C-terminal, alpha helical domain of Class Zeta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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. 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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262209002 114 RAHVRALAQMVACEIHPLNNLRVLKYLVHQMGASDEAKNGWYAHWVRSGLEAFERQLALldaerkamglAPSTFCWGDAP 193
Cdd:cd03191    4 RARVRAIALIIACDIHPLQNLRVLKYLTEKLGVSEEEKLAWAQHWIERGFQALEKLLAS----------TAGKYCVGDEP 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 262209002 194 TLAECCLVPQIYNAQRFNVNLEALPRLMDVVERCNALPAFQQAHPS 239
Cdd:cd03191   74 TLADICLVPQVYNARRFGVDLSPYPTIVRINEACLELPAFQAAHPE 119

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 262209002   33 SSASYRVRIALQLKGLSYDSVPVHLvRGEQKAAAYASHVGDALVPALVTDEGHWLTQSMAIIEYLDET 100
Cdd:pfam13409   2 SPFSHRVRLALEEKGLPYEIELVDL-DPKDKPPELLALNPLGTVPVLVLPDGTVLTDSLVILEYLEEL 68

C-terminal, alpha helical domain of Class Zeta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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. 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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262209002 114 RAHVRALAQMVACEIHPLNNLRVLKYLVHQMGASDEAKNGWYAHWVRSGLEAFERQLALldaerkamglAPSTFCWGDAP 193
Cdd:cd03191    4 RARVRAIALIIACDIHPLQNLRVLKYLTEKLGVSEEEKLAWAQHWIERGFQALEKLLAS----------TAGKYCVGDEP 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 262209002 194 TLAECCLVPQIYNAQRFNVNLEALPRLMDVVERCNALPAFQQAHPS 239
Cdd:cd03191   74 TLADICLVPQVYNARRFGVDLSPYPTIVRINEACLELPAFQAAHPE 119

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 262209002  25 MKLHTYFRSSASYRVRIALQLKGLSYDSVPVHLVRGEQKAAAYASHVGDALVPALVTDeGHWLTQSMAIIEYLD 98
Cdd:cd03042    1 MILYSYFRSSASYRVRIALNLKGLDYEYVPVNLLKGEQLSPAYRALNPQGLVPTLVID-GLVLTQSLAIIEYLD 73

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 262209002  25 MKLHTYFRSSASYRVRIALQLKGLSYDSVPVHLVRGEQKAAAYASHVGDALVPALVTDEGHWLTQSMAIIEYLD 98
Cdd:cd03051    1 MKLYDSPTAPNPRRVRIFLAEKGIDVPLVTVDLAAGEQRSPEFLAKNPAGTVPVLELDDGTVITESVAICRYLE 74

glutathione transferase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262209002  31 FRSSASYRVRIALQLKGLSYDSVPVHLVRGEQKAAAYASHVGDALVPALVTDeGHWLTQSMAIIEYLDETHAETP---LL 107
Cdd:PRK15113  14 FFSPYVMSAFVALQEKGLPFELKTVDLDAGEHLQPTYQGYSLTRRVPTLQHD-DFELSESSAIAEYLEERFAPPAwerIY 92

                         90
                 ....*....|.
gi 262209002 108 PRDALGRAHVR 118
Cdd:PRK15113  93 PADLQARARAR 103

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        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 262209002  25 MKLHTYFRSSASYRVRIALQLKGLSYDSVPVHLVRGEQKAAAYASHVGDALVPALVtDEGHWLTQSMAIIEYL 97
Cdd:cd03056    1 MKLYGFPLSGNCYKVRLLLALLGIPYEWVEVDILKGETRTPEFLALNPNGEVPVLE-LDGRVLAESNAILVYL 72

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        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 262209002  25 MKLHTYFRSSASYRVRIALQLKGLSYDSVPVHLVRGEQKAAAYASHVGDALVPALVtDEGHWLTQSMAIIEYLDE 99
Cdd:cd03053    2 LKLYGAAMSTCVRRVLLCLEEKGVDYELVPVDLTKGEHKSPEHLARNPFGQIPALE-DGDLKLFESRAITRYLAE 75

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 262209002  37 YRVRIALQLKGLSYDSVPVHLVRGEQKAAAYASHVGDAlVPALVTDEGHWLTQSMAIIEYLDETH 101
Cdd:cd03038   20 WKTRLALNHKGLEYKTVPVEFPDIPPILGELTSGGFYT-VPVIVDGSGEVIGDSFAIAEYLEEAY 83

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 262209002  25 MKLHTYFRSSASYRVRIALQLKGLSYDSVPVHLvrGEQKAAAYASHVGDALVPALVTDeGHWLTQSMAIIEYLDET 100
Cdd:cd03058    1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDL--GNKSELLLASNPVHKKIPVLLHN-GKPICESLIIVEYIDEA 73

glutathione S-transferase

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262209002  34 SASYRVRIALQLKGLSYDSVPVHLVRGEQKAAAYASHVGDALVPALVtDEGHWLTQSMAIIEYLDETHAE--TPLLPRDA 111
Cdd:PLN02395  11 ASPKRALVTLIEKGVEFETVPVDLMKGEHKQPEYLALQPFGVVPVIV-DGDYKIFESRAIMRYYAEKYRSqgPDLLGKTI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262209002 112 LGRAHVRALAQMVACEIHP-LNNLRVLKYLVHQMGASDEAKNgwyahwvrsgLEAFERQLA-LLDA--ERkamgLAPSTF 187
Cdd:PLN02395  90 EERGQVEQWLDVEATSYHPpLLNLTLHILFASKMGFPADEKV----------IKESEEKLAkVLDVyeAR----LSKSKY 155

                        170
                 ....*....|....*
gi 262209002 188 CWGDAPTLAECCLVP 202
Cdd:PLN02395 156 LAGDFVSLADLAHLP 170

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 262209002  26 KLHTyFRSSASYRVRIALQLKGLSYDSVPVHLVRGEQKAAAYASHVGDALVPALV--TDEGHWLTQSMAIIEYLDETH 101
Cdd:cd03048    3 TLYT-HGTPNGFKVSIMLEELGLPYEIHPVDISKGEQKKPEFLKINPNGRIPAIVdhNGTPLTVFESGAILLYLAEKY 79

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 262209002  38 RVRIALQLKGLSYDSVPVHLVRgeqKAAAYASHVGDALVPALVTDEGHWLTQSMAIIEYLD 98
Cdd:cd03055   32 RARLVLAAKNIPHEVININLKD---KPDWFLEKNPQGKVPALEIDEGKVVYESLIICEYLD 89

GST_N family, unknown subfamily 1; composed of uncharacterized proteins, predominantly from bacteria, 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 262209002  33 SSASYRVRIALQLKGLSYDSVPVHLVRGEQKAAAyASHVGDALVPALVTDEGH-WltQSMAIIEYL 97
Cdd:cd03043   10 SSWSLRPWLLLKAAGIPFEEILVPLYTPDTRARI-LEFSPTGKVPVLVDGGIVvW--DSLAICEYL 72

GST_N family, unknown subfamily 3; 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        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 262209002  25 MKLhtyFRSSAS-Y--RVRIALQLKGLSyDSVPVHLVRGEQKAAAYASHVGDALVPALVTDEGHWLTQSMAIIEYLD 98
Cdd:cd03049    1 MKL---LYSPTSpYvrKVRVAAHETGLG-DDVELVLVNPWSDDESLLAVNPLGKIPALVLDDGEALFDSRVICEYLD 73