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 42563094  35 VKLIGTWASPFAIRAQVALHLKSVEHEYVEETdvLKGKSDLLIKSNPIHKKVPVLIHGDVSICESLNIVQYVDESW 110
Cdd:cd03058   1 VKLLGAWASPFVLRVRIALALKGVPYEYVEED--LGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 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 42563094  35 VKLIGTWASPFAIRAQVALHLKSVEHEYVEETdvLKGKSDLLIKSNPIHKKVPVLIHGDVSICESLNIVQYVDESW 110
Cdd:cd03058   1 VKLLGAWASPFVLRVRIALALKGVPYEYVEED--LGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 74

Glutathione S-transferase, N-terminal domain;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42563094    37 LIGTWASPFAIRAQVALHLKSVEHEYVEetdVLKGKSDLLIKSNPIHKKVPVLIHGDVSICESLNIVQYVDE 108
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVP---IPPGDHPPELLAKNPLGKVPVLEDDGGILCESLAIIDYLEE 69

glutathione transferase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563094   41 WASPFAIRAQVALHLKSVEHEyVEETDVLKG---KSDLLIKSnpIHKKVPVLIHGDVSICESLNIVQYVDESWPS--DLS 115
Cdd:PRK15113  14 FFSPYVMSAFVALQEKGLPFE-LKTVDLDAGehlQPTYQGYS--LTRRVPTLQHDDFELSESSAIAEYLEERFAPpaWER 90

                         90
                 ....*....|...
gi 42563094  116 ILPTLPSERAFAR 128
Cdd:PRK15113  91 IYPADLQARARAR 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 42563094  35 VKLIGTWASPFAIRAQVALHLKSVEHEYVEETdvLKGKSDLLIKSNPIHKKVPVLIHGDVSICESLNIVQYVDESW 110
Cdd:cd03058   1 VKLLGAWASPFVLRVRIALALKGVPYEYVEED--LGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 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        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42563094  35 VKLIGTWASPFAIRAQVALHLKSVEHEYVEeTDVLKGKSDLLIKSNPiHKKVPVLIHGDVSICESLNIVQYVD 107
Cdd:cd00570   1 LKLYYFPGSPRSLRVRLALEEKGLPYELVP-VDLGEGEQEEFLALNP-LGKVPVLEDGGLVLTESLAILEYLA 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 42563094    34 TVKLIGTWASPFAIRAQVALHLKSVEHEYVEETDVLKG-KSDLLIKSNPIhKKVPVLIHGDVSICESLNIVQYVDE 108
Cdd:pfam02798   2 VLTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGAGPeKSPELLKLNPL-GKVPALEDGGKKLTESRAILEYIAR 76

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 42563094  36 KLIGTWASPFAIRAQVALHLKSVEHEYVEeTDVLKG--KSDLLIKSNPIhKKVPVLIHGDVSICESLNIVQYVD 107
Cdd:cd03042   2 ILYSYFRSSASYRVRIALNLKGLDYEYVP-VNLLKGeqLSPAYRALNPQ-GLVPTLVIDGLVLTQSLAIIEYLD 73

stringent starvation protein A; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563094   57 SVEHEYVEETDVlkgkSDLLIKSNPiHKKVPVLIHGDVSICESLNIVQYVDESWPSDlSILPTLPSERAFARFWAHFVDG 136
Cdd:PRK09481  35 SVEIEQVEKDNL----PQDLIDLNP-YQSVPTLVDRELTLYESRIIMEYLDERFPHP-PLMPVYPVARGESRLMMHRIEK 108

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 42563094  137 ---KLFESIDAVAGAKDDAARmtlaGNLMENLAALEEAF 172
Cdd:PRK09481 109 dwySLMNKIVNGSASEADAAR----KQLREELLAIAPVF 143

glutathione transferase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563094   41 WASPFAIRAQVALHLKSVEHEyVEETDVLKG---KSDLLIKSnpIHKKVPVLIHGDVSICESLNIVQYVDESWPS--DLS 115
Cdd:PRK15113  14 FFSPYVMSAFVALQEKGLPFE-LKTVDLDAGehlQPTYQGYS--LTRRVPTLQHDDFELSESSAIAEYLEERFAPpaWER 90

                         90
                 ....*....|...
gi 42563094  116 ILPTLPSERAFAR 128
Cdd:PRK15113  91 IYPADLQARARAR 103

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 42563094 127 ARFWAHFVDGKLFESI------DAVAGAKDDAARMTLAGNLMENLAALEEAFQksskGGDFFGGGNIGFVDITVGAIvgp 200
Cdd:cd00299   1 VRALEDWADATLAPPLvrllylEKVPLPKDEAAVEAAREELPALLAALEQLLA----GRPYLAGDQFSLADVALAPV--- 73

                        90       100
                ....*....|....*....|....*..
gi 42563094 201 ISVIEAFsGVKFLRPDTTPGLIQWAEK 227
Cdd:cd00299  74 LARLEAL-GPYYDLLDEYPRLKAWYDR 99

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
                ....*....|....*....|....*.
gi 42563094  80 NPiHKKVPVLIHGDVSICESLNIVQY 105
Cdd:cd03046  46 NP-LGKVPVLVDGDLVLTESAAIILY 70

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42563094  44 PFAIRAQVALHLKSVEheyVEETDV-LKGKSDLLIKSNPiHKKVPVLI-HGDVSICESLNIVQY 105
Cdd:cd03060  10 PYAMRARMALLLAGIT---VELREVeLKNKPAEMLAASP-KGTVPVLVlGNGTVIEESLDIMRW 69