C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, including GSTs from class Mu, Pi, and Alpha. 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. Vertebrate class Sigma GSTs are characterized as GSH-dependent hematopoietic prostaglandin (PG) D synthases and are responsible for the production of PGD2 by catalyzing the isomerization of PGH2. The functions of PGD2 include the maintenance of body temperature, inhibition of platelet aggregation, bronchoconstriction, vasodilation, and mediation of allergy and inflammation. Other class Sigma-like members include the class II insect GSTs, S-crystallins from cephalopods, nematode-specific GSTs, and 28-kDa GSTs from parasitic flatworms. Drosophila GST2 is associated with indirect flight muscle and exhibits preference for catalyzing GSH conjugation to lipid peroxidation products, indicating an anti-oxidant role. S-crystallin constitutes the major lens protein in cephalopod eyes and is responsible for lens transparency and proper refractive index. The 28-kDa GST from Schistosoma is a multifunctional enzyme, exhibiting GSH transferase, GSH peroxidase, and PGD2 synthase activities, and may play an important role in host-parasite interactions. Members also include novel GSTs from the fungus Cunninghamella elegans, designated as class Gamma, and from the protozoan Blepharisma japonicum, described as a light-inducible GST.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540934  83 EEELQADEVVDTFKDFIESFRKFVIAVLSGESEEILKnireEVIKPAVKTYTAYLKAILEKSSSGYLVGNELTWADLVIA 162
Cdd:cd03192   1 EEEARVDAIVDTIADLRAEFAPYFYEPDGEEKKEKKK----EFLEEALPKFLGKFEKILKKSGGGYFVGDKLTWADLALF 76

                        90       100
                ....*....|....*....|....*...
gi 17540934 163 DNLTTLINAELLDIEND-KLLKEFREKI 189
Cdd:cd03192  77 DVLDYLLYLLPKDLLEKyPKLKALRERV 104

C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, including GSTs from class Mu, Pi, and Alpha. 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. Vertebrate class Sigma GSTs are characterized as GSH-dependent hematopoietic prostaglandin (PG) D synthases and are responsible for the production of PGD2 by catalyzing the isomerization of PGH2. The functions of PGD2 include the maintenance of body temperature, inhibition of platelet aggregation, bronchoconstriction, vasodilation, and mediation of allergy and inflammation. Other class Sigma-like members include the class II insect GSTs, S-crystallins from cephalopods, nematode-specific GSTs, and 28-kDa GSTs from parasitic flatworms. Drosophila GST2 is associated with indirect flight muscle and exhibits preference for catalyzing GSH conjugation to lipid peroxidation products, indicating an anti-oxidant role. S-crystallin constitutes the major lens protein in cephalopod eyes and is responsible for lens transparency and proper refractive index. The 28-kDa GST from Schistosoma is a multifunctional enzyme, exhibiting GSH transferase, GSH peroxidase, and PGD2 synthase activities, and may play an important role in host-parasite interactions. Members also include novel GSTs from the fungus Cunninghamella elegans, designated as class Gamma, and from the protozoan Blepharisma japonicum, described as a light-inducible GST.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540934  83 EEELQADEVVDTFKDFIESFRKFVIAVLSGESEEILKnireEVIKPAVKTYTAYLKAILEKSSSGYLVGNELTWADLVIA 162
Cdd:cd03192   1 EEEARVDAIVDTIADLRAEFAPYFYEPDGEEKKEKKK----EFLEEALPKFLGKFEKILKKSGGGYFVGDKLTWADLALF 76

                        90       100
                ....*....|....*....|....*...
gi 17540934 163 DNLTTLINAELLDIEND-KLLKEFREKI 189
Cdd:cd03192  77 DVLDYLLYLLPKDLLEKyPKLKALRERV 104

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540934   4 YKLTYFNARGLAEISRQLFHMAGVEFEDERINEEKFSQLKPTF----PSGQVPILCIDGAQFSQSTAIARYLARKFG--- 76
Cdd:COG0625   2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFlalnPLGKVPVLVDDGLVLTESLAILEYLAERYPepp 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540934  77 FVGQTAEEELQADEVVdtfkDFIES-----FRKFVIAVLSGESEEILKNIREEvikpaVKTYTAYLKAILEKssSGYLVG 151
Cdd:COG0625  82 LLPADPAARARVRQWL----AWADGdlhpaLRNLLERLAPEKDPAAIARARAE-----LARLLAVLEARLAG--GPYLAG 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17540934 152 NELTWADLVIADNLTTLINAElLDIENDKLLKEFREKIIETPKLKEWLAKR 202
Cdd:COG0625 151 DRFSIADIALAPVLRRLDRLG-LDLADYPNLAAWLARLAARPAFQRALAAA 200

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 17540934     6 LTYFNARG--LAEISRQLFHMAGVEFEDERIN----EEKFSQLKPTFPSGQVPILCIDGAQFSQSTAIARYLAR 73
Cdd:pfam02798   3 LTLYGIRGspRAHRIRWLLAEKGVEYEIVPLDfgagPEKSPELLKLNPLGKVPALEDGGKKLTESRAILEYIAR 76

C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, including GSTs from class Mu, Pi, and Alpha. 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. Vertebrate class Sigma GSTs are characterized as GSH-dependent hematopoietic prostaglandin (PG) D synthases and are responsible for the production of PGD2 by catalyzing the isomerization of PGH2. The functions of PGD2 include the maintenance of body temperature, inhibition of platelet aggregation, bronchoconstriction, vasodilation, and mediation of allergy and inflammation. Other class Sigma-like members include the class II insect GSTs, S-crystallins from cephalopods, nematode-specific GSTs, and 28-kDa GSTs from parasitic flatworms. Drosophila GST2 is associated with indirect flight muscle and exhibits preference for catalyzing GSH conjugation to lipid peroxidation products, indicating an anti-oxidant role. S-crystallin constitutes the major lens protein in cephalopod eyes and is responsible for lens transparency and proper refractive index. The 28-kDa GST from Schistosoma is a multifunctional enzyme, exhibiting GSH transferase, GSH peroxidase, and PGD2 synthase activities, and may play an important role in host-parasite interactions. Members also include novel GSTs from the fungus Cunninghamella elegans, designated as class Gamma, and from the protozoan Blepharisma japonicum, described as a light-inducible GST.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540934  83 EEELQADEVVDTFKDFIESFRKFVIAVLSGESEEILKnireEVIKPAVKTYTAYLKAILEKSSSGYLVGNELTWADLVIA 162
Cdd:cd03192   1 EEEARVDAIVDTIADLRAEFAPYFYEPDGEEKKEKKK----EFLEEALPKFLGKFEKILKKSGGGYFVGDKLTWADLALF 76

                        90       100
                ....*....|....*....|....*...
gi 17540934 163 DNLTTLINAELLDIEND-KLLKEFREKI 189
Cdd:cd03192  77 DVLDYLLYLLPKDLLEKyPKLKALRERV 104

GST_N family, Class Pi 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 Pi GST is a homodimeric eukaryotic protein. The human GSTP1 is mainly found in erythrocytes, kidney, placenta and fetal liver. It is involved in stress responses and in cellular proliferation pathways as an inhibitor of JNK (c-Jun N-terminal kinase). Following oxidative stress, monomeric GSTP1 dissociates from JNK and dimerizes, losing its ability to bind JNK and causing an increase in JNK activity, thereby promoting apoptosis. GSTP1 is expressed in various tumors and is the predominant GST in a wide range of cancer cells. It has been implicated in the development of multidrug-resistant tumours.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17540934   4 YKLTYFNARGLAEISRQLFHMAGVEFEDERIN-EEKFSQLKPTFPSGQVPILCIDGAQFSQSTAIARYLARK 74
Cdd:cd03076   2 YTLTYFPVRGRAEAIRLLLADQGISWEEERVTyEEWQESLKPKMLFGQLPCFKDGDLTLVQSNAILRHLGRK 73

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540934    96 KDFIESFRKFviavLSGESEEILKNIREEVIKPAVKTYTAYLKAILEKSSSGYLVGNELTWADLVIADNLTTLINAELLD 175
Cdd:pfam14497   1 HDLHHPIASS----LYYEDEKKKAKRRKEFREERLPKFLGYFEKVLNKNGGGYLVGDKLTYADLALFQVLDGLLYPKAPD 76

                          90       100
                  ....*....|....*....|....*...
gi 17540934   176 IEND-KLLKEFREKIIETPKLKEWLAKR 202
Cdd:pfam14497  77 ALDKyPKLKALHERVAARPNIKAYLASR 104

GST_N family, Class Alpha 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 class Alpha subfamily is composed of eukaryotic GSTs which can form homodimer and heterodimers. There are at least six types of class Alpha GST subunits in rats, four of which have human counterparts, resulting in many possible isoenzymes with different activities, tissue distribution and substrate specificities. Human GSTA1-1 and GSTA2-2 show high GSH peroxidase activity. GSTA3-3 catalyzes the isomerization of intermediates in steroid hormone biosynthesis. GSTA4-4 preferentially catalyzes the GSH conjugation of alkenals.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17540934   5 KLTYFNARGLAEISRQLFHMAGVEFEDERINE-EKFSQLKP--TFPSGQVPILCIDGAQFSQSTAIARYLARKF 75
Cdd:cd03077   3 VLHYFNGRGRMESIRWLLAAAGVEFEEKFIESaEDLEKLKKdgSLMFQQVPMVEIDGMKLVQTRAILNYIAGKY 76

glutathione S-transferase

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540934   22 FHMAGVEFEDERINEEKFSQLKPTF----PSGQVPILCIDGAQFSQSTAIARYLARKFG-----FVGQTAEEELQADEVV 92
Cdd:PLN02473  21 FLEKGIEFEVIHVDLDKLEQKKPEHllrqPFGQVPAIEDGDLKLFESRAIARYYATKYAdqgtdLLGKTLEHRAIVDQWV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540934   93 DtfkdfIESFRKFVIAvlsgesEEILKNIreeVIKPA---------VKTYTAYLKAILE-----KSSSGYLVGNELTWAD 158
Cdd:PLN02473 101 E-----VENNYFYAVA------LPLVINL---VFKPRlgepcdvalVEELKVKFDKVLDvyenrLATNRYLGGDEFTLAD 166

                 .
gi 17540934  159 L 159
Cdd:PLN02473 167 L 167

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
                ....*....|....*....|....*....|....*....|....*....|....
gi 17540934  22 FHMAGVEFEDERINEEKFSQLKPTF----PSGQVPILCIDGAQFSQSTAIARYL 71
Cdd:cd03042  19 LNLKGLDYEYVPVNLLKGEQLSPAYralnPQGLVPTLVIDGLVLTQSLAIIEYL 72

C-terminal, alpha helical domain of Class Pi Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Pi 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 Pi GST is a homodimeric eukaryotic protein. The human GSTP1 is mainly found in erythrocytes, kidney, placenta and fetal liver. It is involved in stress responses and in cellular proliferation pathways as an inhibitor of JNK (c-Jun N-terminal kinase). Following oxidative stress, monomeric GSTP1 dissociates from JNK and dimerizes, losing its ability to bind JNK and causing an increase in JNK activity, thereby promoting apoptosis. GSTP1 is expressed in various tumors and is the predominant GST in a wide range of cancer cells. It has been implicated in the development of multidrug-resistant tumors.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540934 122 REEVIKpAVKTYTAYLKAILEKSSS-GYLVGNELTWADLVIADnltTLINAELLD---IENDKLLKEFREKIIETPKLKE 197
Cdd:cd03210  33 KDDYIK-DLPEQLKPFEKLLAKNNGkGFIVGDKISFADYNLFD---LLDIHLVLApgcLDAFPLLKAFVERLSARPKLKA 108

                ....*
gi 17540934 198 WLAKR 202
Cdd:cd03210 109 YLESD 113

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
                ....*....|....*....|....*....|....*....|....*....|.
gi 17540934  26 GVEFEDERINEEKFSQLKPTF----PSGQVPILCI-DGAQFSQSTAIARYL 71
Cdd:cd03051  23 GIDVPLVTVDLAAGEQRSPEFlaknPAGTVPVLELdDGTVITESVAICRYL 73

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
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17540934  25 AGVEFEDERINEEKFSQLKPTF----PSGQVPILCIDGAQFSQSTAIARYLARKFG 76
Cdd:cd03046  21 LGLPYELVLYDRGPGEQAPPEYlainPLGKVPVLVDGDLVLTESAAIILYLAEKYG 76

glutathione S-transferase

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540934   26 GVEFEDERINEEKFSQLKPTF----PSGQVPILCIDGAQFSQSTAIARYLARKF-----GFVGQTAEEELQADEVVDT-F 95
Cdd:PLN02395  24 GVEFETVPVDLMKGEHKQPEYlalqPFGVVPVIVDGDYKIFESRAIMRYYAEKYrsqgpDLLGKTIEERGQVEQWLDVeA 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540934   96 KDFIESFRKFVIAVLSGESEEILKNirEEVIKPAVKTYTAYLKAILEK-SSSGYLVGNELTWADLV---IADNLTTLINA 171
Cdd:PLN02395 104 TSYHPPLLNLTLHILFASKMGFPAD--EKVIKESEEKLAKVLDVYEARlSKSKYLAGDFVSLADLAhlpFTEYLVGPIGK 181

                        170       180       190
                 ....*....|....*....|....*....|..
gi 17540934  172 ELLdIENDKLLKEFREKIIETPKLKEWLAKRP 203
Cdd:PLN02395 182 AYL-IKDRKHVSAWWDDISSRPAWKEVLAKYS 212

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
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17540934  22 FHMAGVEFEDERINEEKFSQLKPTF----PSGQVPILCIDGAQFSQSTAIARYLARK 74
Cdd:cd03053  20 LEEKGVDYELVPVDLTKGEHKSPEHlarnPFGQIPALEDGDLKLFESRAITRYLAEK 76

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
                ....*....|....*....|....*....|....*....|....*....|...
gi 17540934  24 MAGVEFEDERINEEKFSqlkptfPSGQVPILCIDGAQFSQSTAIARYLARKFG 76
Cdd:cd03080  29 MAGIPYENKFGGLAKRS------PKGKLPFIELNGEKIADSELIIDHLEEKYG 75

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 17540934  24 MAGVEFEDERINEEKFSQLKPTF----PSGQVPILCIDGAQFSQSTAIARYLA 72
Cdd:cd03056  21 LLGIPYEWVEVDILKGETRTPEFlalnPNGEVPVLELDGRVLAESNAILVYLA 73

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 17540934   104 KFVIAVLSGESEEILKNIREEVIKPAVKTYTAYLKaileksSSGYLVGNELTWADLVIADnlTTLINAEL-LDIENDK-- 180
Cdd:pfam00043   9 ALLPYVPPEEKKEPEVDEALEKVARVLSALEEVLK------GQTYLVGDKLTLADIALAP--ALLWLYELdPACLREKfp 80

                          90
                  ....*....|...
gi 17540934   181 LLKEFREKIIETP 193
Cdd:pfam00043  81 NLKAWFERVAARP 93