MULTISPECIES: glutathione S-transferase family protein [Enterobacteriaceae]
glutathione S-transferase family protein( domain architecture ID 11427749)
glutathione S-transferase (GST) family protein may catalyze the conjugation of reduced glutathione to a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
GstA | COG0625 | Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; |
1-203 | 2.27e-30 | ||||
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; : Pssm-ID: 440390 [Multi-domain] Cd Length: 205 Bit Score: 110.76 E-value: 2.27e-30
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Name | Accession | Description | Interval | E-value | ||||
GstA | COG0625 | Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; |
1-203 | 2.27e-30 | ||||
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440390 [Multi-domain] Cd Length: 205 Bit Score: 110.76 E-value: 2.27e-30
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GST_N_Beta | cd03057 | GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ... |
2-79 | 2.81e-24 | ||||
GST_N 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit limited GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they also bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH. Pssm-ID: 239355 [Multi-domain] Cd Length: 77 Bit Score: 91.06 E-value: 2.81e-24
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PRK10542 | PRK10542 | glutathionine S-transferase; Provisional |
46-200 | 6.45e-15 | ||||
glutathionine S-transferase; Provisional Pssm-ID: 182533 [Multi-domain] Cd Length: 201 Bit Score: 70.10 E-value: 6.45e-15
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GST_N_2 | pfam13409 | Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798. |
17-78 | 3.24e-06 | ||||
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798. Pssm-ID: 433184 [Multi-domain] Cd Length: 68 Bit Score: 43.39 E-value: 3.24e-06
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Name | Accession | Description | Interval | E-value | ||||
GstA | COG0625 | Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; |
1-203 | 2.27e-30 | ||||
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440390 [Multi-domain] Cd Length: 205 Bit Score: 110.76 E-value: 2.27e-30
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GST_N_Beta | cd03057 | GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ... |
2-79 | 2.81e-24 | ||||
GST_N 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit limited GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they also bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH. Pssm-ID: 239355 [Multi-domain] Cd Length: 77 Bit Score: 91.06 E-value: 2.81e-24
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GST_C_Beta | cd03188 | C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ... |
88-199 | 4.80e-21 | ||||
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: 83.84 E-value: 4.80e-21
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PRK10542 | PRK10542 | glutathionine S-transferase; Provisional |
46-200 | 6.45e-15 | ||||
glutathionine S-transferase; Provisional Pssm-ID: 182533 [Multi-domain] Cd Length: 201 Bit Score: 70.10 E-value: 6.45e-15
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GST_N_family | cd00570 | Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ... |
2-71 | 6.16e-07 | ||||
Glutathione S-transferase (GST) family, N-terminal 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 subfamily, a member of the DsbA family). 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. 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, metaxin 2 and stringent starvation protein A. Pssm-ID: 238319 [Multi-domain] Cd Length: 71 Bit Score: 45.26 E-value: 6.16e-07
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GST_N_2 | pfam13409 | Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798. |
17-78 | 3.24e-06 | ||||
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798. Pssm-ID: 433184 [Multi-domain] Cd Length: 68 Bit Score: 43.39 E-value: 3.24e-06
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GST_N_4 | cd03056 | GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ... |
16-70 | 8.13e-06 | ||||
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with similarity to GSTs. 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Pssm-ID: 239354 [Multi-domain] Cd Length: 73 Bit Score: 42.18 E-value: 8.13e-06
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GST_N_GTT1_like | cd03046 | GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ... |
2-79 | 1.91e-05 | ||||
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly uncharacterized proteins with similarity to the S. cerevisiae GST protein, GTT1, and the Schizosaccharomyces pombe GST-III. 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GTT1, a homodimer, exhibits GST activity with standard substrates and associates with the endoplasmic reticulum. Its expression is induced after diauxic shift and remains high throughout the stationary phase. S. pombe GST-III is implicated in the detoxification of various metals. Pssm-ID: 239344 [Multi-domain] Cd Length: 76 Bit Score: 41.33 E-value: 1.91e-05
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GST_N_3 | pfam13417 | Glutathione S-transferase, N-terminal domain; |
17-80 | 1.87e-04 | ||||
Glutathione S-transferase, N-terminal domain; Pssm-ID: 433190 [Multi-domain] Cd Length: 75 Bit Score: 38.75 E-value: 1.87e-04
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sspA | PRK09481 | stringent starvation protein A; Provisional |
29-163 | 1.81e-03 | ||||
stringent starvation protein A; Provisional Pssm-ID: 236537 [Multi-domain] Cd Length: 211 Bit Score: 37.77 E-value: 1.81e-03
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Blast search parameters | ||||
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