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 15241956 113 DHAKREFGDELLKYTDTFVKTMYVSL-KGDPSKETAPVLDYLENALYKFDDGPFFLGQLSLVDIAYIPFIERFQTVLNEL 191
Cdd:cd03203   1 DPAKREFADELLAYADTFTKAVYSALiKGDMTAEAAAAFDYLENALSKFDDGPFFLGQFSLVDIAYAPFIERFQIVLSEL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15241956 192 FKCDITAERPKLSAWIEEINKSDGYAQTKMDPKEIVEVFK 231
Cdd:cd03203  81 RNYDITAGRPNLAKWIEEMNKIEAYTQTKVDPEELLELYK 120

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 15241956 113 DHAKREFGDELLKYTDTFVKTMYVSL-KGDPSKETAPVLDYLENALYKFDDGPFFLGQLSLVDIAYIPFIERFQTVLNEL 191
Cdd:cd03203   1 DPAKREFADELLAYADTFTKAVYSALiKGDMTAEAAAAFDYLENALSKFDDGPFFLGQFSLVDIAYAPFIERFQIVLSEL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15241956 192 FKCDITAERPKLSAWIEEINKSDGYAQTKMDPKEIVEVFK 231
Cdd:cd03203  81 RNYDITAGRPNLAKWIEEMNKIEAYTQTKVDPEELLELYK 120

Glutathione S-transferase, N-terminal domain;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15241956    31 LYTSYVCPFAQRVWITRNFKGLQekIKLVPLDLGNRPAWYKeKVYPENKVPALEHNGKIIGESLDLIKYLDNTFEGPS 108
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLP--YEFVPIPPGDHPPELL-AKNPLGKVPVLEDDGGILCESLAIIDYLEELYPGPP 75

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        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241956  19 SDPPSLFDGTTRLYTSYVCPFAQRVWITRNFKGLQEKIklVPLDLGNRPAWYKEKvYPENKVPALEHN-GKIIGESLDLI 97
Cdd:cd03055   9 SAEPPPVPGIIRLYSMRFCPYAQRARLVLAAKNIPHEV--ININLKDKPDWFLEK-NPQGKVPALEIDeGKVVYESLIIC 85

                ....
gi 15241956  98 KYLD 101
Cdd:cd03055  86 EYLD 89

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241956   150 LDYLENALYkfDDGPFFLGQLSLVDIAYIPFIERFQTVLNELfkcDITAERPKLSAWIEE 209
Cdd:pfam13410  13 LDALEARLA--DGPGLLGDRPTLADIALAPVLARLDAAYPGL---DLREGYPRLRAWLER 67

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 15241956 113 DHAKREFGDELLKYTDTFVKTMYVSL-KGDPSKETAPVLDYLENALYKFDDGPFFLGQLSLVDIAYIPFIERFQTVLNEL 191
Cdd:cd03203   1 DPAKREFADELLAYADTFTKAVYSALiKGDMTAEAAAAFDYLENALSKFDDGPFFLGQFSLVDIAYAPFIERFQIVLSEL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15241956 192 FKCDITAERPKLSAWIEEINKSDGYAQTKMDPKEIVEVFK 231
Cdd:cd03203  81 RNYDITAGRPNLAKWIEEMNKIEAYTQTKVDPEELLELYK 120

Glutathione S-transferase, N-terminal domain;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15241956    31 LYTSYVCPFAQRVWITRNFKGLQekIKLVPLDLGNRPAWYKeKVYPENKVPALEHNGKIIGESLDLIKYLDNTFEGPS 108
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLP--YEFVPIPPGDHPPELL-AKNPLGKVPVLEDDGGILCESLAIIDYLEELYPGPP 75

glutathione dehydrogenase (ascorbate)

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241956   37 CPFAQRVWITRNFKGLQEKIKLVplDLGNRPAWYKeKVYPENKVPALEHNGKIIGESLDLIKYLDNTFEGPSLY--PEdh 114
Cdd:PLN02817  73 CPFCQRVLLTLEEKHLPYDMKLV--DLTNKPEWFL-KISPEGKVPVVKLDEKWVADSDVITQALEEKYPDPPLAtpPE-- 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241956  115 aKREFGDELLKYTDTFVKTMyvslkgDPSKETAPVldyLENALYKFDD-----GPFFLGQ-LSLVDIAYIPFIERFQTVL 188
Cdd:PLN02817 148 -KASVGSKIFSTFIGFLKSK------DPGDGTEQA---LLDELTSFDDyikenGPFINGEkISAADLSLGPKLYHLEIAL 217

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 15241956  189 NELFKCDITAERPKLSAWIEEINKSDGYAQTKMDPKEIVEVFKKKFM 235
Cdd:PLN02817 218 GHYKNWSVPDSLPFVKSYMKNIFSMESFVKTRALPEDVIAGWRPKVM 264

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 15241956  30 RLYTSYVCPFAQRVWITRNFKGLQekIKLVPLDLGNRPAWYKEKVYPENKVPALEHNGKIIGESLDLIKYLD 101
Cdd:cd00570   2 KLYYFPGSPRSLRVRLALEEKGLP--YELVPVDLGEGEQEEFLALNPLGKVPVLEDGGLVLTESLAILEYLA 71

glutathione transferase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241956   30 RLYT--SYVCPFAQRVWITRNFKGLQEKIKLVPLDLG-NRPAWYKEkVYPENKVPALEHNGKIIGESLDLIKYLDNTFEG 106
Cdd:PRK15113   7 TLYSdaHFFSPYVMSAFVALQEKGLPFELKTVDLDAGeHLQPTYQG-YSLTRRVPTLQHDDFELSESSAIAEYLEERFAP 85

                         90
                 ....*....|....
gi 15241956  107 P---SLYPEDHAKR 117
Cdd:PRK15113  86 PaweRIYPADLQAR 99

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15241956 144 KETAPVLDYLENALykfDDGPFFLG-QLSLVDIAYIPFIERFQTVlneLFKCDITAERPKLSAWIE 208
Cdd:cd00299  39 EELPALLAALEQLL---AGRPYLAGdQFSLADVALAPVLARLEAL---GPYYDLLDEYPRLKAWYD 98

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 15241956  31 LYTSYVCPFAQRVWITRNFKGLqeKIKLVPLDLGN---RPAWYKeKVYPENKVPALEHNGKIIGESLDLIKYLD 101
Cdd:cd03042   3 LYSYFRSSASYRVRIALNLKGL--DYEYVPVNLLKgeqLSPAYR-ALNPQGLVPTLVIDGLVLTQSLAIIEYLD 73

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 15241956 144 KETAPVLDYLENALykFDDGPFFLGQ-LSLVDIAYIPF---IERFQTVLNELFkcdITAER-PKLSAWIEEINKSDGYAQ 218
Cdd:cd03185  38 EEALEALKVLEEEL--KGGKPFFGGDtIGYLDIALGSFlgwFKAIEEVGGVKL---LDEEKfPLLAAWAERFLEREAVKE 112

                        90
                ....*....|....
gi 15241956 219 TKMDPKEIVEVFKK 232
Cdd:cd03185 113 VLPDRDKLVEFLKA 126

C-terminal, alpha helical domain of Class Omega-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae Omega-like subfamily; composed of three Saccharomyces cerevisiae GST omega-like (Gto) proteins, Gto1p, Gto2p (also known as Extracellular mutant protein 4 or ECM4p), and Gto3p, as well as similar uncharacterized proteins from fungi and bacteria. The three Saccharomyces cerevisiae Gto proteins are omega-class GSTs with low or no GST activity against standard substrates, but have glutaredoxin/thiol oxidoreductase and dehydroascorbate reductase activity through a single cysteine residue in the active site. Gto1p is located in the peroxisomes while Gto2p and Gto3p are cytosolic. The gene encoding Gto2p, called ECM4, is involved in cell surface biosynthesis and architecture. S. cerevisiae ECM4 mutants show increased amounts of the cell wall hexose, N-acetylglucosamine. More recently, global gene expression analysis shows that ECM4 is upregulated during genotoxic conditions and together with the expression profiles of 18 other genes could potentially differentiate between genotoxic and cytotoxic insults in yeast.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15241956 150 LDYLENALykfDDGPFFLG-QLSLVDIAYIPFIERFQTVLNELFKCDI--TAERPKLSAWIEEI 210
Cdd:cd03190  46 LDKLEKRL---SKQPYLLGdRLTEADIRLFTTLIRFDPVYHQHFKCNLktIRDYPNLWRYLRRL 106

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 15241956  40 AQRV-WItrnfkgLQE-----KIKLVPLDLGN-RPAWYKeKVYPENKVPALEHNGKIIGESLDLIKYL 100
Cdd:cd03046  11 SFRIlWL------LEElglpyELVLYDRGPGEqAPPEYL-AINPLGKVPVLVDGDLVLTESAAIILYL 71

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 15241956  31 LYTSYVCPFAQRVWITRNFKGLQEKIKLVplDLGNRPAWYKEKVyPENKVPALE-HNGKIIGESLDLIKY 99
Cdd:cd03060   3 LYSFRRCPYAMRARMALLLAGITVELREV--ELKNKPAEMLAAS-PKGTVPVLVlGNGTVIEESLDIMRW 69

C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 6; composed of uncharacterized bacterial proteins with similarity to GSTs, including Pseudomonas fluorescens GST with a known three-dimensional structure. 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. Though the three-dimensional structure of Pseudomonas fluorescens GST has been determined, there is no information on its functional characterization.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15241956 150 LDYLENALYKFDDGPFFLGQLSL-VDIAYIPFieRFqtvlnelFKCDITAERPKLSAWIEEINKSDGYAQTK 220
Cdd:cd03205  46 LDALEAELGDLPGGRLTLGDIAVaCALGYLDF--RF-------PELDWRAGHPALAAWFARFEARPSFQATP 108