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 1864409169  67 QREAAMVDVVNDGVEDLRCKYASLIYTNYEAGKADYVKALPRHLKPFETLLSQNqGGKTFIVGDQVSFADYNLLDLLLIH 146
Cdd:cd03210     1 EKEAALIDMVNDGVEDLRLKYVRMIYQNYEAGKDDYIKDLPEQLKPFEKLLAKN-NGKGFIVGDKISFADYNLFDLLDIH 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1864409169 147 QVLAPSCLDAFPLLSAYVERLCARPKLKAFLASPEHVNLPINGNGKQ 193
Cdd:cd03210    80 LVLAPGCLDAFPLLKAFVERLSARPKLKAYLESDAFKNRPINGNGKQ 126

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 1864409169  67 QREAAMVDVVNDGVEDLRCKYASLIYTNYEAGKADYVKALPRHLKPFETLLSQNqGGKTFIVGDQVSFADYNLLDLLLIH 146
Cdd:cd03210     1 EKEAALIDMVNDGVEDLRLKYVRMIYQNYEAGKDDYIKDLPEQLKPFEKLLAKN-NGKGFIVGDKISFADYNLFDLLDIH 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1864409169 147 QVLAPSCLDAFPLLSAYVERLCARPKLKAFLASPEHVNLPINGNGKQ 193
Cdd:cd03210    80 LVLAPGCLDAFPLLKAFVERLSARPKLKAYLESDAFKNRPINGNGKQ 126

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864409169  81 EDLRCKYASLIYTNYEAGKA----DYVK-ALPRHLKPFETLLSQNQGGktFIVGDQVSFADYNLLDLLL-IHQVLAPSCL 154
Cdd:pfam14497   1 HDLHHPIASSLYYEDEKKKAkrrkEFREeRLPKFLGYFEKVLNKNGGG--YLVGDKLTYADLALFQVLDgLLYPKAPDAL 78

                          90       100
                  ....*....|....*....|....*.
gi 1864409169 155 DAFPLLSAYVERLCARPKLKAFLASP 180
Cdd:pfam14497  79 DKYPKLKALHERVAARPNIKAYLASR 104

glutathione s-transferase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864409169  33 YGQLPKFQDGDLTLYQSNAILRHLGRTLGLYGKDQREAAMVDVVNDGVEDLRCKYASliyTN-YEAGKADYV-KALPRHL 110
Cdd:PTZ00057   56 FEQVPILEMDNIIFAQSQAIVRYLSKKYKICGESELNEFYADMIFCGVQDIHYKFNN---TNlFKQNETTFLnEELPKWS 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1864409169 111 KPFETLLSQNQggKTFIVGDQVSFADYNLLDLLLIHQVLAPSCLDAFPLLSAYVERLCARPKLKAFLAS 179
Cdd:PTZ00057  133 GYFENILKKNH--CNYFVGDNLTYADLAVFNLYDDIETKYPNSLKNFPLLKAHNEFISNLPNIKNYISN 199

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 1864409169  67 QREAAMVDVVNDGVEDLRCKYASLIYTNYEAGKADYVKALPRHLKPFETLLSQNqGGKTFIVGDQVSFADYNLLDLLLIH 146
Cdd:cd03210     1 EKEAALIDMVNDGVEDLRLKYVRMIYQNYEAGKDDYIKDLPEQLKPFEKLLAKN-NGKGFIVGDKISFADYNLFDLLDIH 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1864409169 147 QVLAPSCLDAFPLLSAYVERLCARPKLKAFLASPEHVNLPINGNGKQ 193
Cdd:cd03210    80 LVLAPGCLDAFPLLKAFVERLSARPKLKAYLESDAFKNRPINGNGKQ 126

C-terminal, alpha helical domain of Class Mu Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Mu 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 class Mu subfamily is composed of eukaryotic GSTs. In rats, at least six distinct class Mu subunits have been identified, with homologous genes in humans for five of these subunits. Class Mu GSTs can form homodimers and heterodimers, giving a large number of possible isoenzymes that can be formed, all with overlapping activities but different substrate specificities. They are the most abundant GSTs in human liver, skeletal muscle and brain, and are believed to provide protection against diseases including cancer and neurodegenerative disorders. Some isoenzymes have additional specific functions. Human GST M1-1 acts as an endogenous inhibitor of ASK1 (apoptosis signal-regulating kinase 1) thereby suppressing ASK1-mediated cell death. Human GSTM2-2 and 3-3 have been identified as prostaglandin E2 synthases in the brain and may play crucial roles in temperature and sleep-wake regulation.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864409169  68 REAAMVDVVNDGVEDLRCKYASLIYT-NYEAGKADYVKALPRHLKPFETLLsqnqGGKTFIVGDQVSFADYNLLDLLLIH 146
Cdd:cd03209     1 KERIRVDMLEQQAMDLRMGLIRICYSpDFEKLKPDYLEKLPDKLKLFSEFL----GDRPWFAGDKITYVDFLLYEALDQH 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1864409169 147 QVLAPSCLDAFPLLSAYVERLCARPKLKAFLASPEHVNLPING 189
Cdd:cd03209    77 RIFEPDCLDAFPNLKDFLERFEALPKISAYMKSDRFIKWPING 119

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
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1864409169   1 MRMLLADQGQSWKEEVVSMETWQQGSLKASCLYGQLPKFQDGDLTLYQSNAILRHLGR 58
Cdd:cd03039    15 IRLLLADAGVEYEDVRITYEEWPELDLKPTLPFGQLPVLEIDGKKLTQSNAILRYLAR 72

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 1864409169  80 VEDLRCKYASLIYTNYEAGKADYV-KALPRHLKPFETLLSQnQGGKTFIVGDQVSFADYNLLDLLLIHQVLAPSCL-DAF 157
Cdd:pfam00043   1 LMDLRMQIALLPYVPPEEKKEPEVdEALEKVARVLSALEEV-LKGQTYLVGDKLTLADIALAPALLWLYELDPACLrEKF 79

                          90
                  ....*....|....
gi 1864409169 158 PLLSAYVERLCARP 171
Cdd:pfam00043  80 PNLKAWFERVAARP 93

C-terminal, alpha helical domain of Class Alpha Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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 class Alpha subfamily is composed of vertebrate 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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864409169  67 QREAAMVDVVNDGVEDLRCKYASLIYTNYEAGKADYV----KALPRHLKPFETLLSQNqgGKTFIVGDQVSFADYNLLDL 142
Cdd:cd03208     1 LKERALIDMYVEGTADLMEMIMMLPFLPPEEKEAKLAlikeKAKNRYFPVFEKVLKDH--GQDFLVGNKLSRADVQLLEA 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1864409169 143 LLIHQVLAPSCLDAFPLLSAYVERLCARPKLKAFLA 178
Cdd:cd03208    79 ILMVEELDPSILSDFPLLQAFKTRISNIPTIKKFLQ 114

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
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1864409169   2 RMLLADQGQSWKEEVVSMETWQQGSLKASCLYGQLPKFQDGDLTLYQSNAILRHL 56
Cdd:cd00570    16 RLALEEKGLPYELVPVDLGEGEQEEFLALNPLGKVPVLEDGGLVLTESLAILEYL 70

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
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1864409169   2 RMLLADQGQSWKEEVVSMETWQQGS--LKASCLYGQLPKFQDGDLTLYQSNAILRHLGR 58
Cdd:pfam02798  18 RWLLAEKGVEYEIVPLDFGAGPEKSpeLLKLNPLGKVPALEDGGKKLTESRAILEYIAR 76

C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 8; composed of Agrobacterium tumefaciens GST and other 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. The three-dimensional structure of Agrobacterium tumefaciens GST has been determined but there is no information on its functional characterization.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1864409169 117 LSQNQGGKTFIVGDQVSFADYNLLDLLLIhqvlAPSC--LDAFPLLSAYVERLCARPK 172
Cdd:cd03207    48 LEAALAGRPYLVGERFSAADLLLASVLRW----ARAFglLPEYPALRAYVARCTARPA 101

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
                  ....*....|....*....|....
gi 1864409169  34 GQLPKFQDGDLTLYQSNAILRHLG 57
Cdd:cd03047    50 GRVPVLEDGDFVLWESNAILRYLA 73

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 1864409169  92 YTNYEAGKADYVKA-LPRHLKPFETLLSqnqgGKTFIVGDQVSFADYNLLDLLLI--HQVLAPSCLDAFPLLSAYVERLC 168
Cdd:cd03181    30 IAPYNKKAVDKAKEdLKRALGVLEEHLL----TRTYLVGERITLADIFVASALLRgfETVLDPEFRKKYPNVTRWFNTVV 105

                          90
                  ....*....|...
gi 1864409169 169 ARPKLKAFLASPE 181
Cdd:cd03181   106 NQPKFKAVFGEVK 118

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 1864409169 102 YVKALPRHLKPFETLLSQNQGGktFIVGDQVSFAD------YNLLDLLLIHQVLAPSclDAFPLLSAYVERLCARPKLKA 175
Cdd:cd10293    41 YTNEIRRVLGVLETALAERYRV--WLVGDKFTIADlafvpwNNVVDMIFIDPELDIK--KEFPHVYKWLKRMLARPAVKK 116