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 2103227677  88 PYQRAMARFWVKFIDEKCEPAMWIACWSEGKEQEKAMEEAWEHLRKLENELKG-KKFFGGETIGFVDIAANLIAFWFGIF 166
Cdd:cd03185     1 PYERAQARFWAAYIDDKLFPAGRKVWAAKGEEQEKAVEEALEALKVLEEELKGgKPFFGGDTIGYLDIALGSFLGWFKAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2103227677 167 EEVVGIKLVDEEKLPILCRWIEQFLSCDVVKECLPPRDELLLFFQAR 213
Cdd:cd03185    81 EEVGGVKLLDEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFLKAL 127

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 2103227677  88 PYQRAMARFWVKFIDEKCEPAMWIACWSEGKEQEKAMEEAWEHLRKLENELKG-KKFFGGETIGFVDIAANLIAFWFGIF 166
Cdd:cd03185     1 PYERAQARFWAAYIDDKLFPAGRKVWAAKGEEQEKAVEEALEALKVLEEELKGgKPFFGGDTIGYLDIALGSFLGWFKAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2103227677 167 EEVVGIKLVDEEKLPILCRWIEQFLSCDVVKECLPPRDELLLFFQAR 213
Cdd:cd03185    81 EEVGGVKLLDEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFLKAL 127

Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103227677   9 GMWISPFSRRVELALKLKGVSYEYIEEDLA---NKSPLLLKYNPIHKkIPVLLHNEKIIIESTVILEYIVETWKGYSLLP 85
Cdd:COG0625     6 GSPPSPNSRRVRIALEEKGLPYELVPVDLAkgeQKSPEFLALNPLGK-VPVLVDDGLVLTESLAILEYLAERYPEPPLLP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103227677  86 EDPYQRAMARFWVKFIDEKCEPAMWIACWSEGKEQ-----EKAMEEAWEHLRKLENELKGKKFFGGETIGFVDIAanlIA 160
Cdd:COG0625    85 ADPAARARVRQWLAWADGDLHPALRNLLERLAPEKdpaaiARARAELARLLAVLEARLAGGPYLAGDRFSIADIA---LA 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2103227677 161 FWFGIFEEvVGIKLvdeEKLPILCRWIEQFLSCDVVKECLPPRDELL 207
Cdd:COG0625   162 PVLRRLDR-LGLDL---ADYPNLAAWLARLAARPAFQRALAAAEPDL 204

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 2103227677 118 KEQEKAMEEAWEHLRKLENELKGKKFFGGETIGFVDIAANLIAFWFGIFEEVVGiklvdEEKLPILCRWIEQFLS 192
Cdd:pfam00043  22 PEVDEALEKVARVLSALEEVLKGQTYLVGDKLTLADIALAPALLWLYELDPACL-----REKFPNLKAWFERVAA 91

glutathione dehydrogenase (ascorbate)

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2103227677  14 PFSRRVELALKLKGVSYEYIEEDLANKSPLLLKYNPiHKKIPVLLHNEKIIIESTVILEYIVETWkgysllPEDP 88
Cdd:PLN02817   74 PFCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISP-EGKVPVVKLDEKWVADSDVITQALEEKY------PDPP 141

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 2103227677  88 PYQRAMARFWVKFIDEKCEPAMWIACWSEGKEQEKAMEEAWEHLRKLENELKG-KKFFGGETIGFVDIAANLIAFWFGIF 166
Cdd:cd03185     1 PYERAQARFWAAYIDDKLFPAGRKVWAAKGEEQEKAVEEALEALKVLEEELKGgKPFFGGDTIGYLDIALGSFLGWFKAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2103227677 167 EEVVGIKLVDEEKLPILCRWIEQFLSCDVVKECLPPRDELLLFFQAR 213
Cdd:cd03185    81 EEVGGVKLLDEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFLKAL 127

Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103227677   9 GMWISPFSRRVELALKLKGVSYEYIEEDLA---NKSPLLLKYNPIHKkIPVLLHNEKIIIESTVILEYIVETWKGYSLLP 85
Cdd:COG0625     6 GSPPSPNSRRVRIALEEKGLPYELVPVDLAkgeQKSPEFLALNPLGK-VPVLVDDGLVLTESLAILEYLAERYPEPPLLP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103227677  86 EDPYQRAMARFWVKFIDEKCEPAMWIACWSEGKEQ-----EKAMEEAWEHLRKLENELKGKKFFGGETIGFVDIAanlIA 160
Cdd:COG0625    85 ADPAARARVRQWLAWADGDLHPALRNLLERLAPEKdpaaiARARAELARLLAVLEARLAGGPYLAGDRFSIADIA---LA 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2103227677 161 FWFGIFEEvVGIKLvdeEKLPILCRWIEQFLSCDVVKECLPPRDELL 207
Cdd:COG0625   162 PVLRRLDR-LGLDL---ADYPNLAAWLARLAARPAFQRALAAAEPDL 204

Glutathione S-transferase, N-terminal domain;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2103227677   9 GMWISPFSRRVELALKLKGVSYEYIEEDLANKSPLLLKYNPiHKKIPVLLHNEKIIIESTVILEYI 74
Cdd:pfam13417   3 GFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNP-LGKVPVLEDDGGILCESLAIIDYL 67

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2103227677  13 SPFSRRVELALKLKGVSYEYIEEDL--ANKSPLLLKYNPIHkKIPVL-LHNEKIIIESTVILEYIVET 77
Cdd:pfam13409   2 SPFSHRVRLALEEKGLPYEIELVDLdpKDKPPELLALNPLG-TVPVLvLPDGTVLTDSLVILEYLEEL 68

GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP)-associated protein required for the lytic development of phage P1 and for stationary phase-induced acid tolerance of E. coli. It is implicated in survival during nutrient starvation. SspA adopts the GST fold with an N-terminal TRX-fold domain and a C-terminal alpha helical domain, but it does not bind glutathione (GSH) and lacks GST activity. SspA is highly conserved among gram-negative bacteria. Related proteins found in Neisseria (called RegF), Francisella and Vibrio regulate the expression of virulence factors necessary for pathogenesis.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2103227677  14 PFSRRVELALKLKGVSYEYIEEDLANKSPLLLKYNPIHkKIPVLLHNEKIIIESTVILEYIVE 76
Cdd:cd03059    10 VYSHRVRIVLAEKGVSVEIIDVDPDNPPEDLAELNPYG-TVPTLVDRDLVLYESRIIMEYLDE 71

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        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2103227677  12 ISPFSRRVELALKLKGVSYEYIEEDLANK---SPLLLKYNPIHKkIPVLLHNEKIIIESTVILEYIVE 76
Cdd:cd03045     8 GSPPCRAVLLTAKALGLELNLKEVNLMKGehlKPEFLKLNPQHT-VPTLVDNGFVLWESHAILIYLVE 74

C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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 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 2103227677 125 EEAWEHLRKLENEL--KGKKFFGGETIGFVDIaanLIAFWF---GIFEEVVGIKLvDEEKLPILCRWIEQFLSCDVVKEC 199
Cdd:cd03184    35 EELRSALENLEEELakRGTPFFGGNSPGMVDY---MIWPWFerlEALKLLDGYEL-CLDRFPKLKKWMAAMKQDPAVKAF 110

                          90
                  ....*....|....
gi 2103227677 200 LPPRDELLLFFQAR 213
Cdd:cd03184   111 YTDPETHAEFLNSY 124

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
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2103227677  18 RVELALKLKGVSYEYIEEDLAN---KSPLLLKYNPiHKKIPVLLHNEKIIIESTVILEY 73
Cdd:cd03056    14 KVRLLLALLGIPYEWVEVDILKgetRTPEFLALNP-NGEVPVLELDGRVLAESNAILVY 71

putative glutathione S-transferase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103227677   8 MGMWISPFSRRVELALKLKGVSYEYIEEDLANKSPLLLKYNPIhKKIPVLLHNE-KIIIESTVILEYIVETWKGYSLLPE 86
Cdd:PRK10357    4 IGSYTSPFVRKISILLLEKGITFEFVNELPYNADNGVAQYNPL-GKVPALVTEEgECWFDSPIIAEYIELLNVAPAMLPR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103227677  87 DPYQRAMARFWVKFIDEKCEPAMWIAcwsegKEQEKAMEEAWEH--LRKLENELKG---------KKFFGGETIGFVDIA 155
Cdd:PRK10357   83 DPLAALRVRQLEALADGIMDAALVSV-----REQARPAAQQSEDelLRQREKINRSldalegylvDGTLKTDTVNLATIA 157

                  .
gi 2103227677 156 A 156
Cdd:PRK10357  158 I 158

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 2103227677  94 ARFWVKFIDEK-CEPAMWIACWSEGKE--QEKAMEEAWE----HLRKLENELKGKKFFGGETIGFVDIAanliafWFGIF 166
Cdd:cd00299     1 VRALEDWADATlAPPLVRLLYLEKVPLpkDEAAVEAAREelpaLLAALEQLLAGRPYLAGDQFSLADVA------LAPVL 74

                          90       100
                  ....*....|....*....|....
gi 2103227677 167 E--EVVGIKLVDEEKLPILCRWIE 188
Cdd:cd00299    75 ArlEALGPYYDLLDEYPRLKAWYD 98

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2103227677  13 SPFSRRVELALKLKGVSYEYIEEDLA---NKSPLLLKYNPiHKKIPVL-LHNEKIIIESTVILEYI 74
Cdd:cd03051     9 APNPRRVRIFLAEKGIDVPLVTVDLAageQRSPEFLAKNP-AGTVPVLeLDDGTVITESVAICRYL 73

glutathione transferase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103227677  11 WISPFSRRVELALKLKGVSYEYIEEDLANKSPLLLKYN--PIHKKIPVLLHNEKIIIESTVILEYIVETWKG---YSLLP 85
Cdd:PRK15113   14 FFSPYVMSAFVALQEKGLPFELKTVDLDAGEHLQPTYQgySLTRRVPTLQHDDFELSESSAIAEYLEERFAPpawERIYP 93

                          90
                  ....*....|
gi 2103227677  86 EDPYQRAMAR 95
Cdd:PRK15113   94 ADLQARARAR 103

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 2103227677  12 ISPFSRRVELALKLKGVSYEYIEEDLANKSPlllkynpiHKKIPVLLHNEKIIIESTVILEYIVETWK 79
Cdd:cd03080    16 LSPFCLKVETFLRMAGIPYENKFGGLAKRSP--------KGKLPFIELNGEKIADSELIIDHLEEKYG 75

glutathione S-transferase DHAR1

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103227677  14 PFSRRVELALKLKGVSYEYIEEDLANKSPLLLKYNPiHKKIPVLLHNEKIIIESTVILEYIVETWkgysllPEDPYQRAm 93
Cdd:PLN02378   21 PFSQRALLTLEEKSLTYKIHLINLSDKPQWFLDISP-QGKVPVLKIDDKWVTDSDVIVGILEEKY------PDPPLKTP- 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2103227677  94 arfwVKFIDEKCEPAMWIACWSEGKEQEKAMEEA-WEHLRKLENELKGKK--FFGGETIGFVDIA 155
Cdd:PLN02378   93 ----AEFASVGSNIFGTFGTFLKSKDSNDGSEHAlLVELEALENHLKSHDgpFIAGERVSAVDLS 153

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 2103227677  13 SPFSRRVELALKLKGVSYEYIEEDLANKS--PLLLKYNPiHKKIPVLLHNEKIIIESTVILEYI 74
Cdd:cd03043    10 SSWSLRPWLLLKAAGIPFEEILVPLYTPDtrARILEFSP-TGKVPVLVDGGIVVWDSLAICEYL 72