C-terminal, alpha helical domain of Escherichia coli Yghu Glutathione S-transferases and related uncharacterized proteins; Glutathione S-transferase (GST) C-terminal domain family, YghU-like subfamily; composed of the Escherichia coli YghU and related 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. 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. YghU is one of nine GST homologs in the genome of Escherichia coli. It is similar to Escherichia coli YfcG in that it has poor GSH transferase activity towards typical substrates. It shows modest reductase activity towards some organic hydroperoxides. Like YfcG, YghU also shows good disulfide bond oxidoreductase activity comparable to the activities of glutaredoxins and thioredoxins. YghU does not contain a redox active cysteine residue, and may use a bound thiol disulfide couple such as 2GSH/GSSG for activity. The crystal structure of YghU reveals two GSH molecules bound in its active site.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309086001 139 ARAEVLSWVFWQVGTGPFIGGGFGHFYAYAPEKYEYPINRYAMETKRIFDVADKRLGETRFLAGDDYTIADIANFPWLAP 218
Cdd:cd10292     1 KRTETLNWLFWQMGSAPYLGGGFGHFYSYAPVKIEYAIDRFTMEAKRQLDVLDRQLATHKYLAGDEYTIADMAIWPWYGG 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1309086001 219 FTTGEIYnDAKTFLSIDEYKNVGRWVKDIYARPAVKRGR 257
Cdd:cd10292    81 LALGSLY-DAAEFLDVDEYKHVQRWAKDIAARPAVKRGR 118

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 1309086001 182 ETKRIFDVADKRLGETRFLAGDDYTIADIANFPWLapfttgEIYNDAKTFLSIDEYKNVGRWVKDIYARP 251
Cdd:pfam00043  30 KVARVLSALEEVLKGQTYLVGDKLTLADIALAPAL------LWLYELDPACLREKFPNLKAWFERVAARP 93

C-terminal, alpha helical domain of Escherichia coli Yghu Glutathione S-transferases and related uncharacterized proteins; Glutathione S-transferase (GST) C-terminal domain family, YghU-like subfamily; composed of the Escherichia coli YghU and related 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. 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. YghU is one of nine GST homologs in the genome of Escherichia coli. It is similar to Escherichia coli YfcG in that it has poor GSH transferase activity towards typical substrates. It shows modest reductase activity towards some organic hydroperoxides. Like YfcG, YghU also shows good disulfide bond oxidoreductase activity comparable to the activities of glutaredoxins and thioredoxins. YghU does not contain a redox active cysteine residue, and may use a bound thiol disulfide couple such as 2GSH/GSSG for activity. The crystal structure of YghU reveals two GSH molecules bound in its active site.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309086001 139 ARAEVLSWVFWQVGTGPFIGGGFGHFYAYAPEKYEYPINRYAMETKRIFDVADKRLGETRFLAGDDYTIADIANFPWLAP 218
Cdd:cd10292     1 KRTETLNWLFWQMGSAPYLGGGFGHFYSYAPVKIEYAIDRFTMEAKRQLDVLDRQLATHKYLAGDEYTIADMAIWPWYGG 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1309086001 219 FTTGEIYnDAKTFLSIDEYKNVGRWVKDIYARPAVKRGR 257
Cdd:cd10292    81 LALGSLY-DAAEFLDVDEYKHVQRWAKDIAARPAVKRGR 118

GSH-dependent disulfide bond oxidoreductase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309086001  47 LYSLATPNGVKVTVMLEElieaghAGAEYDAWTVNIGSGDQFTSGFVAANPNSKIPALIDRS---GPQPFRVFESGAILV 123
Cdd:PRK13972    4 LYFAPTPNGHKITLFLEE------AELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDHSpadGGEPLSLFESGAILL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309086001 124 HLAEKFGAFLPTDPQARAEVLSWVFWQVG-TGPFIGGGFgHFYAYAPEKYEYPINRYAMETKRIFDVADKRLGETRFLAG 202
Cdd:PRK13972   78 YLAEKTGLFLSHETRERAATLQWLFWQVGgLGPMLGQNH-HFNHAAPQTIPYAIERYQVETQRLYHVLNKRLENSPWLGG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1309086001 203 DDYTIADIANFPWLAPFTTGEIyndaktflSIDEYKNVGRWVKDIYARPA 252
Cdd:PRK13972  157 ENYSIADIACWPWVNAWTRQRI--------DLAMYPAVKNWHERIRSRPA 198

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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309086001 139 ARAEVLSWVFWQVGTGPFIGGGFGHFYAYAPEKYEYPINRYAMETKRIFDVADKRLGETRFLAGDDYTIADIANFPWLAP 218
Cdd:cd03178     1 ERAEVLQWLFFQMSGLGPMFGQAGHFLYFAPEKIPYAIERYTDEVKRLYGVLDKRLSDRPYLAGEEYSIADIALYPWTHY 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1309086001 219 FTTGEIYndaktflSIDEYKNVGRWVKDIYARPAVKR 255
Cdd:cd03178    81 ADLGGFA-------DLSEYPNVKRWLERIAARPAVQK 110

C-terminal, alpha helical domain of fungal Ure2p Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Ure2p subfamily; composed of the Saccharomyces cerevisiae Ure2p and related fungal 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. 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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309086001 141 AEVLSWVFWQV-GTGPFIGGgFGHFYAYAPEKYEYPINRYAMETKRIFDVADKRLGET--RFLAGDDYTIADIANFPWLA 217
Cdd:cd10293     3 YQAKQWLFFQAsGQGPYWGQ-AGWFNVFHAEKVPSAIERYTNEIRRVLGVLETALAERyrVWLVGDKFTIADLAFVPWNN 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1309086001 218 pfTTGEIYNDAKTFLsIDEYKNVGRWVKDIYARPAVKRG 256
Cdd:cd10293    82 --VVDMIFIDPELDI-KKEFPHVYKWLKRMLARPAVKKA 117

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        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309086001  61 MLEELieaghaGAEYDAWTVNIGSGDQFTSGFVAANPNSKIPALIDrsgpQPFRVFESGAILVHLAEKFG 130
Cdd:cd03046    17 LLEEL------GLPYELVLYDRGPGEQAPPEYLAINPLGKVPVLVD----GDLVLTESAAIILYLAEKYG 76

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309086001  46 QLYSLAT-PNGVKVTVMLEELieaghaGAEYDAWTVNIGSGDQFTsgFVAANPNSKIPALIDRsgpqPFRVFESGAILVH 124
Cdd:cd00570     2 KLYYFPGsPRSLRVRLALEEK------GLPYELVPVDLGEGEQEE--FLALNPLGKVPVLEDG----GLVLTESLAILEY 69

                  ..
gi 1309086001 125 LA 126
Cdd:cd00570    70 LA 71

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309086001 138 QARAEVLSWVFWQVGT-GPFIGGGFGHFYAYAPEKYEYP-INRYAMETKRIFDVADKRLGETRFLAGDDYTIADIA---- 211
Cdd:cd03180     1 AQRALADRWMDWQTSTlNPAFRYAFWGLVRTPPEQRDPAaIAASLAACNKLMAILDAQLARQAYLAGDRFTLADIAlgcs 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1309086001 212 NFPWLApfttgeiyndaktfLSID--EYKNVGRWVKDIYARPA 252
Cdd:cd03180    81 VYRWLE--------------LPIErpALPHLERWYARLSQRPA 109

GST_N 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. 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 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 aryl or alkyl sulfate esters.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1309086001  74 EYDAWTVNIGSGDQFTSGFVAANPNSKIPALIDRSgpqpFRVFESGAILVHLAEKF 129
Cdd:cd03050    25 PFEECPIDLRKGEQLTPEFKKINPFGKVPAIVDGD----FTLAESVAILRYLARKF 76

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        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309086001  60 VMLEELieaghaGAEYDAWTVNIGSGDQFTSGFVAANPNSKIPALIDrsgPQPFRVFESGAILVHLAEKF 129
Cdd:cd03057    16 IALEEL------GLPFELVRVDLRTKTQKGADYLAINPKGQVPALVL---DDGEVLTESAAILQYLADLH 76

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309086001  44 PFQLYSLA-TPNGVKVTVMLEElieaghAGAEYDAWTVNIGSGDQFTSGFVAANPNSKIPALIDrsgpQPFRVFESGAIL 122
Cdd:cd03053     1 VLKLYGAAmSTCVRRVLLCLEE------KGVDYELVPVDLTKGEHKSPEHLARNPFGQIPALED----GDLKLFESRAIT 70

                  ....*.
gi 1309086001 123 VHLAEK 128
Cdd:cd03053    71 RYLAEK 76

C-terminal, alpha helical domain of an unknown subfamily 7 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 7; composed of uncharacterized 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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309086001 174 YPIN--RYAMETKRIFDVADKRLGETRFLAGDDYTIADIANFPWLAPFTTGEIyndaktflSIDEYKNVGRWVKDIYARP 251
Cdd:cd03206    27 APLDpeRARAISHRLLRLLDQHLAGRDWLAGDRPTIADVACYPYIALAPEGGV--------SLEPYPAIRAWLARVEALP 98

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 1309086001 166 AYAPEKYEYPINRYAMETKR-----IFDVADKRLGETRFLAGDDYTIADIANFPWLAPFTTGEIYndaktFLSIDEYKNV 240
Cdd:cd00299    19 LLYLEKVPLPKDEAAVEAAReelpaLLAALEQLLAGRPYLAGDQFSLADVALAPVLARLEALGPY-----YDLLDEYPRL 93

                  ....*
gi 1309086001 241 GRWVK 245
Cdd:cd00299    94 KAWYD 98

glutathione transferase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309086001  44 PFQLYS---LATPNGVKVTVMLEElieaghAGAEYDAWTVNIGSGDQFTSGFVAANPNSKIPAL-IDRsgpqpFRVFESG 119
Cdd:PRK15113    5 AITLYSdahFFSPYVMSAFVALQE------KGLPFELKTVDLDAGEHLQPTYQGYSLTRRVPTLqHDD-----FELSESS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309086001 120 AILVHLAEKFGA-----FLPTDPQARA---EVLSW----------------VFWQVGTGPFIGGGfghfyayapekyeyp 175
Cdd:PRK15113   74 AIAEYLEERFAPpawerIYPADLQARArarQIQAWlrsdlmplreerptdvVFAGAKKAPLSEAG--------------- 138

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1309086001 176 inRYAMEtkRIFDVADKRLGETR-FLAGdDYTIAD 209
Cdd:PRK15113  139 --KAAAE--KLFAVAERLLAPGQpNLFG-EWCIAD 168

GST_N family, Class Delta and Epsilon 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. 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. The class Delta and Epsilon subfamily is made up primarily of insect GSTs, which play major roles in insecticide resistance by facilitating reductive dehydrochlorination of insecticides or conjugating them with GSH to produce water-soluble metabolites that are easily excreted. They are also implicated in protection against cellular damage by oxidative stress.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1309086001  72 GAEYDAWTVNIGSGDQFTSGFVAANPNSKIPALIDrsgpQPFRVFESGAILVHLAE 127
Cdd:cd03045    23 GLELNLKEVNLMKGEHLKPEFLKLNPQHTVPTLVD----NGFVLWESHAILIYLVE 74

glutathionine S-transferase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309086001  92 FVAANPNSKIPALIDRSGPQpfrVFESGAILVHLAEKF---GAFLPTDPQARAEVLSWVFWqvgTGPFIGGGFGH-FYAY 167
Cdd:PRK10542   43 YLAINPKGQVPALLLDDGTL---LTEGVAIMQYLADSVpdrQLLAPVGSLSRYHTIEWLNY---IATELHKGFTPlFRPD 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309086001 168 APEKYEyPINRYAMETKriFDVADKRLGETRFLAGDDYTIADianfPWLapFTTGEIYNDAKtfLSIDEYKNVGRWVKDI 247
Cdd:PRK10542  117 TPEEYK-PTVRAQLEKK--FQYVDEALADEQWICGQRFTIAD----AYL--FTVLRWAYAVK--LNLEGLEHIAAYMQRV 185

                  ....*..
gi 1309086001 248 YARPAVK 254
Cdd:PRK10542  186 AERPAVA 192

GST_N 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The sequence from Burkholderia cepacia was identified as part of a gene cluster involved in the degradation of 2,4,5-trichlorophenoxyacetic acid. Some GSTs (e.g. Class Zeta and Delta) are known to catalyze dechlorination reactions.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309086001  57 KVTVMLEELieaghaGAEYDawtvNIGSGDQF----TSGFVAANPNSKIPALIDRSgpqpFRVFESGAILVHLA 126
Cdd:cd03047    14 KVLWLLDEL------GLPYE----RIDAGGQFggldTPEFLAMNPNGRVPVLEDGD----FVLWESNAILRYLA 73

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309086001  53 PNGVKVTVMLEELieaghaGAEYDAWTVNIgSGDQFTSGFVAANPNSKIPALIDRSGpqpFRVFESGAILVHLAEK 128
Cdd:pfam13409   3 PFSHRVRLALEEK------GLPYEIELVDL-DPKDKPPELLALNPLGTVPVLVLPDG---TVLTDSLVILEYLEEL 68

C-terminal, alpha helical domain of Metaxin and related proteins; Glutathione S-transferase (GST) C-terminal domain family, Metaxin subfamily; composed of metaxins and related proteins. 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. Metaxin 2 binds to metaxin 1 and may also play a role in protein translocation into the mitochondria. Genome sequencing shows that a third metaxin gene also exists in zebrafish, Xenopus, chicken, and mammals. Sequence analysis suggests that all three metaxins share a common ancestry and that they possess similarity to GSTs. Also included in the subfamily are uncharacterized proteins with similarity to metaxins, including a novel GST from Rhodococcus with toluene o-monooxygenase and glutamylcysteine synthetase activities. Other 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.

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gi 1309086001 174 YPINRYAMETK--RIFDVADKRLGETRFLAGDDYTIADIANFPWLAPF 219
Cdd:cd03193    13 YWALRREIYELalEDLEALSTLLGDKKFLFGDKPTSVDATVFAHLASI 60