glutathione S-transferase U17-like [Phoenix dactylifera]
Protein Classification
glutathione S-transferase( domain architecture ID 10122769)
glutathione S-transferase (GST) catalyzes 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; such as plant tau class GSTs that are primarily responsible for herbicide detoxification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||
| GST_C_Tau | cd03185 | C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione ... |
167-295 | 9.52e-62 | |||
C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Tau 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 plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones. : Pssm-ID: 198294 [Multi-domain] Cd Length: 127 Bit Score: 192.01 E-value: 9.52e-62
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| GST_N_Tau | cd03058 | GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ... |
82-155 | 5.90e-46 | |||
GST_N family, Class Tau 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. The plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones. : Pssm-ID: 239356 [Multi-domain] Cd Length: 74 Bit Score: 149.74 E-value: 5.90e-46
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| Name | Accession | Description | Interval | E-value | ||||
| GST_C_Tau | cd03185 | C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione ... |
167-295 | 9.52e-62 | ||||
C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Tau 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 plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones. Pssm-ID: 198294 [Multi-domain] Cd Length: 127 Bit Score: 192.01 E-value: 9.52e-62
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| GST_N_Tau | cd03058 | GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ... |
82-155 | 5.90e-46 | ||||
GST_N family, Class Tau 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. The plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones. Pssm-ID: 239356 [Multi-domain] Cd Length: 74 Bit Score: 149.74 E-value: 5.90e-46
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| GstA | COG0625 | Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; |
83-286 | 8.72e-36 | ||||
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440390 [Multi-domain] Cd Length: 205 Bit Score: 127.70 E-value: 8.72e-36
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| GST_N | pfam02798 | Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ... |
80-153 | 1.32e-15 | ||||
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to a variety of targets. Also included in the alignment, but not GSTs: S-crystallins from squid (similarity to GST previously noted); eukaryotic elongation factors 1-gamma (not known to have GST activity and similarity not previously recognized); HSP26 family of stress-related proteins including auxin-regulated proteins in plants and stringent starvation proteins in E. coli (not known to have GST activity and similarity not previously recognized). The glutathione molecule binds in a cleft between the N- and C-terminal domains - the catalytically important residues are proposed to reside in the N-terminal domain. Pssm-ID: 460698 [Multi-domain] Cd Length: 76 Bit Score: 70.41 E-value: 1.32e-15
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| maiA | TIGR01262 | maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and ... |
83-287 | 7.13e-15 | ||||
maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and phenylalanine catabolism. It requires glutathione and belongs by homology to the zeta family of glutathione S-transferases. The enzyme (EC 5.2.1.2) is described as active also on maleylpyruvate, and the example from a Ralstonia sp. catabolic plasmid is described as a maleylpyruvate isomerase involved in gentisate catabolism. [Energy metabolism, Amino acids and amines] Pssm-ID: 273527 [Multi-domain] Cd Length: 210 Bit Score: 71.97 E-value: 7.13e-15
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| PRK10357 | PRK10357 | putative glutathione S-transferase; Provisional |
83-247 | 4.63e-12 | ||||
putative glutathione S-transferase; Provisional Pssm-ID: 182405 [Multi-domain] Cd Length: 202 Bit Score: 63.97 E-value: 4.63e-12
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| GST_C | pfam00043 | Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ... |
175-276 | 6.03e-08 | ||||
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: 49.59 E-value: 6.03e-08
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| sspA | PRK09481 | stringent starvation protein A; Provisional |
95-209 | 3.85e-07 | ||||
stringent starvation protein A; Provisional Pssm-ID: 236537 [Multi-domain] Cd Length: 211 Bit Score: 49.71 E-value: 3.85e-07
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| GrxB | COG2999 | Glutaredoxin 2 [Posttranslational modification, protein turnover, chaperones]; |
91-167 | 8.17e-03 | ||||
Glutaredoxin 2 [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 442237 [Multi-domain] Cd Length: 215 Bit Score: 36.74 E-value: 8.17e-03
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| Name | Accession | Description | Interval | E-value | ||||
| GST_C_Tau | cd03185 | C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione ... |
167-295 | 9.52e-62 | ||||
C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Tau 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 plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones. Pssm-ID: 198294 [Multi-domain] Cd Length: 127 Bit Score: 192.01 E-value: 9.52e-62
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| GST_N_Tau | cd03058 | GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ... |
82-155 | 5.90e-46 | ||||
GST_N family, Class Tau 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. The plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones. Pssm-ID: 239356 [Multi-domain] Cd Length: 74 Bit Score: 149.74 E-value: 5.90e-46
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| GstA | COG0625 | Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; |
83-286 | 8.72e-36 | ||||
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440390 [Multi-domain] Cd Length: 205 Bit Score: 127.70 E-value: 8.72e-36
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| GST_N | pfam02798 | Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ... |
80-153 | 1.32e-15 | ||||
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to a variety of targets. Also included in the alignment, but not GSTs: S-crystallins from squid (similarity to GST previously noted); eukaryotic elongation factors 1-gamma (not known to have GST activity and similarity not previously recognized); HSP26 family of stress-related proteins including auxin-regulated proteins in plants and stringent starvation proteins in E. coli (not known to have GST activity and similarity not previously recognized). The glutathione molecule binds in a cleft between the N- and C-terminal domains - the catalytically important residues are proposed to reside in the N-terminal domain. Pssm-ID: 460698 [Multi-domain] Cd Length: 76 Bit Score: 70.41 E-value: 1.32e-15
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| GST_N_3 | pfam13417 | Glutathione S-transferase, N-terminal domain; |
84-153 | 2.93e-15 | ||||
Glutathione S-transferase, N-terminal domain; Pssm-ID: 433190 [Multi-domain] Cd Length: 75 Bit Score: 69.56 E-value: 2.93e-15
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| maiA | TIGR01262 | maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and ... |
83-287 | 7.13e-15 | ||||
maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and phenylalanine catabolism. It requires glutathione and belongs by homology to the zeta family of glutathione S-transferases. The enzyme (EC 5.2.1.2) is described as active also on maleylpyruvate, and the example from a Ralstonia sp. catabolic plasmid is described as a maleylpyruvate isomerase involved in gentisate catabolism. [Energy metabolism, Amino acids and amines] Pssm-ID: 273527 [Multi-domain] Cd Length: 210 Bit Score: 71.97 E-value: 7.13e-15
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| GST_N_family | cd00570 | Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ... |
82-152 | 1.45e-14 | ||||
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: 67.21 E-value: 1.45e-14
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| PRK10357 | PRK10357 | putative glutathione S-transferase; Provisional |
83-247 | 4.63e-12 | ||||
putative glutathione S-transferase; Provisional Pssm-ID: 182405 [Multi-domain] Cd Length: 202 Bit Score: 63.97 E-value: 4.63e-12
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| GST_N_2 | pfam13409 | Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798. |
89-153 | 1.19e-10 | ||||
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798. Pssm-ID: 433184 [Multi-domain] Cd Length: 68 Bit Score: 56.48 E-value: 1.19e-10
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| GST_N_Zeta | cd03042 | GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ... |
83-152 | 1.27e-09 | ||||
GST_N family, Class Zeta 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. Class Zeta GSTs, also known as maleylacetoacetate (MAA) isomerases, catalyze the isomerization of MAA to fumarylacetoacetate, the penultimate step in tyrosine/phenylalanine catabolism, using GSH as a cofactor. They show little GSH-conjugating activity towards traditional GST substrates but display modest GSH peroxidase activity. They are also implicated in the detoxification of the carcinogen dichloroacetic acid by catalyzing its dechlorination to glyoxylic acid. Pssm-ID: 239340 [Multi-domain] Cd Length: 73 Bit Score: 53.73 E-value: 1.27e-09
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| GST_C | pfam00043 | Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ... |
175-276 | 6.03e-08 | ||||
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: 49.59 E-value: 6.03e-08
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| GST_C_family | cd00299 | C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ... |
173-273 | 7.02e-08 | ||||
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: 49.80 E-value: 7.02e-08
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| GST_C_2 | pfam13410 | Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043. |
199-273 | 3.58e-07 | ||||
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043. Pssm-ID: 433185 [Multi-domain] Cd Length: 67 Bit Score: 46.54 E-value: 3.58e-07
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| sspA | PRK09481 | stringent starvation protein A; Provisional |
95-209 | 3.85e-07 | ||||
stringent starvation protein A; Provisional Pssm-ID: 236537 [Multi-domain] Cd Length: 211 Bit Score: 49.71 E-value: 3.85e-07
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| GST_N_Phi | cd03053 | GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ... |
82-153 | 8.58e-07 | ||||
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related fungal and bacterial proteins. 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. The class Phi GST subfamily has experience extensive gene duplication. The Arabidopsis and Oryza genomes contain 13 and 16 Phi GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Tau GSTs, showing class specificity in substrate preference. Phi enzymes are highly reactive toward chloroacetanilide and thiocarbamate herbicides. Some Phi GSTs have other functions including transport of flavonoid pigments to the vacuole, shoot regeneration and GSH peroxidase activity. Pssm-ID: 239351 [Multi-domain] Cd Length: 76 Bit Score: 45.72 E-value: 8.58e-07
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| GST_N_SspA | cd03059 | GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ... |
91-153 | 2.25e-06 | ||||
GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP)-associated protein required for the lytic development of phage P1 and for stationary phase-induced acid tolerance of E. coli. It is implicated in survival during nutrient starvation. SspA adopts the GST fold with an N-terminal TRX-fold domain and a C-terminal alpha helical domain, but it does not bind glutathione (GSH) and lacks GST activity. SspA is highly conserved among gram-negative bacteria. Related proteins found in Neisseria (called RegF), Francisella and Vibrio regulate the expression of virulence factors necessary for pathogenesis. Pssm-ID: 239357 [Multi-domain] Cd Length: 73 Bit Score: 44.63 E-value: 2.25e-06
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| GST_N_Omega | cd03055 | GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ... |
91-152 | 3.66e-06 | ||||
GST_N family, Class Omega 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. Class Omega GSTs show little or no GSH-conjugating activity towards standard GST substrates. Instead, they catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins. They contain a conserved cysteine equivalent to the first cysteine in the CXXC motif of glutaredoxins, which is a redox active residue capable of reducing GSH mixed disulfides in a monothiol mechanism. Polymorphisms of the class Omega GST genes may be associated with the development of some types of cancer and the age-at-onset of both Alzheimer's and Parkinson's diseases. Pssm-ID: 239353 [Multi-domain] Cd Length: 89 Bit Score: 44.65 E-value: 3.66e-06
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| GST_N_3 | cd03049 | GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with ... |
83-152 | 4.01e-06 | ||||
GST_N family, unknown subfamily 3; 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: 239347 [Multi-domain] Cd Length: 73 Bit Score: 43.79 E-value: 4.01e-06
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| GST_C_Beta | cd03188 | C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ... |
184-281 | 1.21e-05 | ||||
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: 43.77 E-value: 1.21e-05
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| GST_N_etherase_LigE | cd03038 | GST_N family, Beta etherase LigE subfamily; composed of proteins similar to Sphingomonas ... |
90-153 | 1.91e-05 | ||||
GST_N family, Beta etherase LigE subfamily; composed of proteins similar to Sphingomonas paucimobilis beta etherase, LigE, a GST-like protein that catalyzes the cleavage of the beta-aryl ether linkages present in low-moleculer weight lignins using GSH as the hydrogen donor. This reaction is an essential step in the degradation of lignin, a complex phenolic polymer that is the most abundant aromatic material in the biosphere. The beta etherase activity of LigE is enantioselective and it complements the activity of the other GST family beta etherase, LigF. Pssm-ID: 239336 [Multi-domain] Cd Length: 84 Bit Score: 42.33 E-value: 1.91e-05
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| PRK15113 | PRK15113 | glutathione transferase; |
88-240 | 2.14e-05 | ||||
glutathione transferase; Pssm-ID: 185068 [Multi-domain] Cd Length: 214 Bit Score: 44.56 E-value: 2.14e-05
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| GST_C_Omega | cd03184 | C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione ... |
185-295 | 1.16e-04 | ||||
C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Omega 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. Class Omega GSTs show little or no GSH-conjugating activity towards standard GST substrates. Instead, they catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins. They contain a conserved cysteine equivalent to the first cysteine in the CXXC motif of glutaredoxins, which is a redox active residue capable of reducing GSH mixed disulfides in a monothiol mechanism. Polymorphisms of the class Omega GST genes may be associated with the development of some types of cancer and the age-at-onset of both Alzheimer's and Parkinson's diseases. Pssm-ID: 198293 [Multi-domain] Cd Length: 124 Bit Score: 41.15 E-value: 1.16e-04
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| GST_N_GRX2 | cd03037 | GST_N family, Glutaredoxin 2 (GRX2) subfamily; composed of bacterial proteins similar to E. ... |
91-152 | 1.07e-03 | ||||
GST_N family, Glutaredoxin 2 (GRX2) subfamily; composed of bacterial proteins similar to E. coli GRX2, an atypical GRX with a molecular mass of about 24kD, compared with other GRXs which are 9-12kD in size. GRX2 adopts a GST fold containing an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. It contains a redox active CXXC motif located in the N-terminal domain but is not able to reduce ribonucleotide reductase like other GRXs. However, it catalyzes GSH-dependent protein disulfide reduction of other substrates efficiently. GRX2 is thought to function primarily in catalyzing the reversible glutathionylation of proteins in cellular redox regulation including stress responses. Pssm-ID: 239335 [Multi-domain] Cd Length: 71 Bit Score: 36.99 E-value: 1.07e-03
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| GST_C_6 | cd03205 | C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; ... |
205-285 | 1.45e-03 | ||||
C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 6; composed of uncharacterized bacterial proteins with similarity to GSTs, including Pseudomonas fluorescens GST with a known three-dimensional structure. 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. Though the three-dimensional structure of Pseudomonas fluorescens GST has been determined, there is no information on its functional characterization. Pssm-ID: 198314 [Multi-domain] Cd Length: 109 Bit Score: 37.57 E-value: 1.45e-03
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| GST_N_GTT1_like | cd03046 | GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ... |
95-151 | 4.33e-03 | ||||
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: 35.56 E-value: 4.33e-03
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| GST_N_4 | cd03056 | GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ... |
95-150 | 4.87e-03 | ||||
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: 35.24 E-value: 4.87e-03
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| GrxB | COG2999 | Glutaredoxin 2 [Posttranslational modification, protein turnover, chaperones]; |
91-167 | 8.17e-03 | ||||
Glutaredoxin 2 [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 442237 [Multi-domain] Cd Length: 215 Bit Score: 36.74 E-value: 8.17e-03
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