssm-ID: 440204 [Multi-domain] Cd Length: 321 Bit Score: 652.19 E-value: 0e+00
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| GST_C_Omega_like | cd03190 | C-terminal, alpha helical domain of Class Omega-like Glutathione S-transferases; Glutathione ... |
172-313 | 1.11e-82 | ||||||
C-terminal, alpha helical domain of Class Omega-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae Omega-like subfamily; composed of three Saccharomyces cerevisiae GST omega-like (Gto) proteins, Gto1p, Gto2p (also known as Extracellular mutant protein 4 or ECM4p), and Gto3p, as well as similar uncharacterized proteins from fungi and bacteria. The three Saccharomyces cerevisiae Gto proteins are omega-class GSTs with low or no GST activity against standard substrates, but have glutaredoxin/thiol oxidoreductase and dehydroascorbate reductase activity through a single cysteine residue in the active site. Gto1p is located in the peroxisomes while Gto2p and Gto3p are cytosolic. The gene encoding Gto2p, called ECM4, is involved in cell surface biosynthesis and architecture. S. cerevisiae ECM4 mutants show increased amounts of the cell wall hexose, N-acetylglucosamine. More recently, global gene expression analysis shows that ECM4 is upregulated during genotoxic conditions and together with the expression profiles of 18 other genes could potentially differentiate between genotoxic and cytotoxic insults in yeast. Pssm-ID: 198299 [Multi-domain] Cd Length: 142 Bit Score: 246.72 E-value: 1.11e-82
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| GST_C_2 | pfam13410 | Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043. |
205-268 | 7.77e-11 | ||||||
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043. Pssm-ID: 433185 [Multi-domain] Cd Length: 67 Bit Score: 56.95 E-value: 7.77e-11
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| Name | Accession | Description | Interval | E-value | ||||||
| ECM4 | COG0435 | Glutathionyl-hydroquinone reductase [Energy production and conversion]; |
1-328 | 0e+00 | ||||||
Glutathionyl-hydroquinone reductase [Energy production and conversion]; Pssm-ID: 440204 [Multi-domain] Cd Length: 321 Bit Score: 652.19 E-value: 0e+00
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| GST_C_Omega_like | cd03190 | C-terminal, alpha helical domain of Class Omega-like Glutathione S-transferases; Glutathione ... |
172-313 | 1.11e-82 | ||||||
C-terminal, alpha helical domain of Class Omega-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae Omega-like subfamily; composed of three Saccharomyces cerevisiae GST omega-like (Gto) proteins, Gto1p, Gto2p (also known as Extracellular mutant protein 4 or ECM4p), and Gto3p, as well as similar uncharacterized proteins from fungi and bacteria. The three Saccharomyces cerevisiae Gto proteins are omega-class GSTs with low or no GST activity against standard substrates, but have glutaredoxin/thiol oxidoreductase and dehydroascorbate reductase activity through a single cysteine residue in the active site. Gto1p is located in the peroxisomes while Gto2p and Gto3p are cytosolic. The gene encoding Gto2p, called ECM4, is involved in cell surface biosynthesis and architecture. S. cerevisiae ECM4 mutants show increased amounts of the cell wall hexose, N-acetylglucosamine. More recently, global gene expression analysis shows that ECM4 is upregulated during genotoxic conditions and together with the expression profiles of 18 other genes could potentially differentiate between genotoxic and cytotoxic insults in yeast. Pssm-ID: 198299 [Multi-domain] Cd Length: 142 Bit Score: 246.72 E-value: 1.11e-82
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| GST_C_2 | pfam13410 | Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043. |
205-268 | 7.77e-11 | ||||||
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043. Pssm-ID: 433185 [Multi-domain] Cd Length: 67 Bit Score: 56.95 E-value: 7.77e-11
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| GST_N_2 | pfam13409 | Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798. |
62-159 | 6.65e-09 | ||||||
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798. Pssm-ID: 433184 [Multi-domain] Cd Length: 68 Bit Score: 51.86 E-value: 6.65e-09
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| GST_C_family | cd00299 | C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ... |
179-269 | 7.29e-09 | ||||||
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione S-transferase (GST) family, C-terminal alpha helical domain; a large, diverse group of cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. In addition, GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. This family, also referred to as soluble GSTs, is the largest family of GSH transferases and is only distantly related to the mitochondrial GSTs (GSTK). Soluble GSTs bear no structural similarity to microsomal GSTs (MAPEG family) and display additional activities unique to their group, such as catalyzing thiolysis, reduction and isomerization of certain compounds. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Based on sequence similarity, different classes of GSTs have been identified, which display varying tissue distribution, substrate specificities and additional specific activities. In humans, GSTs display polymorphisms which may influence individual susceptibility to diseases such as cancer, arthritis, allergy and sclerosis. Some GST family members with non-GST functions include glutaredoxin 2, the CLIC subfamily of anion channels, prion protein Ure2p, crystallins, metaxins, stringent starvation protein A, and aminoacyl-tRNA synthetases. Pssm-ID: 198286 [Multi-domain] Cd Length: 100 Bit Score: 52.50 E-value: 7.29e-09
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| GstA | COG0625 | Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; |
57-287 | 5.50e-08 | ||||||
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440390 [Multi-domain] Cd Length: 205 Bit Score: 52.21 E-value: 5.50e-08
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| GST_C | pfam00043 | Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ... |
195-240 | 4.24e-05 | ||||||
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety of targets including S-crystallin from squid, the eukaryotic elongation factor 1-gamma, the HSP26 family of stress-related proteins and auxin-regulated proteins in plants. Stringent starvation proteins in E. coli are also included in the alignment but are not known to have GST activity. The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed to reside in the N-terminal domain. In plants, GSTs are encoded by a large gene family (48 GST genes in Arabidopsis) and can be divided into the phi, tau, theta, zeta, and lambda classes. Pssm-ID: 459647 [Multi-domain] Cd Length: 93 Bit Score: 41.50 E-value: 4.24e-05
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| GST_C_3 | pfam14497 | Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043. |
203-285 | 1.14e-04 | ||||||
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043. Pssm-ID: 464190 [Multi-domain] Cd Length: 104 Bit Score: 40.62 E-value: 1.14e-04
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| GST_C_Delta_Epsilon | cd03177 | C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; ... |
194-250 | 4.20e-04 | ||||||
C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The class Delta and Epsilon subfamily is made up primarily of insect GSTs, which play major roles in insecticide resistance by facilitating reductive dehydrochlorination of insecticides or conjugating them with GSH to produce water-soluble metabolites that are easily excreted. They are also implicated in protection against cellular damage by oxidative stress. Pssm-ID: 198287 [Multi-domain] Cd Length: 117 Bit Score: 39.44 E-value: 4.20e-04
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| GST_C_Beta | cd03188 | C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ... |
190-285 | 9.23e-04 | ||||||
C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they are involved in the protection against oxidative stress and are able to bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs, contributing to antibiotic resistance. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH. One member of this subfamily is a GST from Burkholderia xenovorans LB400 that is encoded by the bphK gene and is part of the biphenyl catabolic pathway. Pssm-ID: 198297 [Multi-domain] Cd Length: 113 Bit Score: 38.38 E-value: 9.23e-04
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| GST_C_Mu | cd03209 | C-terminal, alpha helical domain of Class Mu Glutathione S-transferases; Glutathione ... |
210-303 | 5.64e-03 | ||||||
C-terminal, alpha helical domain of Class Mu Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Mu subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The class Mu subfamily is composed of eukaryotic GSTs. In rats, at least six distinct class Mu subunits have been identified, with homologous genes in humans for five of these subunits. Class Mu GSTs can form homodimers and heterodimers, giving a large number of possible isoenzymes that can be formed, all with overlapping activities but different substrate specificities. They are the most abundant GSTs in human liver, skeletal muscle and brain, and are believed to provide protection against diseases including cancer and neurodegenerative disorders. Some isoenzymes have additional specific functions. Human GST M1-1 acts as an endogenous inhibitor of ASK1 (apoptosis signal-regulating kinase 1) thereby suppressing ASK1-mediated cell death. Human GSTM2-2 and 3-3 have been identified as prostaglandin E2 synthases in the brain and may play crucial roles in temperature and sleep-wake regulation. Pssm-ID: 198318 [Multi-domain] Cd Length: 121 Bit Score: 36.46 E-value: 5.64e-03
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