dehydroascorbate reductase 1 [Arabidopsis thaliana]
Protein Classification
glutathione S-transferase family protein( domain architecture ID 11477165)
glutathione S-transferase family protein similar to Arabidopsis thaliana glutathione S-transferase DHAR1 that exhibitsglutathione-dependent thiol transferase and dehydroascorbate (DHA)reductase activities
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| PLN02817 | PLN02817 | glutathione dehydrogenase (ascorbate) |
3-258 | 0e+00 | |||||
glutathione dehydrogenase (ascorbate) : Pssm-ID: 166458 [Multi-domain] Cd Length: 265 Bit Score: 512.23 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||
| PLN02817 | PLN02817 | glutathione dehydrogenase (ascorbate) |
3-258 | 0e+00 | |||||
glutathione dehydrogenase (ascorbate) Pssm-ID: 166458 [Multi-domain] Cd Length: 265 Bit Score: 512.23 E-value: 0e+00
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| GST_C_DHAR | cd03201 | C-terminal, alpha helical domain of Dehydroascorbate Reductase; Glutathione S-transferase (GST) ... |
135-255 | 5.15e-79 | |||||
C-terminal, alpha helical domain of Dehydroascorbate Reductase; Glutathione S-transferase (GST) C-terminal domain family, Dehydroascorbate Reductase (DHAR) subfamily; composed of plant-specific DHARs, which are monomeric enzymes catalyzing the reduction of DHA into ascorbic acid (AsA) using glutathione as the reductant. DHAR allows plants to recycle oxidized AsA before it is lost. AsA serves as a cofactor of violaxanthin de-epoxidase in the xanthophyll cycle and as an antioxidant in the detoxification of reactive oxygen species. Because AsA is the major reductant in plants, DHAR serves to regulate their redox state. It has been suggested that a significant portion of DHAR activity is plastidic, acting to reduce the large amounts of ascorbate oxidized during hydrogen peroxide scavenging by ascorbate peroxidase. DHAR contains a conserved cysteine in its active site and in addition to its reductase activity, shows thiol transferase activity similar to glutaredoxins. Pssm-ID: 198310 Cd Length: 121 Bit Score: 233.85 E-value: 5.15e-79
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| GstA | COG0625 | Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; |
66-250 | 1.15e-29 | |||||
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440390 [Multi-domain] Cd Length: 205 Bit Score: 110.37 E-value: 1.15e-29
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| O-ClC | TIGR00862 | intracellular chloride channel protein; The Organellar Chloride Channel (O-ClC) Family (TC 1.A. ... |
49-248 | 2.20e-26 | |||||
intracellular chloride channel protein; The Organellar Chloride Channel (O-ClC) Family (TC 1.A.12) Proteins of the O-ClC family are voltage-sensitive chloride channels found in intracellular membranes but not the plasma membranes of animal cells. They are found in human nuclear membranes, and the bovine protein targets to the microsomes, but not the plasma membrane, when expressed in Xenopus laevis oocytes. These proteins are thought to function in the regulation of the membrane potential and in transepithelial ion absorption and secretion in the kidney. [Transport and binding proteins, Anions] Pssm-ID: 129941 [Multi-domain] Cd Length: 236 Bit Score: 102.63 E-value: 2.20e-26
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| GST_N_3 | pfam13417 | Glutathione S-transferase, N-terminal domain; |
65-134 | 1.47e-17 | |||||
Glutathione S-transferase, N-terminal domain; Pssm-ID: 433190 [Multi-domain] Cd Length: 75 Bit Score: 74.96 E-value: 1.47e-17
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| Name | Accession | Description | Interval | E-value | |||||
| PLN02817 | PLN02817 | glutathione dehydrogenase (ascorbate) |
3-258 | 0e+00 | |||||
glutathione dehydrogenase (ascorbate) Pssm-ID: 166458 [Multi-domain] Cd Length: 265 Bit Score: 512.23 E-value: 0e+00
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| PLN02378 | PLN02378 | glutathione S-transferase DHAR1 |
49-256 | 1.24e-93 | |||||
glutathione S-transferase DHAR1 Pssm-ID: 166019 [Multi-domain] Cd Length: 213 Bit Score: 274.28 E-value: 1.24e-93
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| GST_C_DHAR | cd03201 | C-terminal, alpha helical domain of Dehydroascorbate Reductase; Glutathione S-transferase (GST) ... |
135-255 | 5.15e-79 | |||||
C-terminal, alpha helical domain of Dehydroascorbate Reductase; Glutathione S-transferase (GST) C-terminal domain family, Dehydroascorbate Reductase (DHAR) subfamily; composed of plant-specific DHARs, which are monomeric enzymes catalyzing the reduction of DHA into ascorbic acid (AsA) using glutathione as the reductant. DHAR allows plants to recycle oxidized AsA before it is lost. AsA serves as a cofactor of violaxanthin de-epoxidase in the xanthophyll cycle and as an antioxidant in the detoxification of reactive oxygen species. Because AsA is the major reductant in plants, DHAR serves to regulate their redox state. It has been suggested that a significant portion of DHAR activity is plastidic, acting to reduce the large amounts of ascorbate oxidized during hydrogen peroxide scavenging by ascorbate peroxidase. DHAR contains a conserved cysteine in its active site and in addition to its reductase activity, shows thiol transferase activity similar to glutaredoxins. Pssm-ID: 198310 Cd Length: 121 Bit Score: 233.85 E-value: 5.15e-79
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| GstA | COG0625 | Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; |
66-250 | 1.15e-29 | |||||
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440390 [Multi-domain] Cd Length: 205 Bit Score: 110.37 E-value: 1.15e-29
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| GST_C_CLIC | cd03198 | C-terminal, alpha helical domain of Chloride Intracellular Channels; Glutathione S-transferase ... |
139-253 | 8.13e-29 | |||||
C-terminal, alpha helical domain of Chloride Intracellular Channels; Glutathione S-transferase (GST) C-terminal domain family, Chloride Intracellular Channel (CLIC) subfamily; composed of CLICs (CLIC1-6 in vertebrates), p64, parchorin, and similar proteins. They are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division, and apoptosis. They can exist in both water-soluble and membrane-bound states and are found in various vesicles and membranes, and they may play roles in the maintenance of these intracellular membranes. Biochemical studies of the Caenorhabditis elegans homolog, EXC-4, show that the membrane localization domain is present in the N-terminal part of the protein. CLICs display structural plasticity, with CLIC1 adopting two soluble conformations. The structure of soluble human CLIC1 reveals that it is monomeric and adopts a fold similar to GSTs, containing an N-terminal domain with a thioredoxin fold and a C-terminal alpha helical domain. Upon oxidation, the N-terminal domain of CLIC1 undergoes a structural change to form a non-covalent dimer stabilized by the formation of an intramolecular disulfide bond between two cysteines that are far apart in the reduced form. The CLIC1 dimer bears no similarity to GST dimers. The redox-controlled structural rearrangement exposes a large hydrophobic surface, which is masked by dimerization in vitro. In vivo, this surface may represent the docking interface of CLIC1 in its membrane-bound state. The two cysteines in CLIC1 that form the disulfide bond in oxidizing conditions are essential for dimerization and chloride channel activity, however, in other subfamily members, the second cysteine is not conserved. Pssm-ID: 198307 Cd Length: 119 Bit Score: 105.77 E-value: 8.13e-29
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| O-ClC | TIGR00862 | intracellular chloride channel protein; The Organellar Chloride Channel (O-ClC) Family (TC 1.A. ... |
49-248 | 2.20e-26 | |||||
intracellular chloride channel protein; The Organellar Chloride Channel (O-ClC) Family (TC 1.A.12) Proteins of the O-ClC family are voltage-sensitive chloride channels found in intracellular membranes but not the plasma membranes of animal cells. They are found in human nuclear membranes, and the bovine protein targets to the microsomes, but not the plasma membrane, when expressed in Xenopus laevis oocytes. These proteins are thought to function in the regulation of the membrane potential and in transepithelial ion absorption and secretion in the kidney. [Transport and binding proteins, Anions] Pssm-ID: 129941 [Multi-domain] Cd Length: 236 Bit Score: 102.63 E-value: 2.20e-26
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| GST_N_3 | pfam13417 | Glutathione S-transferase, N-terminal domain; |
65-134 | 1.47e-17 | |||||
Glutathione S-transferase, N-terminal domain; Pssm-ID: 433190 [Multi-domain] Cd Length: 75 Bit Score: 74.96 E-value: 1.47e-17
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| GST_N_family | cd00570 | Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ... |
66-127 | 2.23e-17 | |||||
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: 74.15 E-value: 2.23e-17
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| GST_N_2 | pfam13409 | Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798. |
66-129 | 1.04e-16 | |||||
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798. Pssm-ID: 433184 [Multi-domain] Cd Length: 68 Bit Score: 72.28 E-value: 1.04e-16
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| GST_C_CLIC4 | cd10296 | C-terminal, alpha helical domain of Chloride Intracellular Channel 4; Glutathione ... |
139-241 | 1.25e-16 | |||||
C-terminal, alpha helical domain of Chloride Intracellular Channel 4; Glutathione S-transferase (GST) C-terminal domain family, Chloride Intracellular Channel (CLIC) 4 subfamily; CLICs are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division, and apoptosis. They can exist in both water-soluble and membrane-bound states and are found in various vesicles and membranes, and they may play roles in the maintenance of these intracellular membranes. The membrane localization domain is present in the N-terminal part of the protein. Structures of soluble CLICs reveal that they adopt a fold similar to GSTs, containing an N-terminal domain with a thioredoxin fold and a C-terminal alpha helical domain. CLIC4, also known as p64H1, is expressed ubiquitously and its localization varies depending on the nature of the cells and tissues, from the plasma membrane to subcellular compartments including the nucleus, mitochondria, ER, and the trans-Golgi network, among others. In response to cellular stress such as DNA damage and senescence, cytoplasmic CLIC4 translocates to the nucleus, where it acts on the TGF-beta pathway. Studies on knockout mice suggest that CLIC4 also plays an important role in angiogenesis, specifically in network formation, capillary sprouting, and lumen formation. CLIC4 has been found to induce apoptosis in several cell types and to retard the growth of grafted tumors in vivo. Pssm-ID: 198329 Cd Length: 141 Bit Score: 74.29 E-value: 1.25e-16
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| GST_C_CLIC6 | cd10301 | C-terminal, alpha helical domain of Chloride Intracellular Channel 6; Glutathione ... |
139-241 | 9.17e-16 | |||||
C-terminal, alpha helical domain of Chloride Intracellular Channel 6; Glutathione S-transferase (GST) C-terminal domain family, Chloride Intracellular Channel (CLIC) 6 subfamily; CLICs are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division, and apoptosis. They can exist in both water-soluble and membrane-bound states and are found in various vesicles and membranes, and they may play roles in the maintenance of these intracellular membranes. The membrane localization domain is present in the N-terminal part of the protein. Structures of soluble CLICs reveal that they adopt a fold similar to GSTs, containing an N-terminal domain with a thioredoxin fold and a C-terminal alpha helical domain. CLIC6 is expressed predominantly in the stomach, pituitary, and brain. It interacts with D2-like dopamine receptors directly and through scaffolding proteins. CLIC6 may be involved in the regulation of secretion, possibly through chloride ion transport regulation. Pssm-ID: 198334 Cd Length: 140 Bit Score: 71.97 E-value: 9.17e-16
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| sspA | PRK09481 | stringent starvation protein A; Provisional |
42-246 | 1.03e-13 | |||||
stringent starvation protein A; Provisional Pssm-ID: 236537 [Multi-domain] Cd Length: 211 Bit Score: 68.20 E-value: 1.03e-13
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| GST_C_CLIC5 | cd10297 | C-terminal, alpha helical domain of Chloride Intracellular Channel 5; Glutathione ... |
140-248 | 1.58e-13 | |||||
C-terminal, alpha helical domain of Chloride Intracellular Channel 5; Glutathione S-transferase (GST) C-terminal domain family, Chloride Intracellular Channel (CLIC) 5 subfamily; CLICs are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division, and apoptosis. They can exist in both water-soluble and membrane-bound states and are found in various vesicles and membranes, and they may play roles in the maintenance of these intracellular membranes. The membrane localization domain is present in the N-terminal part of the protein. Structures of soluble CLICs reveal that they adopt a fold similar to GSTs, containing an N-terminal domain with a thioredoxin fold and a C-terminal alpha helical domain. CLIC5 exists in two alternatively-spliced isoforms, CLIC5A or CLIC5B (also called p64). It is expressed at high levels in hair cell stereocilia and is associated with the actin cytoskeleton and ezrin. A recessive mutation in the CLIC5 gene in mice led to the lack of coordination and deafness, due to a defect in the basal region of the hair bundle causing stereocilia to degrade. CLIC5 is therefore essential for normal inner ear function. CLIC5 is also highly expressed in podocytes where it is colocalized with the ezrin/radixin/moesin (ERM) complex. It is essential for foot process integrity, and for podocyte morphology and function. Pssm-ID: 198330 Cd Length: 141 Bit Score: 66.14 E-value: 1.58e-13
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| GST_N_Omega | cd03055 | GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ... |
66-116 | 1.66e-12 | |||||
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: 61.60 E-value: 1.66e-12
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| GST_C_CLIC1 | cd10300 | C-terminal, alpha helical domain of Chloride Intracellular Channel 1; Glutathione ... |
139-248 | 1.67e-12 | |||||
C-terminal, alpha helical domain of Chloride Intracellular Channel 1; Glutathione S-transferase (GST) C-terminal domain family, Chloride Intracellular Channel (CLIC) 1 subfamily; CLICs are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division, and apoptosis. They can exist in both water-soluble and membrane-bound states and are found in various vesicles and membranes, and they may play roles in the maintenance of these intracellular membranes. The membrane localization domain is present in the N-terminal part of the protein. Soluble CLIC1 is monomeric and adopts a fold similar to GSTs, containing an N-terminal domain with a thioredoxin fold and a C-terminal alpha helical domain. Upon oxidation, the N-terminal domain of CLIC1 undergoes a structural change to form a non-covalent dimer stabilized by the formation of an intramolecular disulfide bond between two cysteines that are far apart in the reduced form. The CLIC1 dimer bears no similarity to GST dimers. The redox-controlled structural rearrangement exposes a large hydrophobic surface, which is masked by dimerization in vitro. In vivo, this surface may represent the docking interface of CLIC1 in its membrane-bound state. The two cysteines in CLIC1 that form the disulfide bond in oxidizing conditions are essential for dimerization and chloride channel activity. CLIC1 is widely expressed in many tissues and its subcellular localization is dependent on cell type and cell cycle phase. It acts as a sensor of cell oxidation and appears to have a role in diseases that involve oxidative stress including tumorigenic and neurodegenerative diseases. Pssm-ID: 198333 Cd Length: 139 Bit Score: 63.04 E-value: 1.67e-12
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| GST_C_CLIC2 | cd10298 | C-terminal, alpha helical domain of Chloride Intracellular Channel 2; Glutathione ... |
139-248 | 1.40e-11 | |||||
C-terminal, alpha helical domain of Chloride Intracellular Channel 2; Glutathione S-transferase (GST) C-terminal domain family, Chloride Intracellular Channel (CLIC) 2 subfamily; CLICs are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division, and apoptosis. They can exist in both water-soluble and membrane-bound states and are found in various vesicles and membranes, and they may play roles in the maintenance of these intracellular membranes. The membrane localization domain is present in the N-terminal part of the protein. Structures of soluble CLICs reveal that they adopt a fold similar to GSTs, containing an N-terminal domain with a thioredoxin fold and a C-terminal alpha helical domain. CLIC2 contains an intramolecular disulfide bond and exists as a monomer regardless of redox conditions, in contrast to CLIC1 which forms a dimer under oxidizing conditions. It is expressed in most tissues except the brain, and is highly expressed in the lung, spleen, and in cardiac and skeletal muscles. CLIC2 interacts with ryanodine receptors (cardiac RyR2 and skeletal RyR1) and modulates their activity, suggesting that CLIC2 may function in the regulation of calcium release and signaling in cardiac and skeletal muscles. Pssm-ID: 198331 Cd Length: 138 Bit Score: 60.66 E-value: 1.40e-11
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| GST_C_CLIC3 | cd10299 | C-terminal, alpha helical domain of Chloride Intracellular Channel 3; Glutathione ... |
139-253 | 1.04e-09 | |||||
C-terminal, alpha helical domain of Chloride Intracellular Channel 3; Glutathione S-transferase (GST) C-terminal domain family, Chloride Intracellular Channel (CLIC) 3 subfamily; CLICs are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division, and apoptosis. They can exist in both water-soluble and membrane-bound states and are found in various vesicles and membranes, and they may play roles in the maintenance of these intracellular membranes. The membrane localization domain is present in the N-terminal part of the protein. Structures of soluble CLICs reveal that they adopt a fold similar to GSTs, containing an N-terminal domain with a thioredoxin fold and a C-terminal alpha helical domain. CLIC3 is highly expressed in placental tissues, and may play a role in fetal development. Pssm-ID: 198332 Cd Length: 133 Bit Score: 55.16 E-value: 1.04e-09
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| GST_N_Ure2p_like | cd03048 | GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related ... |
58-131 | 1.46e-09 | |||||
GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related GSTs. Ure2p is a regulator for nitrogen catabolism in yeast. It represses the expression of several gene products involved in the use of poor nitrogen sources when rich sources are available. A transmissible conformational change of Ure2p results in a prion called [Ure3], an inactive, self-propagating and infectious amyloid. Ure2p displays a GST fold containing 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 N-terminal TRX-fold domain is sufficient to induce the [Ure3] phenotype and is also called the prion domain of Ure2p. In addition to its role in nitrogen regulation, Ure2p confers protection to cells against heavy metal ion and oxidant toxicity, and shows glutathione (GSH) peroxidase activity. Characterized GSTs in this subfamily include Aspergillus fumigatus GSTs 1 and 2, and Schizosaccharomyces pombe GST-I. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of 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. Pssm-ID: 239346 [Multi-domain] Cd Length: 81 Bit Score: 53.32 E-value: 1.46e-09
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| GST_N_Phi | cd03053 | GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ... |
66-129 | 4.15e-09 | |||||
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: 51.88 E-value: 4.15e-09
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| GST_N_4 | cd03056 | GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ... |
69-122 | 1.36e-08 | |||||
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: 50.65 E-value: 1.36e-08
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| GST_N_SspA | cd03059 | GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ... |
65-130 | 1.95e-08 | |||||
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: 50.02 E-value: 1.95e-08
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| GST_N_GTT1_like | cd03046 | GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ... |
70-131 | 2.07e-08 | |||||
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: 50.19 E-value: 2.07e-08
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| GST_N_Tau | cd03058 | GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ... |
67-128 | 3.04e-07 | |||||
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: 46.89 E-value: 3.04e-07
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| GST_N_CLIC | cd03061 | GST_N family, Chloride Intracellular Channel (CLIC) subfamily; composed of CLIC1-5, p64, ... |
49-133 | 4.58e-07 | |||||
GST_N family, Chloride Intracellular Channel (CLIC) subfamily; composed of CLIC1-5, p64, parchorin and similar proteins. They are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division and apoptosis. They can exist in both water-soluble and membrane-bound states, and are found in various vesicles and membranes. Biochemical studies of the C. elegans homolog, EXC-4, show that the membrane localization domain is present in the N-terminal part of the protein. The structure of soluble human CLIC1 reveals that it is monomeric and it adopts a fold similar to GSTs, containing an N-terminal domain with a TRX fold and a C-terminal alpha helical domain. Upon oxidation, the N-terminal domain of CLIC1 undergoes a structural change to form a non-covalent dimer stabilized by the formation of an intramolecular disulfide bond between two cysteines that are far apart in the reduced form. The CLIC1 dimer bears no similarity to GST dimers. The redox-controlled structural rearrangement exposes a large hydrophobic surface, which is masked by dimerization in vitro. In vivo, this surface may represent the docking interface of CLIC1 in its membrane-bound state. The two cysteines in CLIC1 that form the disulfide bond in oxidizing conditions are essential for dimerization and chloride channel activity, however, in other subfamily members, the second cysteine is not conserved. Pssm-ID: 239359 Cd Length: 91 Bit Score: 46.60 E-value: 4.58e-07
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| GrxC | COG0695 | Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; |
58-127 | 5.00e-07 | |||||
Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440459 [Multi-domain] Cd Length: 74 Bit Score: 46.34 E-value: 5.00e-07
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| GST_N_4 | pfam17172 | Glutathione S-transferase N-terminal domain; This domain is homologous to pfam02798. |
67-142 | 1.78e-06 | |||||
Glutathione S-transferase N-terminal domain; This domain is homologous to pfam02798. Pssm-ID: 465370 [Multi-domain] Cd Length: 97 Bit Score: 45.26 E-value: 1.78e-06
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| PRK15113 | PRK15113 | glutathione transferase; |
67-134 | 4.53e-06 | |||||
glutathione transferase; Pssm-ID: 185068 [Multi-domain] Cd Length: 214 Bit Score: 46.11 E-value: 4.53e-06
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| NrdH | cd02976 | NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ... |
65-126 | 1.58e-05 | |||||
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active CXXC motif within a TRX fold, characterized by a glutaredoxin (GRX)-like sequence and TRX-like activity profile. In vitro, it displays protein disulfide reductase activity that is dependent on TRX reductase, not glutathione (GSH). It is part of the NrdHIEF operon, where NrdEF codes for class Ib ribonucleotide reductase (RNR-Ib), an efficient enzyme at low oxygen levels. Under these conditions when GSH is mostly conjugated to spermidine, NrdH can still function and act as a hydrogen donor for RNR-Ib. It has been suggested that the NrdHEF system may be the oldest RNR reducing system, capable of functioning in a microaerophilic environment, where GSH was not yet available. NrdH from Corynebacterium ammoniagenes can form domain-swapped dimers, although it is unknown if this happens in vivo. Domain-swapped dimerization, which results in the blocking of the TRX reductase binding site, could be a mechanism for regulating the oxidation state of the protein. Pssm-ID: 239274 [Multi-domain] Cd Length: 73 Bit Score: 41.83 E-value: 1.58e-05
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| GST_N_etherase_LigE | cd03038 | GST_N family, Beta etherase LigE subfamily; composed of proteins similar to Sphingomonas ... |
67-131 | 2.14e-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: 41.95 E-value: 2.14e-05
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| GST_N_Metaxin_like | cd03080 | GST_N family, Metaxin subfamily, Metaxin-like proteins; a heterogenous group of proteins, ... |
67-130 | 3.27e-05 | |||||
GST_N family, Metaxin subfamily, Metaxin-like proteins; a heterogenous group of proteins, predominantly uncharacterized, with similarity to metaxins and GSTs. Metaxin 1 is a component of a preprotein import complex of the mitochondrial outer membrane. It extends to the cytosol and is anchored to the mitochondrial membrane through its C-terminal domain. In mice, metaxin is required for embryonic development. In humans, alterations in the metaxin gene may be associated with Gaucher disease. One characterized member of this subgroup is a novel GST from Rhodococcus with toluene o-monooxygenase and gamma-glutamylcysteine synthetase activities. Also members are the cadmium-inducible lysosomal protein CDR-1 and its homologs from C. elegans, and the failed axon connections (fax) protein from Drosophila. CDR-1 is an integral membrane protein that functions to protect against cadmium toxicity and may also have a role in osmoregulation to maintain salt balance in C. elegans. The fax gene of Drosophila was identified as a genetic modifier of Abelson (Abl) tyrosine kinase. The fax protein is localized in cellular membranes and is expressed in embryonic mesoderm and axons of the central nervous system. Pssm-ID: 239378 [Multi-domain] Cd Length: 75 Bit Score: 41.07 E-value: 3.27e-05
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| GST_C_family | cd00299 | C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ... |
169-232 | 8.79e-05 | |||||
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: 40.56 E-value: 8.79e-05
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| GST_N_Metaxin | cd03054 | GST_N family, Metaxin subfamily; composed of metaxins and related proteins. Metaxin 1 is a ... |
66-129 | 8.93e-05 | |||||
GST_N family, Metaxin subfamily; composed of metaxins and related proteins. Metaxin 1 is a component of a preprotein import complex of the mitochondrial outer membrane. It extends to the cytosol and is anchored to the mitochondrial membrane through its C-terminal domain. In mice, metaxin is required for embryonic development. In humans, alterations in the metaxin gene may be associated with Gaucher disease. Metaxin 2 binds to metaxin 1 and may also play a role in protein translocation into the mitochondria. Genome sequencing shows that a third metaxin gene also exists in zebrafish, Xenopus, chicken and mammals. Sequence analysis suggests that all three metaxins share a common ancestry and that they possess similarity to GSTs. Also included in the subfamily are uncharacterized proteins with similarity to metaxins, including a novel GST from Rhodococcus with toluene o-monooxygenase and glutamylcysteine synthetase activities. Pssm-ID: 239352 [Multi-domain] Cd Length: 72 Bit Score: 39.90 E-value: 8.93e-05
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| GST_N_Omega_like | cd03060 | GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to ... |
66-127 | 1.61e-04 | |||||
GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to class Omega 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. 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. Like Omega enzymes, proteins in this subfamily 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. Pssm-ID: 239358 [Multi-domain] Cd Length: 71 Bit Score: 39.26 E-value: 1.61e-04
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| GST_N | pfam02798 | Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ... |
65-128 | 1.94e-04 | |||||
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: 38.83 E-value: 1.94e-04
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| GRX_family | cd02066 | Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ... |
64-127 | 7.38e-04 | |||||
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, as well as E. coli GRX1 and GRX3, which are members of this family. E. coli GRX2, however, is a 24-kDa protein that belongs to the GSH S-transferase (GST) family. Pssm-ID: 239017 [Multi-domain] Cd Length: 72 Bit Score: 37.06 E-value: 7.38e-04
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| GST_C_SspA | cd03186 | C-terminal, alpha helical domain of Stringent starvation protein A; Glutathione S-transferase ... |
169-238 | 1.05e-03 | |||||
C-terminal, alpha helical domain of Stringent starvation protein A; Glutathione S-transferase (GST) C-terminal domain 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 thioredoxin-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: 198295 [Multi-domain] Cd Length: 108 Bit Score: 37.64 E-value: 1.05e-03
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| GST_C_3 | pfam14497 | Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043. |
173-236 | 1.27e-03 | |||||
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043. Pssm-ID: 464190 [Multi-domain] Cd Length: 104 Bit Score: 37.54 E-value: 1.27e-03
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| Glutaredoxin | pfam00462 | Glutaredoxin; |
66-116 | 1.56e-03 | |||||
Glutaredoxin; Pssm-ID: 425695 [Multi-domain] Cd Length: 60 Bit Score: 35.94 E-value: 1.56e-03
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| GST_N_mPGES2 | cd03040 | GST_N family; microsomal Prostaglandin E synthase Type 2 (mPGES2) subfamily; mPGES2 is a ... |
66-129 | 2.34e-03 | |||||
GST_N family; microsomal Prostaglandin E synthase Type 2 (mPGES2) subfamily; mPGES2 is a membrane-anchored dimeric protein containing a CXXC motif which catalyzes the isomerization of PGH2 to PGE2. Unlike cytosolic PGE synthase (cPGES) and microsomal PGES Type 1 (mPGES1), mPGES2 does not require glutathione (GSH) for its activity, although its catalytic rate is increased two- to four-fold in the presence of DTT, GSH or other thiol compounds. PGE2 is widely distributed in various tissues and is implicated in the sleep/wake cycle, relaxation/contraction of smooth muscle, excretion of sodium ions, maintenance of body temperature and mediation of inflammation. mPGES2 contains an N-terminal hydrophobic domain which is membrane associated, and a C-terminal soluble domain with a GST-like structure. Pssm-ID: 239338 Cd Length: 77 Bit Score: 35.85 E-value: 2.34e-03
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| GST_N_Beta | cd03057 | GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ... |
76-131 | 3.86e-03 | |||||
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: 35.21 E-value: 3.86e-03
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| GST_N_Delta_Epsilon | cd03045 | GST_N family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved ... |
67-122 | 4.50e-03 | |||||
GST_N 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. 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: 239343 [Multi-domain] Cd Length: 74 Bit Score: 34.89 E-value: 4.50e-03
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| GST_C_2 | pfam13410 | Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043. |
173-230 | 5.89e-03 | |||||
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043. Pssm-ID: 433185 [Multi-domain] Cd Length: 67 Bit Score: 34.60 E-value: 5.89e-03
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| GST_N_GDAP1 | cd03052 | GST_N family, Ganglioside-induced differentiation-associated protein 1 (GDAP1) subfamily; ... |
70-127 | 9.32e-03 | |||||
GST_N family, Ganglioside-induced differentiation-associated protein 1 (GDAP1) subfamily; GDAP1 was originally identified as a highly expressed gene at the differentiated stage of GD3 synthase-transfected cells. More recently, mutations in GDAP1 have been reported to cause both axonal and demyelinating autosomal-recessive Charcot-Marie-Tooth (CMT) type 4A neuropathy. CMT is characterized by slow and progressive weakness and atrophy of muscles. Sequence analysis of GDAP1 shows similarities and differences with GSTs; it appears to contain both N-terminal TRX-fold and C-terminal alpha helical domains of GSTs, however, it also contains additional C-terminal transmembrane domains unlike GSTs. GDAP1 is mainly expressed in neuronal cells and is localized in the mitochondria through its transmembrane domains. It does not exhibit GST activity using standard substrates. Pssm-ID: 239350 [Multi-domain] Cd Length: 73 Bit Score: 34.06 E-value: 9.32e-03
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