MULTISPECIES: glutathione S-transferase family protein [Lactobacillaceae]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| PRK10542 super family | cl32531 | glutathionine S-transferase; Provisional |
2-201 | 8.35e-49 | ||||
glutathionine S-transferase; Provisional The actual alignment was detected with superfamily member PRK10542: Pssm-ID: 182533 [Multi-domain] Cd Length: 201 Bit Score: 157.92 E-value: 8.35e-49
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| Name | Accession | Description | Interval | E-value | ||||
| PRK10542 | PRK10542 | glutathionine S-transferase; Provisional |
2-201 | 8.35e-49 | ||||
glutathionine S-transferase; Provisional Pssm-ID: 182533 [Multi-domain] Cd Length: 201 Bit Score: 157.92 E-value: 8.35e-49
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| GstA | COG0625 | Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; |
1-201 | 6.76e-35 | ||||
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440390 [Multi-domain] Cd Length: 205 Bit Score: 122.31 E-value: 6.76e-35
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| GST_C_Beta | cd03188 | C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ... |
96-197 | 2.15e-31 | ||||
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: 110.41 E-value: 2.15e-31
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| GST_N | pfam02798 | Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ... |
2-74 | 1.99e-06 | ||||
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: 44.22 E-value: 1.99e-06
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| Name | Accession | Description | Interval | E-value | ||||
| PRK10542 | PRK10542 | glutathionine S-transferase; Provisional |
2-201 | 8.35e-49 | ||||
glutathionine S-transferase; Provisional Pssm-ID: 182533 [Multi-domain] Cd Length: 201 Bit Score: 157.92 E-value: 8.35e-49
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| GstA | COG0625 | Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; |
1-201 | 6.76e-35 | ||||
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440390 [Multi-domain] Cd Length: 205 Bit Score: 122.31 E-value: 6.76e-35
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| GST_C_Beta | cd03188 | C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ... |
96-197 | 2.15e-31 | ||||
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: 110.41 E-value: 2.15e-31
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| GST_N_Beta | cd03057 | GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ... |
2-73 | 8.74e-23 | ||||
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: 87.21 E-value: 8.74e-23
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| GST_N_family | cd00570 | Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ... |
2-74 | 2.83e-09 | ||||
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: 51.80 E-value: 2.83e-09
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| GST_N | pfam02798 | Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ... |
2-74 | 1.99e-06 | ||||
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: 44.22 E-value: 1.99e-06
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| PRK15113 | PRK15113 | glutathione transferase; |
12-203 | 2.18e-05 | ||||
glutathione transferase; Pssm-ID: 185068 [Multi-domain] Cd Length: 214 Bit Score: 43.79 E-value: 2.18e-05
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| GST_N_2 | pfam13409 | Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798. |
16-74 | 3.25e-05 | ||||
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798. Pssm-ID: 433184 [Multi-domain] Cd Length: 68 Bit Score: 40.69 E-value: 3.25e-05
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| GST_N_Zeta | cd03042 | GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ... |
23-74 | 7.17e-04 | ||||
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: 36.78 E-value: 7.17e-04
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| GST_C_8 | cd03207 | C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; ... |
96-192 | 1.08e-03 | ||||
C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 8; composed of Agrobacterium tumefaciens GST and other 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 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 three-dimensional structure of Agrobacterium tumefaciens GST has been determined but there is no information on its functional characterization. Pssm-ID: 198316 [Multi-domain] Cd Length: 101 Bit Score: 37.27 E-value: 1.08e-03
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| GST_C_GTT2_like | cd03182 | C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione ... |
130-193 | 1.36e-03 | ||||
C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly uncharacterized proteins with similarity to the Saccharomyces cerevisiae GST protein, GTT2. 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. GTT2, a homodimer, exhibits GST activity with standard substrates. Strains with deleted GTT2 genes are viable but exhibit increased sensitivity to heat shock. Pssm-ID: 198291 [Multi-domain] Cd Length: 116 Bit Score: 37.30 E-value: 1.36e-03
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| GST_N_GTT2_like | cd03051 | GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ... |
2-74 | 1.98e-03 | ||||
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly uncharacterized proteins with similarity to the S. cerevisiae GST protein, GTT2. 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. GTT2, a homodimer, exhibits GST activity with standard substrates. Strains with deleted GTT2 genes are viable but exhibit increased sensitivity to heat shock. Pssm-ID: 239349 [Multi-domain] Cd Length: 74 Bit Score: 35.74 E-value: 1.98e-03
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| GST_N_GTT1_like | cd03046 | GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ... |
2-73 | 2.92e-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: 35.17 E-value: 2.92e-03
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| GST_C_GDAP1_like | cd03204 | C-terminal, alpha helical domain of Ganglioside-induced differentiation-associated protein ... |
144-193 | 4.14e-03 | ||||
C-terminal, alpha helical domain of Ganglioside-induced differentiation-associated protein 1-like proteins; Glutathione S-transferase (GST) C-terminal domain family, Ganglioside-induced differentiation-associated protein 1 (GDAP1)-like 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 thioredoxin-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: 198313 Cd Length: 111 Bit Score: 35.89 E-value: 4.14e-03
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| GST_N_SspA | cd03059 | GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ... |
8-74 | 7.25e-03 | ||||
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: 34.23 E-value: 7.25e-03
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| Blast search parameters | ||||
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