Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732235   6 VFYTNPMSRGRIARWMLEEIGQPYRTELLTFGE-TMKAPEYLAVNPMGKVPAIRHGDTIVTECAAICAYLAETFPEKTLA 84
Cdd:COG0625    4 LYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKgEQKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPEPPLL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732235  85 PR-PEERARYYRWMFFAAGPLESAVTMKALGFE-IPQERLRMAGCGGFGDVMNTLEKAVSGSTYVTGERFTAADVYVGSH 162
Cdd:COG0625   84 PAdPAARARVRQWLAWADGDLHPALRNLLERLApEKDPAAIARARAELARLLAVLEARLAGGPYLAGDRFSIADIALAPV 163

                        170       180       190
                 ....*....|....*....|....*....|...
gi 516732235 163 IGWGLGFG-SIEKRQAFVDYFGRISEREAYKRA 194
Cdd:COG0625  164 LRRLDRLGlDLADYPNLAAWLARLAARPAFQRA 196

Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732235   6 VFYTNPMSRGRIARWMLEEIGQPYRTELLTFGE-TMKAPEYLAVNPMGKVPAIRHGDTIVTECAAICAYLAETFPEKTLA 84
Cdd:COG0625    4 LYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKgEQKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPEPPLL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732235  85 PR-PEERARYYRWMFFAAGPLESAVTMKALGFE-IPQERLRMAGCGGFGDVMNTLEKAVSGSTYVTGERFTAADVYVGSH 162
Cdd:COG0625   84 PAdPAARARVRQWLAWADGDLHPALRNLLERLApEKDPAAIARARAELARLLAVLEARLAGGPYLAGDRFSIADIALAPV 163

                        170       180       190
                 ....*....|....*....|....*....|...
gi 516732235 163 IGWGLGFG-SIEKRQAFVDYFGRISEREAYKRA 194
Cdd:COG0625  164 LRRLDRLGlDLADYPNLAAWLARLAARPAFQRA 196

glutathionine S-transferase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732235  44 EYLAVNPMGKVPAIRHGD-TIVTECAAICAYLAETFPEKTLAPRPEERARYY--RWMFFAAGPLESavtmkalGF----- 115
Cdd:PRK10542  42 DYLAINPKGQVPALLLDDgTLLTEGVAIMQYLADSVPDRQLLAPVGSLSRYHtiEWLNYIATELHK-------GFtplfr 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732235 116 -EIPQERLRMagcggfgdVMNTLEK-------AVSGSTYVTGERFTAADVYVGSHIGWGLGFG-SIEKRQAFVDYFGRIS 186
Cdd:PRK10542 115 pDTPEEYKPT--------VRAQLEKkfqyvdeALADEQWICGQRFTIADAYLFTVLRWAYAVKlNLEGLEHIAAYMQRVA 186

                 ....*...
gi 516732235 187 EREAYKRA 194
Cdd:PRK10542 187 ERPAVAAA 194

Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732235   6 VFYTNPMSRGRIARWMLEEIGQPYRTELLTFGE-TMKAPEYLAVNPMGKVPAIRHGDTIVTECAAICAYLAETFPEKTLA 84
Cdd:COG0625    4 LYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKgEQKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPEPPLL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732235  85 PR-PEERARYYRWMFFAAGPLESAVTMKALGFE-IPQERLRMAGCGGFGDVMNTLEKAVSGSTYVTGERFTAADVYVGSH 162
Cdd:COG0625   84 PAdPAARARVRQWLAWADGDLHPALRNLLERLApEKDPAAIARARAELARLLAVLEARLAGGPYLAGDRFSIADIALAPV 163

                        170       180       190
                 ....*....|....*....|....*....|...
gi 516732235 163 IGWGLGFG-SIEKRQAFVDYFGRISEREAYKRA 194
Cdd:COG0625  164 LRRLDRLGlDLADYPNLAAWLARLAARPAFQRA 196

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732235  93 YYRWMFFAAGPLESAVTMKALGFEI---PQERLRMAGCGGFGDVMNTLEKAVSGSTYVTGERFTAADVYVGSHIGWGLGF 169
Cdd:cd03207    1 YLRWLFFAAGTVEPPLLNKALGRFFeppWGEPAIAAAYGDLDERLAALEAALAGRPYLVGERFSAADLLLASVLRWARAF 80

                         90       100
                 ....*....|....*....|.
gi 516732235 170 GSIEKRQAFVDYFGRISEREA 190
Cdd:cd03207   81 GLLPEYPALRAYVARCTARPA 101

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516732235   7 FYTNPMSRGRIARWMLEEIGQPYRTELLTFG-ETMKAPEYLAVNPMGKVPAIRHGD-TIVTECAAICAYLAETFP 79
Cdd:cd03057    3 LYYSPGACSLAPHIALEELGLPFELVRVDLRtKTQKGADYLAINPKGQVPALVLDDgEVLTESAAILQYLADLHP 77

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516732235   5 LVFYTNPMSRGRIARWMLEEIGQPYRTELLTFGET-MKAPEYLAVNPMGKVPAIR---HGDTIVTECAAICAYLAETFP 79
Cdd:cd03048    2 ITLYTHGTPNGFKVSIMLEELGLPYEIHPVDISKGeQKKPEFLKINPNGRIPAIVdhnGTPLTVFESGAILLYLAEKYD 80

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732235  18 ARWMLEEIGQPYRTELLTF--GETmKAPEYLAVNPMGKVPAIRHGDTIVTECAAICAYLA 75
Cdd:cd03056   15 VRLLLALLGIPYEWVEVDIlkGET-RTPEFLALNPNGEVPVLELDGRVLAESNAILVYLA 73

GST_N family, unknown subfamily 2; 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. The sequence from Burkholderia cepacia was identified as part of a gene cluster involved in the degradation of 2,4,5-trichlorophenoxyacetic acid. Some GSTs (e.g. Class Zeta and Delta) are known to catalyze dechlorination reactions.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 516732235  20 WMLEEIGQPYRTEL--LTFGETmKAPEYLAVNPMGKVPAIRHGDTIVTECAAICAYLA 75
Cdd:cd03047   17 WLLDELGLPYERIDagGQFGGL-DTPEFLAMNPNGRVPVLEDGDFVLWESNAILRYLA 73

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516732235  16 RIARWMLEEIGQPYrtEL----LTFGETmKAPEYLAVNPMGKVPAIRHGDTIVTECAAICAYLAE 76
Cdd:cd03053   14 RRVLLCLEEKGVDY--ELvpvdLTKGEH-KSPEHLARNPFGQIPALEDGDLKLFESRAITRYLAE 75

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516732235    3 EELVFYTNPMS-RGRIARWMLEEIGQPYRTELLTFGET-MKAPEYLAVNPMGKVPAIRHGDTIVTECAAICAYLAE 76
Cdd:pfam02798   1 MVLTLYGIRGSpRAHRIRWLLAEKGVEYEIVPLDFGAGpEKSPELLKLNPLGKVPALEDGGKKLTESRAILEYIAR 76

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732235  89 ERARYYRWMFFAAGPLESAVTMK----ALGFEIPQERLRMAGCGGFGDVMNTLEKAVSGSTYVTGERFTAADVYVGSHIG 164
Cdd:cd03188    2 ERARLLEWLNFIASELHKAFGPLfypaRWADDALAEEVKAAARERLERRLAYLDAQLAGGPYLLGDQFSVADAYLFVVLR 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 516732235 165 WGLGFG-SIEKRQAFVDYFGRISEREAYKRA 194
Cdd:cd03188   82 WARAVGlDLSDWPHLAAYLARVAARPAVQAA 112

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516732235   5 LVFYTNPMSR-GRIARWMLEEIGQPYRTELLTF--GETMKaPEYLAVNPMGKVPAIRHGDTIVTECAAICAYLAE 76
Cdd:cd03045    1 IDLYYLPGSPpCRAVLLTAKALGLELNLKEVNLmkGEHLK-PEFLKLNPQHTVPTLVDNGFVLWESHAILIYLVE 74

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.

                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 516732235  37 GETMKaPEYLAVNPMGKVPAIRHGD-TIVTECAAICAYL 74
Cdd:cd03051   36 GEQRS-PEFLAKNPAGTVPVLELDDgTVITESVAICRYL 73

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.

                         10        20        30
                 ....*....|....*....|....*....|....
gi 516732235  41 KAPEYLAVNPMGKVPAIRHGDTIVTECAAICAYL 74
Cdd:cd03042   39 LSPAYRALNPQGLVPTLVIDGLVLTQSLAIIEYL 72

GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. The EF1B gamma subunit contains a GST fold consisting of an N-terminal TRX-fold domain and a C-terminal alpha helical domain. The GST-like domain of EF1Bgamma is believed to mediate the dimerization of the EF1 complex, which in yeast is a dimer of the heterotrimer EF1A:EF1Balpha:EF1Bgamma. In addition to its role in protein biosynthesis, EF1Bgamma may also display other functions. The recombinant rice protein has been shown to possess GSH conjugating activity. The yeast EF1Bgamma binds membranes in a calcium dependent manner and is also part of a complex that binds to the msrA (methionine sulfoxide reductase) promoter suggesting a function in the regulation of its gene expression.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 516732235  35 TFGETMKAPEYLAVNPMGKVPAIRHGD-TIVTECAAICAYLAET 77
Cdd:cd03044   32 QPGKENKTPEFLKKFPLGKVPAFEGADgFCLFESNAIAYYVANL 75

glutathione dehydrogenase (ascorbate)

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516732235  22 LEEIGQPYRTELLTFGetmKAPE-YLAVNPMGKVPAIRHGDTIVTECAAICAYLAETFPEKTLAPRPEE 89
Cdd:PLN02817  83 LEEKHLPYDMKLVDLT---NKPEwFLKISPEGKVPVVKLDEKWVADSDVITQALEEKYPDPPLATPPEK 148

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732235  95 RWMFFAAGPLESAVTMKALGFEIPQERLRMAGCGG---FGDVMNTLEKAVSGSTYVTGERFTAADVYVGSHIGW----GL 167
Cdd:cd00299    3 ALEDWADATLAPPLVRLLYLEKVPLPKDEAAVEAAreeLPALLAALEQLLAGRPYLAGDQFSLADVALAPVLARlealGP 82

                         90
                 ....*....|....*...
gi 516732235 168 GFGSIEKRQAFVDYFGRI 185
Cdd:cd00299   83 YYDLLDEYPRLKAWYDRL 100

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516732235  18 ARWMLEEIGQPYrtELLTFGETMKAPEYLAVNPM-GKVPAIRHGDTIVTECAAICAYLAETF 78
Cdd:cd03058   15 VRIALALKGVPY--EYVEEDLGNKSELLLASNPVhKKIPVLLHNGKPICESLIIVEYIDEAW 74

C-terminal, alpha helical domain of GTT1-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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. 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732235  85 PRPEERARYYRWMFFAAGPLESAVTMK-ALGFEIPQERLRMAGCGGFGD--------------VMNTLEKAVSGSTYVTG 149
Cdd:cd03189    3 PDTAEYADYLYWLHFAEGSLMPPLLLKlVFGKIGEAPPPFFRPISRKIAdkplqafinpelkrHLDFLEDHLAKHPYFAG 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 516732235 150 ERFTAADVyvgsHIGWGL-----GFGSIEKRQAFVDYFGRISERE 189
Cdd:cd03189   83 DELTAADI----MMSFPLeaalaRGPLLEQYPNIAAYLERIEARP 123