C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 6; composed of uncharacterized bacterial proteins with similarity to GSTs, including Pseudomonas fluorescens GST with a known three-dimensional structure. 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. Though the three-dimensional structure of Pseudomonas fluorescens GST has been determined, there is no information on its functional characterization.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275595495  91 TLRAIGLAMAALDKSIQIVYEHELRPEDKRHGPWVERVTGQLLAACAAMEADLGRRPLGattaTLDQAGVTTAVAWTFLQ 170
Cdd:cd03205     1 ALRLEALADGICDAAVLIVYERRLRPEEKQHQPWIERQWGKIERALDALEAELGDLPGG----RLTLGDIAVACALGYLD 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1275595495 171 AMVPDRVPAASHPRLVAFTAECEALPAFTAAP 202
Cdd:cd03205    77 FRFPELDWRAGHPALAAWFARFEARPSFQATP 108

C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 6; composed of uncharacterized bacterial proteins with similarity to GSTs, including Pseudomonas fluorescens GST with a known three-dimensional structure. 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. Though the three-dimensional structure of Pseudomonas fluorescens GST has been determined, there is no information on its functional characterization.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275595495  91 TLRAIGLAMAALDKSIQIVYEHELRPEDKRHGPWVERVTGQLLAACAAMEADLGRRPLGattaTLDQAGVTTAVAWTFLQ 170
Cdd:cd03205     1 ALRLEALADGICDAAVLIVYERRLRPEEKQHQPWIERQWGKIERALDALEAELGDLPGG----RLTLGDIAVACALGYLD 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1275595495 171 AMVPDRVPAASHPRLVAFTAECEALPAFTAAP 202
Cdd:cd03205    77 FRFPELDWRAGHPALAAWFARFEARPSFQATP 108

Glutathione S-transferase, N-terminal domain;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1275595495   3 LVGMLDSPYVRRVAVSLQLLGLPFEHRSVSVFRTFPQFQAINPVVKAPTLVcDDGEVLMDSTLILDYAEALAAGRR 78
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNPLGKVPVLE-DDGGILCESLAIIDYLEELYPGPP 75

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 1275595495   1 MQLVGMLDSPYVRRVAVSLQLLGLPFEHRSVSVFRTFP-QFQAINPVVKAPTLVcDDGEVLMDSTLILDYAE 71
Cdd:cd00570     1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQeEFLALNPLGKVPVLE-DGGLVLTESLAILEYLA 71

glutathionine S-transferase; Provisional

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1275595495  40 FQAINPVVKAPTLVCDDGEVLMDSTLILDYAEALAAGRRSLMPAALPARQHTL 92
Cdd:PRK10542   43 YLAINPKGQVPALLLDDGTLLTEGVAIMQYLADSVPDRQLLAPVGSLSRYHTI 95

C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 6; composed of uncharacterized bacterial proteins with similarity to GSTs, including Pseudomonas fluorescens GST with a known three-dimensional structure. 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. Though the three-dimensional structure of Pseudomonas fluorescens GST has been determined, there is no information on its functional characterization.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275595495  91 TLRAIGLAMAALDKSIQIVYEHELRPEDKRHGPWVERVTGQLLAACAAMEADLGRRPLGattaTLDQAGVTTAVAWTFLQ 170
Cdd:cd03205     1 ALRLEALADGICDAAVLIVYERRLRPEEKQHQPWIERQWGKIERALDALEAELGDLPGG----RLTLGDIAVACALGYLD 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1275595495 171 AMVPDRVPAASHPRLVAFTAECEALPAFTAAP 202
Cdd:cd03205    77 FRFPELDWRAGHPALAAWFARFEARPSFQATP 108

Glutathione S-transferase, N-terminal domain;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1275595495   3 LVGMLDSPYVRRVAVSLQLLGLPFEHRSVSVFRTFPQFQAINPVVKAPTLVcDDGEVLMDSTLILDYAEALAAGRR 78
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNPLGKVPVLE-DDGGILCESLAIIDYLEELYPGPP 75

putative glutathione S-transferase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275595495   1 MQLVGMLDSPYVRRVAVSLQLLGLPFEHRSVSVFRTFPQFQAINPVVKAPTLVCDDGEVLMDSTLILDYAEALAAGRRsL 80
Cdd:PRK10357    1 MKLIGSYTSPFVRKISILLLEKGITFEFVNELPYNADNGVAQYNPLGKVPALVTEEGECWFDSPIIAEYIELLNVAPA-M 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275595495  81 MP----AALPARQHTLRAIGLAMAALdksiqIVYEHELRPEDKRHGPWVERVTGQLLAACAAMEADLGRRPLGATTATLd 156
Cdd:PRK10357   80 LPrdplAALRVRQLEALADGIMDAAL-----VSVREQARPAAQQSEDELLRQREKINRSLDALEGYLVDGTLKTDTVNL- 153

                         170
                  ....*....|...
gi 1275595495 157 qAGVTTAVAWTFL 169
Cdd:PRK10357  154 -ATIAIACAVGYL 165

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 1275595495  14 RVAVSLQLLGLPFEHRSVSVFRTF----PQFQAINPVVKAPTLVcDDGEVLMDSTLILDYAEALAAGRRsLMPAALPARQ 89
Cdd:TIGR01262  13 RVRIALALKGIDYEYVPVNLLRDGeqrsPEFLALNPQGLVPTLD-IDGEVLTQSLAIIEYLEETYPDPP-LLPADPIKRA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275595495  90 HtLRAIGLAMAA-----LDKSIQIVYEHELRPEDKRHGPWVERVTGQLLAACAAMEAD-LGRRPLGATTATLDQAGV-TT 162
Cdd:TIGR01262  91 R-VRALALLIACdihplNNLRVLQYLREKLGVEEEARNRWYQHWISKGFAALEALLQPhAGRFCVGDTPTLADLCLVpQV 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1275595495 163 AVAWTFLQAMVPdrvpaasHPRLVAFTAECEALPAF-TAAPHG-PDT 207
Cdd:TIGR01262 170 YNAERFGVDLTP-------YPTLRRIAAALAALPAFqRAHPENqPDT 209

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        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1275595495   1 MQLVGMLDSPYVR--RVAVSLQLLGLPFE-HRSVSVFRTfPQFQAINPVVKAPTLVCDDGEVLMDSTLILDY 69
Cdd:cd03049     1 MKLLYSPTSPYVRkvRVAAHETGLGDDVElVLVNPWSDD-ESLLAVNPLGKIPALVLDDGEALFDSRVICEY 71

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        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1275595495  14 RVAVSLQLLGLPFEHRSVSVFR---TFPQFQAINPVVKAPTLVcDDGEVLMDSTLILDYAE 71
Cdd:cd03042    14 RVRIALNLKGLDYEYVPVNLLKgeqLSPAYRALNPQGLVPTLV-IDGLVLTQSLAIIEYLD 73

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 1275595495   1 MQLVGMLDSPYVRRVAVSLQLLGLPFEHRSVSV---FRTFPQFQAINPVVKAPTLVcDDGEVLMDSTLILDY 69
Cdd:pfam02798   3 LTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFgagPEKSPELLKLNPLGKVPALE-DGGKKLTESRAILEY 73

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        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1275595495   9 SPYVRRVAVSL--QLLGLPF--------EHRSvsvfrtfPQFQAINPVVKAPTLVCDDGEVLMDSTLILDYAE 71
Cdd:cd03051     9 APNPRRVRIFLaeKGIDVPLvtvdlaagEQRS-------PEFLAKNPAGTVPVLELDDGTVITESVAICRYLE 74

GST_N 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275595495   1 MQLVGMLDSPYVRRVAVSLQLLGLPFEHRSVSVFRTFPQFQAINPVV-KAPTLVcDDGEVLMDSTLILDY 69
Cdd:cd03058     1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHkKIPVLL-HNGKPICESLIIVEY 69

GST_N family, Beta etherase LigE subfamily; composed of proteins similar to Sphingomonas paucimobilis beta etherase, LigE, a GST-like protein that catalyzes the cleavage of the beta-aryl ether linkages present in low-moleculer weight lignins using GSH as the hydrogen donor. This reaction is an essential step in the degradation of lignin, a complex phenolic polymer that is the most abundant aromatic material in the biosphere. The beta etherase activity of LigE is enantioselective and it complements the activity of the other GST family beta etherase, LigF.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275595495   9 SPYVRRVAVSLQLLGLPFEhrsvSVFRTFPQFQAI------NPVVKAPTLVCDDGEVLMDSTLILDYAEA 72
Cdd:cd03038    16 SPNVWKTRLALNHKGLEYK----TVPVEFPDIPPIlgeltsGGFYTVPVIVDGSGEVIGDSFAIAEYLEE 81

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
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1275595495  19 LQLLGLPFEHRSVSvFRTFPQ----FQAINPVVKAPTLVCDDGEVLMDSTLILDY 69
Cdd:cd03057    18 LEELGLPFELVRVD-LRTKTQkgadYLAINPKGQVPALVLDDGEVLTESAAILQY 71