GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit limited GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they also bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488995984   2 ITVYGVPGWGSTISELMLSLADIPYEVVDVEGFDQPGPARERLRqINPLCQVPTLRLADGSIMTETAAIALMILDQRP 79
Cdd:cd03057    1 MKLYYSPGACSLAPHIALEELGLPFELVRVDLRTKTQKGADYLA-INPKGQVPALVLDDGEVLTESAAILQYLADLHP 77

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488995984   17 LMLSLADIPYEVVDVEgfDQPGPARERLRQINPLCQVPTLRLADGSIMTETAAIALMILDQ 77
Cdd:pfam13409  10 LALEEKGLPYEIELVD--LDPKDKPPELLALNPLGTVPVLVLPDGTVLTDSLVILEYLEEL 68

GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit limited GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they also bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488995984   2 ITVYGVPGWGSTISELMLSLADIPYEVVDVEGFDQPGPARERLRqINPLCQVPTLRLADGSIMTETAAIALMILDQRP 79
Cdd:cd03057    1 MKLYYSPGACSLAPHIALEELGLPFELVRVDLRTKTQKGADYLA-INPKGQVPALVLDDGEVLTESAAILQYLADLHP 77

glutathionine S-transferase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488995984  47 INPLCQVPTLRLADGSIMTETAAIALMILDQRPD--LAPAPGTPQRQQFQRLLVWLVANVYPTFT---YADYPERWAPAA 121
Cdd:PRK10542  46 INPKGQVPALLLDDGTLLTEGVAIMQYLADSVPDrqLLAPVGSLSRYHTIEWLNYIATELHKGFTplfRPDTPEEYKPTV 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488995984 122 AEQLVencrqyRKNLYLwfEQQLAAGPWALGASVTLLDCYIAAMYSWGPRQAWFDDHAPKFAAIARAVCQRPELAVALRR 201
Cdd:PRK10542 126 RAQLE------KKFQYV--DEALADEQWICGQRFTIADAYLFTVLRWAYAVKLNLEGLEHIAAYMQRVAERPAVAAALKA 197

                 ....
gi 488995984 202 NKLI 205
Cdd:PRK10542 198 EGLK 201

Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. In addition, GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. This family, also referred to as soluble GSTs, is the largest family of GSH transferases and is only distantly related to the mitochondrial GSTs (GSTK subfamily, a member of the DsbA family). Soluble GSTs bear no structural similarity to microsomal GSTs (MAPEG family) and display additional activities unique to their group, such as catalyzing thiolysis, reduction and isomerization of certain compounds. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Based on sequence similarity, different classes of GSTs have been identified, which display varying tissue distribution, substrate specificities and additional specific activities. In humans, GSTs display polymorphisms which may influence individual susceptibility to diseases such as cancer, arthritis, allergy and sclerosis. Some GST family members with non-GST functions include glutaredoxin 2, the CLIC subfamily of anion channels, prion protein Ure2p, crystallins, metaxin 2 and stringent starvation protein A.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488995984   2 ITVYGVPGWG-STISELMLSLADIPYEVVDVEGFDQPgpaRERLRQINPLCQVPTLRLaDGSIMTETAAIA 71
Cdd:cd00570    1 LKLYYFPGSPrSLRVRLALEEKGLPYELVPVDLGEGE---QEEFLALNPLGKVPVLED-GGLVLTESLAIL 67

maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and phenylalanine catabolism. It requires glutathione and belongs by homology to the zeta family of glutathione S-transferases. The enzyme (EC 5.2.1.2) is described as active also on maleylpyruvate, and the example from a Ralstonia sp. catabolic plasmid is described as a maleylpyruvate isomerase involved in gentisate catabolism. [Energy metabolism, Amino acids and amines]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488995984   19 LSLADIPYEVVDVEGFDQPGPARERLRQINPLCQVPTLRLaDGSIMTETAAIaLMILD-QRPDLAPAPGTPQRQQFQRLL 97
Cdd:TIGR01262  18 LALKGIDYEYVPVNLLRDGEQRSPEFLALNPQGLVPTLDI-DGEVLTQSLAI-IEYLEeTYPDPPLLPADPIKRARVRAL 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488995984   98 VWLVA-NVYPTFTYA--DYPERWAPAAAEQLVENCRQYRKNLYLWFEQQLA--AGPWALGASVTLLDCYIA 163
Cdd:TIGR01262  96 ALLIAcDIHPLNNLRvlQYLREKLGVEEEARNRWYQHWISKGFAALEALLQphAGRFCVGDTPTLADLCLV 166

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
                 ....*....|....*....|....*....|....*....|....*....
gi 488995984  23 DIPYEVVDVEGFDQPGPArerLRQINPLCQVPTLRLADGSIMTETAAIA 71
Cdd:cd03051   25 DVPLVTVDLAAGEQRSPE---FLAKNPAGTVPVLELDDGTVITESVAIC 70

Glutathione S-transferase, N-terminal domain;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488995984   17 LMLSLADIPYEVVDVEGFDqpgpARERLRQINPLCQVPTLRLaDGSIMTETAAIALMILDQRPD 80
Cdd:pfam13417  15 IALNEKGLPYEFVPIPPGD----HPPELLAKNPLGKVPVLED-DGGILCESLAIIDYLEELYPG 73

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 488995984  99 WLVANVYPTFTYADYPERWAPAAAEQLVENCRQYRKNLYLWFEQQLAAGPWALGASVTLLDCYIAAMYSWGPR---QAWF 175
Cdd:cd00299    7 WADATLAPPLVRLLYLEKVPLPKDEAAVEAAREELPALLAALEQLLAGRPYLAGDQFSLADVALAPVLARLEAlgpYYDL 86

                         90
                 ....*....|....
gi 488995984 176 DDHAPKFAAIARAV 189
Cdd:cd00299   87 LDEYPRLKAWYDRL 100

GST_N family, unknown subfamily 3; 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 488995984  22 ADIPYEVVDVEGFDQPgparERLRQINPLCQVPTLRLADGSIMTETAAIA 71
Cdd:cd03049   24 LGDDVELVLVNPWSDD----ESLLAVNPLGKIPALVLDDGEALFDSRVIC 69

GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) 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 TRX-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 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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488995984   3 TVYGVPG-WGSTISELMLSLADIPYEVVDVE-GFDQPGPARERLrqiNPLCQVPTLRLADGSIMTETAAIALMILDQ 77
Cdd:cd03044    2 TLYTYPGnPRSLKILAAAKYNGLDVEIVDFQpGKENKTPEFLKK---FPLGKVPAFEGADGFCLFESNAIAYYVANL 75