GST_N 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. 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 members include the class II insect GSTs, S-crystallins from cephalopods 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. Also members are 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 198419852   4 YKLCYFDLRGLGEMGRLIFAEAGVDYTDERIKKEDWPA--RKPGMPFGKMPVLFVDDVPIAHSRAMVRYLGR 73
Cdd:cd03039    1 YKLTYFNIRGRGEPIRLLLADAGVEYEDVRITYEEWPEldLKPTLPFGQLPVLEIDGKKLTQSNAILRYLAR 72

GST_N 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. 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 members include the class II insect GSTs, S-crystallins from cephalopods 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. Also members are 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 198419852   4 YKLCYFDLRGLGEMGRLIFAEAGVDYTDERIKKEDWPA--RKPGMPFGKMPVLFVDDVPIAHSRAMVRYLGR 73
Cdd:cd03039    1 YKLTYFNIRGRGEPIRLLLADAGVEYEDVRITYEEWPEldLKPTLPFGQLPVLEIDGKKLTQSNAILRYLAR 72

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198419852   4 YKLCYFDLRGLGEMGRLIFAEAGVDYTDERIKKEDWPARKPGM----PFGKMPVLFVDDVPIAHSRAMVRYLGRTF---N 76
Cdd:COG0625    2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFlalnPLGKVPVLVDDGLVLTESLAILEYLAERYpepP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198419852  77 LMGSNELEAAQIDMW-------IEVLFEAVMEYPFSEQDETKKAEKKETAWTdhffpKFTKLNEQIAKscGPYILGEKVS 149
Cdd:COG0625   82 LLPADPAARARVRQWlawadgdLHPALRNLLERLAPEKDPAAIARARAELAR-----LLAVLEARLAG--GPYLAGDRFS 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 198419852 150 VADIVVCAMIELLKTLydASKFESFGLISKLTDTVAARPNIAAWLKKRPQD 200
Cdd:COG0625  155 IADIALAPVLRRLDRL--GLDLADYPNLAAWLARLAARPAFQRALAAAEPD 203

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 198419852  84 EAAQIDMWIEVLFEAVMEYP--FSEQDETKKAEKKETAWTDHFFPKFTKLNEQIAKSCGPYILGEKVSVADIVVCAMIEL 161
Cdd:cd03192    2 EEARVDAIVDTIADLRAEFApyFYEPDGEEKKEKKKEFLEEALPKFLGKFEKILKKSGGGYFVGDKLTWADLALFDVLDY 81

                         90       100
                 ....*....|....*....|...
gi 198419852 162 LKTLYDASKFESFGLISKLTDTV 184
Cdd:cd03192   82 LLYLLPKDLLEKYPKLKALRERV 104

GST_N 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. 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 members include the class II insect GSTs, S-crystallins from cephalopods 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. Also members are 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 198419852   4 YKLCYFDLRGLGEMGRLIFAEAGVDYTDERIKKEDWPA--RKPGMPFGKMPVLFVDDVPIAHSRAMVRYLGR 73
Cdd:cd03039    1 YKLTYFNIRGRGEPIRLLLADAGVEYEDVRITYEEWPEldLKPTLPFGQLPVLEIDGKKLTQSNAILRYLAR 72

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 198419852   3 TYKLCYFDLRGLGEMGRLIFAEAGVDYTDERIKKEDWP-ARKPGMPFGKMPVLFVDDVPIAHSRAMVRYLGRT 74
Cdd:cd03076    1 PYTLTYFPVRGRAEAIRLLLADQGISWEEERVTYEEWQeSLKPKMLFGQLPCFKDGDLTLVQSNAILRHLGRK 73

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198419852   95 LFEAVMEYPFSEQDETKKAEKKEtaWTDHFFPKF-TKLNEQIAKSCGPYILGEKVSVADIVVCAMIELLKTLYDASKFES 173
Cdd:pfam14497   3 LHHPIASSLYYEDEKKKAKRRKE--FREERLPKFlGYFEKVLNKNGGGYLVGDKLTYADLALFQVLDGLLYPKAPDALDK 80

                          90       100
                  ....*....|....*....|....
gi 198419852  174 FGLISKLTDTVAARPNIAAWLKKR 197
Cdd:pfam14497  81 YPKLKALHERVAARPNIKAYLASR 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 198419852  84 EAAQIDMWIEVLFEAVMEYP--FSEQDETKKAEKKETAWTDHFFPKFTKLNEQIAKSCGPYILGEKVSVADIVVCAMIEL 161
Cdd:cd03192    2 EEARVDAIVDTIADLRAEFApyFYEPDGEEKKEKKKEFLEEALPKFLGKFEKILKKSGGGYFVGDKLTWADLALFDVLDY 81

                         90       100
                 ....*....|....*....|...
gi 198419852 162 LKTLYDASKFESFGLISKLTDTV 184
Cdd:cd03192   82 LLYLLPKDLLEKYPKLKALRERV 104

Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 2; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein (AIMP) 2 subfamily; AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex that functions as a molecular hub to coordinate protein synthesis. There are three AIMPs, named AIMP1-3, which play diverse regulatory roles. AIMP2, also called p38 or JTV-1, contains a C-terminal domain with similarity to the C-terminal alpha helical domain of GSTs. It plays an important role in the control of cell fate via antiproliferative (by enhancing the TGF-beta signal) and proapoptotic (activation of p53 and TNF-alpha) activities. Its roles in the control of cell proliferation and death suggest that it is a potent tumor suppressor. AIMP2 heterozygous mice with lower than normal expression of AIMP2 show high susceptibility to tumorigenesis. AIMP2 is also a substrate of Parkin, an E3 ubiquitin ligase that is involved in the ubiquitylation and proteasomal degradation of its substrates. Mutations in the Parkin gene is found in 50% of patients with autosomal-recessive early-onset parkinsonism. The accumulation of AIMP2, due to impaired Parkin function, may play a role in the pathogenesis of Parkinson's disease.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198419852  69 RYLGRTFNLMGSNELEAAQIDMWIEVLFEAVMEYPFSEQDETKKAekketawtdhffpkftkLNEQIAKScgPYILGEKV 148
Cdd:cd03200    2 RFLFRLLGDESDDPVNATLIDSWVDTAIFQLLEGSSKEKAAVLRA-----------------LNSALGRS--PWLVGSEP 62

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 198419852 149 SVADIVV-CAMIELlktlydaskfesfGLISkltdtvAARPNIAAWLK 195
Cdd:cd03200   63 TVADIALwSAVLQT-------------GLAS------GAPANVQRWMK 91

glutathione S-transferase

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198419852  47 PFGKMPVLFVDDVPIAHSRAMVRYLGRTF-----NLMGSNELEAAQIDMWIEV----------------LFEAVMEYPfS 105
Cdd:PLN02395  49 PFGVVPVIVDGDYKIFESRAIMRYYAEKYrsqgpDLLGKTIEERGQVEQWLDVeatsyhppllnltlhiLFASKMGFP-A 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 198419852 106 EQDETKKAEKKETAWTDHFfpkftklNEQIAKScgPYILGEKVSVADI 153
Cdd:PLN02395 128 DEKVIKESEEKLAKVLDVY-------EARLSKS--KYLAGDFVSLADL 166

glutathione S-transferase

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198419852  20 LIFAEAGVDYTDERIKKEDWPARKPG----MPFGKMPVLFVDDVPIAHSRAMVRYLGRTF-----NLMGSNELEAAQIDM 90
Cdd:PLN02473  19 LCFLEKGIEFEVIHVDLDKLEQKKPEhllrQPFGQVPAIEDGDLKLFESRAIARYYATKYadqgtDLLGKTLEHRAIVDQ 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198419852  91 WIEV---LFEA-----VMEYPFseqdETKKAEKKETAWTDHFFPKFTKL----NEQIAKScgPYILGEKVSVADIVVCAM 158
Cdd:PLN02473  99 WVEVennYFYAvalplVINLVF----KPRLGEPCDVALVEELKVKFDKVldvyENRLATN--RYLGGDEFTLADLTHMPG 172

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 198419852 159 IELLKTLYDASKF-ESFGLISKLTDTVAARPniaAWLK 195
Cdd:PLN02473 173 MRYIMNETSLSGLvTSRENLNRWWNEISARP---AWKK 207

Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of Elongation Factor 1B and similar proteins; Glutathione S-transferase (GST) C-terminal domain family, Gamma subunit of Elongation Factor 1B (EF1Bgamma) subfamily; EF1Bgamma is part of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. The EF1B gamma subunit contains a GST fold consisting of an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The GST-like domain of EF1Bgamma is believed to mediate the dimerization of the EF1 complex, which in yeast is a dimer of the heterotrimer EF1A:EF1Balpha:EF1Bgamma. In addition to its role in protein biosynthesis, EF1Bgamma may also display other functions. The recombinant rice protein has been shown to possess GSH conjugating activity. The yeast EF1Bgamma binds to membranes in a calcium dependent manner and is also part of a complex that binds to the msrA (methionine sulfoxide reductase) promoter suggesting a function in the regulation of its gene expression. Also included in this subfamily is the GST_C-like domain at the N-terminus of human valyl-tRNA synthetase (ValRS) and its homologs. Metazoan ValRS forms a stable complex with Elongation Factor-1H (EF-1H), and together, they catalyze consecutive steps in protein biosynthesis, tRNA aminoacylation and its transfer to EF.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198419852  84 EAAQIDMWI-----EVLFEAVMEY-------PFSEQdETKKAeKKETAWtdhffpKFTKLNEQIAKScgPYILGEKVSVA 151
Cdd:cd03181    1 EAAQVLQWIsfansELLPAAATWVlpllgiaPYNKK-AVDKA-KEDLKR------ALGVLEEHLLTR--TYLVGERITLA 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 198419852 152 DI-VVCAMIELLKTLYDASKFESFGLISKLTDTVAARPNIAAWLKK 196
Cdd:cd03181   71 DIfVASALLRGFETVLDPEFRKKYPNVTRWFNTVVNQPKFKAVFGE 116

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 198419852  24 EAGVDYtdeRIKKEDWPA---RKPGM----PFGKMPVLFVDDVPIAHSRAMVRYLGRTF 75
Cdd:cd03046   20 ELGLPY---ELVLYDRGPgeqAPPEYlainPLGKVPVLVDGDLVLTESAAIILYLAEKY 75

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 198419852   19 RLIFAEAGVDYTDERIKKEDW---PARKPGMPFGKMPVLFVDD-VPIAHSRAMVRYLGRT 74
Cdd:pfam13409   9 RLALEEKGLPYEIELVDLDPKdkpPELLALNPLGTVPVLVLPDgTVLTDSLVILEYLEEL 68

C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly uncharacterized proteins with similarity to the Saccharomyces 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 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. 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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198419852  83 LEAAQIDMW---IEV-LFEAVMEY-----PFSEQDEtkkaEKKETAW-------TDHFFPKFtklNEQIAKScgPYILGE 146
Cdd:cd03182    3 LEKALIEMWqrrAELqGLAPVFQAfrhatPGLKPDR----EVQVPEWgernkkrVIDFLPVL---DKRLAES--PYVAGD 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 198419852 147 KVSVADIVVCAMIELLKTLyDASKFESFGLISKLTDTVAARP 188
Cdd:cd03182   74 RFSIADITAFVALDFAKNL-KLPVPEELTALRRWYERMAARP 114

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 198419852  119 AWTDHFFPKFTKLNEQIAKscGPYILGEKVSVADIVVCAMIELLKTLYdaskfesfglisKLTDTVAARPNIAAWLK 195
Cdd:pfam13410   4 RAREQLRAALDALEARLAD--GPGLLGDRPTLADIALAPVLARLDAAY------------PGLDLREGYPRLRAWLE 66