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        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220905   8 VVVLDFWASPYAMRTKVALREKGVEFEVQEEDLWNKSELLLKSNPVHKKVPVLIHNNTPISESLIQVQYIDETW 81
Cdd:cd03058   1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 74

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        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220905   8 VVVLDFWASPYAMRTKVALREKGVEFEVQEEDLWNKSELLLKSNPVHKKVPVLIHNNTPISESLIQVQYIDETW 81
Cdd:cd03058   1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 74

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 15220905     6 SKVVVLDFWASPYAMRTKVALREKGVEFEVQEEDLW---NKSELLLKSNPVhKKVPVLIHNNTPISESLIQVQYIDE 79
Cdd:pfam02798   1 MVLTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGagpEKSPELLKLNPL-GKVPALEDGGKKLTESRAILEYIAR 76

glutathione transferase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220905   14 WASPYAMRTKVALREKGVEFEVQEEDL---------WNKSELLlksnpvhKKVPVLIHNNTPISESLIQVQYIDETW--T 82
Cdd:PRK15113  14 FFSPYVMSAFVALQEKGLPFELKTVDLdagehlqptYQGYSLT-------RRVPTLQHDDFELSESSAIAEYLEERFapP 86

                         90
                 ....*....|....*..
gi 15220905   83 DAASFLPSDPQSRATAR 99
Cdd:PRK15113  87 AWERIYPADLQARARAR 103

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        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220905   8 VVVLDFWASPYAMRTKVALREKGVEFEVQEEDLWNKSELLLKSNPVHKKVPVLIHNNTPISESLIQVQYIDETW 81
Cdd:cd03058   1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 74

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220905  13 FWASPYAMRTKVALREKGVEFEVQEEDLWNKSELLLKSNPVHKKVPVLIHNNTPISESLIQVQYID 78
Cdd:cd00570   6 FPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQEEFLALNPLGKVPVLEDGGLVLTESLAILEYLA 71

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 15220905     6 SKVVVLDFWASPYAMRTKVALREKGVEFEVQEEDLW---NKSELLLKSNPVhKKVPVLIHNNTPISESLIQVQYIDE 79
Cdd:pfam02798   1 MVLTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGagpEKSPELLKLNPL-GKVPALEDGGKKLTESRAILEYIAR 76

glutathione transferase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220905   14 WASPYAMRTKVALREKGVEFEVQEEDL---------WNKSELLlksnpvhKKVPVLIHNNTPISESLIQVQYIDETW--T 82
Cdd:PRK15113  14 FFSPYVMSAFVALQEKGLPFELKTVDLdagehlqptYQGYSLT-------RRVPTLQHDDFELSESSAIAEYLEERFapP 86

                         90
                 ....*....|....*..
gi 15220905   83 DAASFLPSDPQSRATAR 99
Cdd:PRK15113  87 AWERIYPADLQARARAR 103

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220905    15 ASPYAMRTKVALREKGVEFEVQEEDL--WNKSELLLKSNPVHkKVPVL-IHNNTPISESLIQVQYIDET 80
Cdd:pfam13409   1 FSPFSHRVRLALEEKGLPYEIELVDLdpKDKPPELLALNPLG-TVPVLvLPDGTVLTDSLVILEYLEEL 68

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 15220905   121 KKGEEQEKGKKEFLESLKVLEAELGDKSYFGGETFGYVDITLVPFYSWFYALEKcgdFSVEAECPKIVAWGKRCVER 197
Cdd:pfam00043  19 KKEPEVDEALEKVARVLSALEEVLKGQTYLVGDKLTLADIALAPALLWLYELDP---ACLREKFPNLKAWFERVAAR 92

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220905   127 EKGKKEFLESLKVLEAELGDKSYFGGETFGYVDITLVPFYSWFYALEKCGDFsvEAECPKIVAW 190
Cdd:pfam13410   3 ERAREQLRAALDALEARLADGPGLLGDRPTLADIALAPVLARLDAAYPGLDL--REGYPRLRAW 64

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 15220905  17 PYAMRTKVALREKGVEFEVQEEDLWNKSELLLKSNPVhKKVPVLIHNNTP-ISESLIQVQYID 78
Cdd:cd03055  28 PYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPQ-GKVPALEIDEGKvVYESLIICEYLD 89

putative glutathione S-transferase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220905   14 WASPYAMRTKVALREKGVEFEVQEEDLWNKSELLLKSNPVhKKVPVLIHNNTPI-SESLIQVQYIdETWTDAASFLPSDP 92
Cdd:PRK10357   7 YTSPFVRKISILLLEKGITFEFVNELPYNADNGVAQYNPL-GKVPALVTEEGECwFDSPIIAEYI-ELLNVAPAMLPRDP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220905   93 QSRATARFWADYAD-----KTISFEGGRKIWGNKKGEEQEKGKKEFLESLKVLEAELGDKSyFGGETFGYVDITLVPFYS 167
Cdd:PRK10357  85 LAALRVRQLEALADgimdaALVSVREQARPAAQQSEDELLRQREKINRSLDALEGYLVDGT-LKTDTVNLATIAIACAVG 163

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 15220905  168 WFYALEKCGDFSVEAecPKIVAWGKRCVERNSVAATLP 205
Cdd:PRK10357 164 YLNFRRVAPGWCVDR--PHLVKLVENLFQRESFARTEP 199

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        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220905  12 DFWASPYAMRTKVALREKGVEFEVQEEDLWN---KSELLLKSNPVhKKVPVLIHNNTPISESLIQVQYID 78
Cdd:cd03042   5 SYFRSSASYRVRIALNLKGLDYEYVPVNLLKgeqLSPAYRALNPQ-GLVPTLVIDGLVLTQSLAIIEYLD 73

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.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220905  19 AMRTKVALREKGVEFEVQEEDL---WNKSELLLKSNPvHKKVPVLIHNNTPISESLIQVQYI 77
Cdd:cd03046  11 SFRILWLLEELGLPYELVLYDRgpgEQAPPEYLAINP-LGKVPVLVDGDLVLTESAAIILYL 71

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        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220905  12 DFWASPYAMRTKVALREKGVEFEVQEEDLW---NKSELLLKSNPvHKKVPVL-IHNNTPISESLIQVQYID 78
Cdd:cd03051   5 DSPTAPNPRRVRIFLAEKGIDVPLVTVDLAageQRSPEFLAKNP-AGTVPVLeLDDGTVITESVAICRYLE 74

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 15220905 137 LKVLEAELGDKSYFGGETFGYVDITLvpfYSWFYALEKCGDFSVEaECPKIVAWGKRCVERNSV 200
Cdd:cd03178  49 YGVLDKRLSDRPYLAGEEYSIADIAL---YPWTHYADLGGFADLS-EYPNVKRWLERIAARPAV 108

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
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220905  24 VALREKGVEFEVQEEDLWNKSEL---LLKSNPVHkKVPVLIHNN-TPISESLIQVQYIDET 80
Cdd:cd03057  16 IALEELGLPFELVRVDLRTKTQKgadYLAINPKG-QVPALVLDDgEVLTESAAILQYLADL 75

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
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220905 137 LKVLEAELGDKSYFGGETFGYVDITLvpfysWFyALEKCGDFSV-EAECPKIVAWGKRCVER 197
Cdd:cd03189  67 LDFLEDHLAKHPYFAGDELTAADIMM-----SF-PLEAALARGPlLEQYPNIAAYLERIEAR 122

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 15220905 114 GRKIWGNKKGEEQEKGKKEFLESLKVLEAELGDKSYFGGETFGYVDITLVPFYSWFYalekcgDFSVEAECPKIVAWGKR 193
Cdd:cd03207  22 GRFFEPPWGEPAIAAAYGDLDERLAALEAALAGRPYLVGERFSAADLLLASVLRWAR------AFGLLPEYPALRAYVAR 95

                ....
gi 15220905 194 CVER 197
Cdd:cd03207  96 CTAR 99

C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220905 127 EKGKKEFLESLKVLEAELGDKSYFGGETFGYVDITLVPF-YSWFyalekcgDFSVE-AECPKIVAWGKRCVER 197
Cdd:cd03180  42 AASLAACNKLMAILDAQLARQAYLAGDRFTLADIALGCSvYRWL-------ELPIErPALPHLERWYARLSQR 107