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 1757624879  87 PFEKALAQFWTKFEDDK-SLAFFAFFRGVGEEQEKATKEAKQLLKIIEDHGLGEKKFFGGNKIGLADLAFGWLSAWLEVM 165
Cdd:cd03185     1 PYERAQARFWAAYIDDKlFPAGRKVWAAKGEEQEKAVEEALEALKVLEEELKGGKPFFGGDTIGYLDIALGSFLGWFKAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1757624879 166 EEVIGVKLKEANSFPRLEAWTKSFKEDPMIKENLPDRDEMLTYFR 210
Cdd:cd03185    81 EEVGGVKLLDEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFLK 125

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 1757624879  87 PFEKALAQFWTKFEDDK-SLAFFAFFRGVGEEQEKATKEAKQLLKIIEDHGLGEKKFFGGNKIGLADLAFGWLSAWLEVM 165
Cdd:cd03185     1 PYERAQARFWAAYIDDKlFPAGRKVWAAKGEEQEKAVEEALEALKVLEEELKGGKPFFGGDTIGYLDIALGSFLGWFKAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1757624879 166 EEVIGVKLKEANSFPRLEAWTKSFKEDPMIKENLPDRDEMLTYFR 210
Cdd:cd03185    81 EEVGGVKLLDEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFLK 125

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 1757624879   4 VKLLGAWPSIYCYKVIWALKLKGVKYEYVEEDLSNKSDLLLKYNPVHKKVPVLVHHGKLVAETSVILEYIQEIW 77
Cdd:cd03058     1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 74

glutathione dehydrogenase (ascorbate)

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757624879   7 LGAWPsiYCYKVIWALKLKGVKYEYVEEDLSNKSDLLLKYNPvHKKVPVLVHHGKLVAETSVILEYIQEIWPQNPLlpND 86
Cdd:PLN02817   70 LGDCP--FCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISP-EGKVPVVKLDEKWVADSDVITQALEEKYPDPPL--AT 144

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1757624879  87 PFEKalAQFWTKFEDdkslAFFAFFR----GVGEEQeKATKEAKQLLKIIEDHGlgekKFFGGNKIGLADLAFG 156
Cdd:PLN02817  145 PPEK--ASVGSKIFS----TFIGFLKskdpGDGTEQ-ALLDELTSFDDYIKENG----PFINGEKISAADLSLG 207

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757624879  95 FWTKFEDDKSLAFFAFFRGVGEEQEKATKEAKQLLKIIEDHgLGEKKFFGGNKIGLADLAfgwLSAWLEVMEEVIGVKLK 174
Cdd:pfam00043   1 LMDLRMQIALLPYVPPEEKKEPEVDEALEKVARVLSALEEV-LKGQTYLVGDKLTLADIA---LAPALLWLYELDPACLR 76

                          90
                  ....*....|....*....
gi 1757624879 175 EAnsFPRLEAWTKSFKEDP 193
Cdd:pfam00043  77 EK--FPNLKAWFERVAARP 93

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 1757624879  87 PFEKALAQFWTKFEDDK-SLAFFAFFRGVGEEQEKATKEAKQLLKIIEDHGLGEKKFFGGNKIGLADLAFGWLSAWLEVM 165
Cdd:cd03185     1 PYERAQARFWAAYIDDKlFPAGRKVWAAKGEEQEKAVEEALEALKVLEEELKGGKPFFGGDTIGYLDIALGSFLGWFKAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1757624879 166 EEVIGVKLKEANSFPRLEAWTKSFKEDPMIKENLPDRDEMLTYFR 210
Cdd:cd03185    81 EEVGGVKLLDEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFLK 125

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 1757624879   4 VKLLGAWPSIYCYKVIWALKLKGVKYEYVEEDLSNKSDLLLKYNPVHKKVPVLVHHGKLVAETSVILEYIQEIW 77
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 1757624879   2 EEVKLLGAWPSIYCYKVIWALKLKGVKYEYVEEDLS---NKSDLLLKYNPVhKKVPVLVHHGKLVAETSVILEYI 73
Cdd:pfam02798   1 MVLTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGagpEKSPELLKLNPL-GKVPALEDGGKKLTESRAILEYI 74

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1757624879  12 SIYCYKVIWALKLKGVKYEYVEEDL--SNKSDLLLKYNPVHkKVPVLVHH-GKLVAETSVILEYIQEI 76
Cdd:pfam13409   2 SPFSHRVRLALEEKGLPYEIELVDLdpKDKPPELLALNPLG-TVPVLVLPdGTVLTDSLVILEYLEEL 68

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 1757624879   5 KLLGAWPSIYCYKVIWALKLKGVKYEYVEEDLSN---KSDLLLKYNPVhKKVPVLVHHGKLVAETSVILEYI 73
Cdd:cd03042     2 ILYSYFRSSASYRVRIALNLKGLDYEYVPVNLLKgeqLSPAYRALNPQ-GLVPTLVIDGLVLTQSLAIIEYL 72

stringent starvation protein A; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757624879  13 IYCYKVIWALKLKGVKYEYVEEDLSNKSDLLLKYNPvHKKVPVLVHHGKLVAETSVILEYIQEIWPQNPLLPNDPFEKAL 92
Cdd:PRK09481   20 IYSHQVRIVLAEKGVSVEIEQVEKDNLPQDLIDLNP-YQSVPTLVDRELTLYESRIIMEYLDERFPHPPLMPVYPVARGE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757624879  93 AQFWT-KFEDD-KSLAfFAFFRGVGEEQEKATKEAKQLLKIIEDHgLGEKKFFGGNKIGLADLAFGWLSAWLEVME-EVI 169
Cdd:PRK09481   99 SRLMMhRIEKDwYSLM-NKIVNGSASEADAARKQLREELLAIAPV-FGEKPYFMSEEFSLVDCYLAPLLWRLPVLGiELS 176

                  ....*.
gi 1757624879 170 GVKLKE 175
Cdd:PRK09481  177 GPGAKE 182

putative glutathione S-transferase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757624879   5 KLLGAWPSIYCYKVIWALKLKGVKYEYVEEDLSNKSDLLLKYNPVhKKVPVLV-HHGKLVAETSVILEYIQEIWPQNPLL 83
Cdd:PRK10357    2 KLIGSYTSPFVRKISILLLEKGITFEFVNELPYNADNGVAQYNPL-GKVPALVtEEGECWFDSPIIAEYIELLNVAPAML 80

                  ....
gi 1757624879  84 PNDP 87
Cdd:PRK10357   81 PRDP 84

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757624879 116 EEQEKATKEAKQLLKIIEDHgLGEKKFFGGNKIGLADLAFGWLSAWLEVMEEVIGVKlkeaNSFPRLEAW 185
Cdd:cd00299    32 AAVEAAREELPALLAALEQL-LAGRPYLAGDQFSLADVALAPVLARLEALGPYYDLL----DEYPRLKAW 96

glutathione transferase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757624879  12 SIYCYKVIWALKLKGVKYEYVEEDLSNKSDLLLKYNPVH--KKVPVLVHHGKLVAETSVILEYIQEIWPQ---NPLLPND 86
Cdd:PRK15113   16 SPYVMSAFVALQEKGLPFELKTVDLDAGEHLQPTYQGYSltRRVPTLQHDDFELSESSAIAEYLEERFAPpawERIYPAD 95

                          90
                  ....*....|...
gi 1757624879  87 PFEKALA---QFW 96
Cdd:PRK15113   96 LQARARArqiQAW 108

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 1757624879 118 QEKATKEAKQL---LKIIEDHGLGEKKFFGGNKIGLADlafgwLSAWLEVME-EVIGVKLKEanSFPRLEAWTKSFKE 191
Cdd:cd03183    40 PEKVKKAEENLeesLDLLENKFLKDKPFLAGDEISIAD-----LSAICEIMQpEAAGYDVFE--GRPKLAAWRKRVKE 110

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 1757624879  12 SIYCYKVIWALKLKGVKYEYVEEDLSNKSDLL-LKYNPVHKKVPVLVH-HGKLVAETSVILEYIQEIWP 78
Cdd:cd03038    16 SPNVWKTRLALNHKGLEYKTVPVEFPDIPPILgELTSGGFYTVPVIVDgSGEVIGDSFAIAEYLEEAYP 84

GST_N family, Metaxin subfamily, Metaxin-like proteins; a heterogenous group of proteins, predominantly uncharacterized, with similarity to metaxins and GSTs. Metaxin 1 is a component of a preprotein import complex of the mitochondrial outer membrane. It extends to the cytosol and is anchored to the mitochondrial membrane through its C-terminal domain. In mice, metaxin is required for embryonic development. In humans, alterations in the metaxin gene may be associated with Gaucher disease. One characterized member of this subgroup is a novel GST from Rhodococcus with toluene o-monooxygenase and gamma-glutamylcysteine synthetase activities. Also members are the cadmium-inducible lysosomal protein CDR-1 and its homologs from C. elegans, and the failed axon connections (fax) protein from Drosophila. CDR-1 is an integral membrane protein that functions to protect against cadmium toxicity and may also have a role in osmoregulation to maintain salt balance in C. elegans. The fax gene of Drosophila was identified as a genetic modifier of Abelson (Abl) tyrosine kinase. The fax protein is localized in cellular membranes and is expressed in embryonic mesoderm and axons of the central nervous system.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1757624879  11 PSIYCYKVIWALKLKGVKYEYVEEDLSNKSDlllkynpvHKKVPVLVHHGKLVAETSVILEYIQE 75
Cdd:cd03080    16 LSPFCLKVETFLRMAGIPYENKFGGLAKRSP--------KGKLPFIELNGEKIADSELIIDHLEE 72