C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218311  89 PYGRAQARFWADFVDKKFTDAQFKVWGKKGEEQEAGKKEFIEAVKILESELGD-KPYFGGDSFGYVDISLITFSSWFQAY 167
Cdd:cd03185   1 PYERAQARFWAAYIDDKLFPAGRKVWAAKGEEQEKAVEEALEALKVLEEELKGgKPFFGGDTIGYLDIALGSFLGWFKAI 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15218311 168 EKFGNFSI--ESESPKLIAWAKRCMEKESVSKSLPDSEKIVAYA 209
Cdd:cd03185  81 EEVGGVKLldEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFL 124

C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218311  89 PYGRAQARFWADFVDKKFTDAQFKVWGKKGEEQEAGKKEFIEAVKILESELGD-KPYFGGDSFGYVDISLITFSSWFQAY 167
Cdd:cd03185   1 PYERAQARFWAAYIDDKLFPAGRKVWAAKGEEQEKAVEEALEALKVLEEELKGgKPFFGGDTIGYLDIALGSFLGWFKAI 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15218311 168 EKFGNFSI--ESESPKLIAWAKRCMEKESVSKSLPDSEKIVAYA 209
Cdd:cd03185  81 EEVGGVKLldEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFL 124

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218311   6 ILLDYWPSMFGMRARVALREKGVEFEYREEDF---SNKSPLLLQSNPIHKkIPVLVHNGKPVCESLNVVQYVDEAWPEKn 82
Cdd:COG0625   3 KLYGSPPSPNSRRVRIALEEKGLPYELVPVDLakgEQKSPEFLALNPLGK-VPVLVDDGLVLTESLAILEYLAERYPEP- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218311  83 PFFPSDPYGRAQARFWADFVDKKFTDAQFKVWGKKGEEQ-----EAGKKEFIEAVKILESELGDKPYFGGDSFGYVDISL 157
Cdd:COG0625  81 PLLPADPAARARVRQWLAWADGDLHPALRNLLERLAPEKdpaaiARARAELARLLAVLEARLAGGPYLAGDRFSIADIAL 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15218311 158 ITFSSWFQAYEkfgnFSIEsESPKLIAWAKRCMEKESVSKSLPDSEKIVA 207
Cdd:COG0625 161 APVLRRLDRLG----LDLA-DYPNLAAWLARLAARPAFQRALAAAEPDLA 205

stringent starvation protein A; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218311   14 MFGMRARVALREKGVEFEYREEDFSNKSPLLLQSNPiHKKIPVLVHNGKPVCESLNVVQYVDEAWPEKnPFFPSDPYGRA 93
Cdd:PRK09481  20 IYSHQVRIVLAEKGVSVEIEQVEKDNLPQDLIDLNP-YQSVPTLVDRELTLYESRIIMEYLDERFPHP-PLMPVYPVARG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218311   94 QARFWADFVDKKFTDAQFKVWGKKGEEQEAGKKEFIEAVKILESELGDKPYFGGDSFGYVDISLITFsSWfqayeKFGNF 173
Cdd:PRK09481  98 ESRLMMHRIEKDWYSLMNKIVNGSASEADAARKQLREELLAIAPVFGEKPYFMSEEFSLVDCYLAPL-LW-----RLPVL 171

                        170       180       190
                 ....*....|....*....|....*....|....
gi 15218311  174 SIESESP---KLIAWAKRCMEKESVSKSLPDSEK 204
Cdd:PRK09481 172 GIELSGPgakELKGYMTRVFERDSFLASLTEAER 205

glutathione transferase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218311    1 MANLPILL---DYWPSMFGMRARVALREKGVEFEYREEDFSNKSPLL--LQSNPIHKKIPVLVHNGKPVCESLNVVQYVD 75
Cdd:PRK15113   1 MSKPAITLysdAHFFSPYVMSAFVALQEKGLPFELKTVDLDAGEHLQptYQGYSLTRRVPTLQHDDFELSESSAIAEYLE 80

                         90       100
                 ....*....|....*....|...
gi 15218311   76 EAW--PEKNPFFPSDPYGRAQAR 96
Cdd:PRK15113  81 ERFapPAWERIYPADLQARARAR 103

C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218311  89 PYGRAQARFWADFVDKKFTDAQFKVWGKKGEEQEAGKKEFIEAVKILESELGD-KPYFGGDSFGYVDISLITFSSWFQAY 167
Cdd:cd03185   1 PYERAQARFWAAYIDDKLFPAGRKVWAAKGEEQEKAVEEALEALKVLEEELKGgKPFFGGDTIGYLDIALGSFLGWFKAI 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15218311 168 EKFGNFSI--ESESPKLIAWAKRCMEKESVSKSLPDSEKIVAYA 209
Cdd:cd03185  81 EEVGGVKLldEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFL 124

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218311   6 ILLDYWPSMFGMRARVALREKGVEFEYREEDF---SNKSPLLLQSNPIHKkIPVLVHNGKPVCESLNVVQYVDEAWPEKn 82
Cdd:COG0625   3 KLYGSPPSPNSRRVRIALEEKGLPYELVPVDLakgEQKSPEFLALNPLGK-VPVLVDDGLVLTESLAILEYLAERYPEP- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218311  83 PFFPSDPYGRAQARFWADFVDKKFTDAQFKVWGKKGEEQ-----EAGKKEFIEAVKILESELGDKPYFGGDSFGYVDISL 157
Cdd:COG0625  81 PLLPADPAARARVRQWLAWADGDLHPALRNLLERLAPEKdpaaiARARAELARLLAVLEARLAGGPYLAGDRFSIADIAL 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15218311 158 ITFSSWFQAYEkfgnFSIEsESPKLIAWAKRCMEKESVSKSLPDSEKIVA 207
Cdd:COG0625 161 APVLRRLDRLG----LDLA-DYPNLAAWLARLAARPAFQRALAAAEPDLA 205

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.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218311   5 PILLDYWPSMFGMRARVALREKGVEFEYREEDFSNKSPLLLQSNPIHKKIPVLVHNGKPVCESLNVVQYVD 75
Cdd:cd00570   1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQEEFLALNPLGKVPVLEDGGLVLTESLAILEYLA 71

Glutathione S-transferase, N-terminal domain;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15218311    13 SMFGMRARVALREKGVEFEYREEDFSNKSPLLLQSNPiHKKIPVLVHNGKPVCESLNVVQYVDEAWPEK 81
Cdd:pfam13417   7 SPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNP-LGKVPVLEDDGGILCESLAIIDYLEELYPGP 74

Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218311    15 FGMRARVALREKGVEFEYREEDF--SNKSPLLLQSNPIHkKIPVLV-HNGKPVCESLNVVQYVDEA 77
Cdd:pfam13409   4 FSHRVRLALEEKGLPYEIELVDLdpKDKPPELLALNPLG-TVPVLVlPDGTVLTDSLVILEYLEEL 68

Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15218311   122 EAGKKEFIEAVKILESELGDKPYFGGDSFGYVDISLITFSSWFQAYekFGNFSIESESPKLIAWAKR 188
Cdd:pfam13410   3 ERAREQLRAALDALEARLADGPGLLGDRPTLADIALAPVLARLDAA--YPGLDLREGYPRLRAWLER 67

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.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218311   5 PILLDYWPSMFGMRARVALREKGVEFEYREEDFSNKSPLLLQSNPiHKKIPVLV-HNGKPVCESLNVVQY 73
Cdd:cd03060   1 PILYSFRRCPYAMRARMALLLAGITVELREVELKNKPAEMLAASP-KGTVPVLVlGNGTVIEESLDIMRW 69

Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety of targets including S-crystallin from squid, the eukaryotic elongation factor 1-gamma, the HSP26 family of stress-related proteins and auxin-regulated proteins in plants. Stringent starvation proteins in E. coli are also included in the alignment but are not known to have GST activity. The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed to reside in the N-terminal domain. In plants, GSTs are encoded by a large gene family (48 GST genes in Arabidopsis) and can be divided into the phi, tau, theta, zeta, and lambda classes.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15218311   116 KKGEEQEAGKKEFIEAVKILESELGDKPYFGGDSFGYVDISLITFSSWFQAYEkfGNFSIEsESPKLIAWAKRCMEKE 193
Cdd:pfam00043  19 KKEPEVDEALEKVARVLSALEEVLKGQTYLVGDKLTLADIALAPALLWLYELD--PACLRE-KFPNLKAWFERVAARP 93

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218311  88 DPYGRAQARFWADFVDKKFTDAQFKVW-----GKKGEEQ-------EAGKKEFIEAVKILESELGDKPYFGGDSFGYVDI 155
Cdd:cd03182   1 TPLEKALIEMWQRRAELQGLAPVFQAFrhatpGLKPDREvqvpewgERNKKRVIDFLPVLDKRLAESPYVAGDRFSIADI 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15218311 156 SLITFSSwfqaYEKFGNFSIESESPKLIAWAKRCMEKESV 195
Cdd:cd03182  81 TAFVALD----FAKNLKLPVPEELTALRRWYERMAARPSA 116

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
                ....*....|....*....|....*....|....*....|....*....|...
gi 15218311  18 RARVALREKGVEFEYREEDFSN---KSPLLLQSNPiHKKIPVLVHNGKPVCES 67
Cdd:cd03056  14 KVRLLLALLGIPYEWVEVDILKgetRTPEFLALNP-NGEVPVLELDGRVLAES 65

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.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15218311  18 RARVALREKGVEFEYREEDFSNKSPlLLQSNPIH--KKIPVLVH-NGKPVCESLNVVQYVDEAWP 79
Cdd:cd03038  21 KTRLALNHKGLEYKTVPVEFPDIPP-ILGELTSGgfYTVPVIVDgSGEVIGDSFAIAEYLEEAYP 84

C-terminal, alpha helical domain of Ure2p and related Glutathione S-transferase-like proteins; Glutathione S-transferase (GST) C-terminal domain family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p, YfcG and YghU from Escherichia coli, and related GST-like proteins. 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 thioredoxin-fold domain and a C-terminal alpha helical domain. The N-terminal thioredoxin-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. YfcG and YghU are two of the nine GST homologs in the genome of Escherichia coli. They display very low or no GSH transferase, but show very good disulfide bond oxidoreductase activity. YghU also shows modest organic hydroperoxide reductase activity. 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. The GST active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15218311 130 EAVKILESELGDKPYFGGDSFGYVDISLITFSswfqAYEKFGNFSIESESPKLIAWAKRCMEKESVSK 197
Cdd:cd03178  47 RLYGVLDKRLSDRPYLAGEEYSIADIALYPWT----HYADLGGFADLSEYPNVKRWLERIAARPAVQK 110

C-terminal, alpha helical domain of Class Lambda Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Lambda subfamily; composed of plant-specific class Lambda GSTs. GSTs are cytosolic, usually dimeric, proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The class Lambda subfamily was recently discovered, together with dehydroascorbate reductases (DHARs), as two outlying groups of the GST superfamily in Arabidopsis thaliana, which contain conserved active site cysteines. Characterization of recombinant A. thaliana proteins show that Lambda class GSTs are monomeric, similar to DHARs. They do not exhibit GSH conjugating or DHAR activities, but are active as thiol transferases, similar to glutaredoxins. Members of this subfamily were originally identified as encoded proteins of the In2-1 gene, which can be induced by treatment with herbicide safeners.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218311 106 FTDAQFKVWGKKGEEQEAGKkefieAVKILESELG---DKPYFGGDsFGYVDISLITFSSWFQ-AYEKFGNFSIESESPK 181
Cdd:cd03203  18 FTKAVYSALIKGDMTAEAAA-----AFDYLENALSkfdDGPFFLGQ-FSLVDIAYAPFIERFQiVLSELRNYDITAGRPN 91

                        90       100
                ....*....|....*....|....*...
gi 15218311 182 LIAWAKRCMEKESVSKSLPDSEKIVAYA 209
Cdd:cd03203  92 LAKWIEEMNKIEAYTQTKVDPEELLELY 119

C-terminal, alpha helical domain of Class Theta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial dichloromethane (DCM) dehalogenase. 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. Mammalian class Theta GSTs show poor GSH conjugating activity towards the standard substrates, CDNB and ethacrynic acid, differentiating them from other mammalian GSTs. GSTT1-1 shows similar cataytic activity as bacterial DCM dehalogenase, catalyzing the GSH-dependent hydrolytic dehalogenation of dihalomethanes. This is an essential process in methylotrophic bacteria to enable them to use chloromethane and DCM as sole carbon and energy sources. The presence of polymorphisms in human GSTT1-1 and its relationship to the onset of diseases including cancer is the subject of many studies. Human GSTT2-2 exhibits a highly specific sulfatase activity, catalyzing the cleavage of sulfate ions from aralkyl sufate esters, but not from the aryl or alkyl sulfate esters.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15218311 119 EEQEAGKKEFIEAVKILESE-LGDKPYFGGDSFGYVDISLITfsswfqayE----KFGNFSIESESPKLIAWAKRCME 191
Cdd:cd03183  41 EKVKKAEENLEESLDLLENKfLKDKPFLAGDEISIADLSAIC--------EimqpEAAGYDVFEGRPKLAAWRKRVKE 110

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218311 134 ILESELGDKPYFGGDSFGYVDISLITFSSWFQAYEKFgnfsiESESPKLIAWAKRCMEKESVSKSL 199
Cdd:cd03188  53 YLDAQLAGGPYLLGDQFSVADAYLFVVLRWARAVGLD-----LSDWPHLAAYLARVAARPAVQAAL 113

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.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218311  15 FGMRARVALREKGVEFEYREEDFSNKSPLLLQSNPIhKKIPVLVHN-GKPVCESLNVVQYVD 75
Cdd:cd03055  29 YAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPQ-GKVPALEIDeGKVVYESLIICEYLD 89

C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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 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        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218311 104 KKFTDAQFKVWGKKGEEQEAGKKEFIEAVKILESELGDKPYFGGDSFGYVDISLI-TFSS--WFQA-YEKFgnfsieses 179
Cdd:cd03177  19 QRLRDYYYPILFGGAEPPEEKLDKLEEALEFLETFLEGSDYVAGDQLTIADLSLVaTVSTleVVGFdLSKY--------- 89

                        90       100       110
                ....*....|....*....|....*....|....
gi 15218311 180 PKLIAWAKRCmekesvSKSLPDSEKIVAYAAEYR 213
Cdd:cd03177  90 PNVAAWYERL------KALPPGEEENGEGAKELK 117