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 506941867    4 KLYSYFRSSAAYRVRIALNLKGLDYEYAAVHLLRDGgQQLKPEYRALNPDGIVPTLVDGDDVLTQSLAIIEYLEETHPEP 83
Cdd:TIGR01262   1 KLYSYWRSSCSYRVRIALALKGIDYEYVPVNLLRDG-EQRSPEFLALNPQGLVPTLDIDGEVLTQSLAIIEYLEETYPDP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506941867   84 PLLPKNPSDRAFVRAVAMQVACEIHPLDNLRVLKYLKHQVKVPDETKDAWYRHWVEAGFDSLEKRLASdkRVGALTFGDT 163
Cdd:TIGR01262  80 PLLPADPIKRARVRALALLIACDIHPLNNLRVLQYLREKLGVEEEARNRWYQHWISKGFAALEALLQP--HAGRFCVGDT 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 506941867  164 PTVADLCIVPQVFNARRFGIDTSRFPTIERIADHACTIDAFARAAPGQQPDAE 216
Cdd:TIGR01262 158 PTLADLCLVPQVYNAERFGVDLTPYPTLRRIAAALAALPAFQRAHPENQPDTP 210

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 506941867    4 KLYSYFRSSAAYRVRIALNLKGLDYEYAAVHLLRDGgQQLKPEYRALNPDGIVPTLVDGDDVLTQSLAIIEYLEETHPEP 83
Cdd:TIGR01262   1 KLYSYWRSSCSYRVRIALALKGIDYEYVPVNLLRDG-EQRSPEFLALNPQGLVPTLDIDGEVLTQSLAIIEYLEETYPDP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506941867   84 PLLPKNPSDRAFVRAVAMQVACEIHPLDNLRVLKYLKHQVKVPDETKDAWYRHWVEAGFDSLEKRLASdkRVGALTFGDT 163
Cdd:TIGR01262  80 PLLPADPIKRARVRALALLIACDIHPLNNLRVLQYLREKLGVEEEARNRWYQHWISKGFAALEALLQP--HAGRFCVGDT 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 506941867  164 PTVADLCIVPQVFNARRFGIDTSRFPTIERIADHACTIDAFARAAPGQQPDAE 216
Cdd:TIGR01262 158 PTLADLCLVPQVYNAERFGVDLTPYPTLRRIAAALAALPAFQRAHPENQPDTP 210

C-terminal, alpha helical domain of Class Zeta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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 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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506941867  90 PSDRAFVRAVAMQVACEIHPLDNLRVLKYLKHQVKVPDETKDAWYRHWVEAGFDSLEKRLASDKrvGALTFGDTPTVADL 169
Cdd:cd03191    1 PKKRARVRAIALIIACDIHPLQNLRVLKYLTEKLGVSEEEKLAWAQHWIERGFQALEKLLASTA--GKYCVGDEPTLADI 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 506941867 170 CIVPQVFNARRFGIDTSRFPTIERIADHACTIDAFARAAPGQQ 212
Cdd:cd03191   79 CLVPQVYNARRFGVDLSPYPTIVRINEACLELPAFQAAHPENQ 121

glutathione transferase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506941867   2 NMKLYS--YFRSSAAYRVRIALNLKGLDYEYAAVHLlrDGGQQLKPEYRALNPDGIVPTLVDGDDVLTQSLAIIEYLEET 79
Cdd:PRK15113   5 AITLYSdaHFFSPYVMSAFVALQEKGLPFELKTVDL--DAGEHLQPTYQGYSLTRRVPTLQHDDFELSESSAIAEYLEER 82

                         90       100
                 ....*....|....*....|...
gi 506941867  80 HPEPP---LLPKNPSDRAFVRAV 99
Cdd:PRK15113  83 FAPPAwerIYPADLQARARARQI 105

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 506941867    4 KLYSYFRSSAAYRVRIALNLKGLDYEYAAVHLLRDGgQQLKPEYRALNPDGIVPTLVDGDDVLTQSLAIIEYLEETHPEP 83
Cdd:TIGR01262   1 KLYSYWRSSCSYRVRIALALKGIDYEYVPVNLLRDG-EQRSPEFLALNPQGLVPTLDIDGEVLTQSLAIIEYLEETYPDP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506941867   84 PLLPKNPSDRAFVRAVAMQVACEIHPLDNLRVLKYLKHQVKVPDETKDAWYRHWVEAGFDSLEKRLASdkRVGALTFGDT 163
Cdd:TIGR01262  80 PLLPADPIKRARVRALALLIACDIHPLNNLRVLQYLREKLGVEEEARNRWYQHWISKGFAALEALLQP--HAGRFCVGDT 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 506941867  164 PTVADLCIVPQVFNARRFGIDTSRFPTIERIADHACTIDAFARAAPGQQPDAE 216
Cdd:TIGR01262 158 PTLADLCLVPQVYNAERFGVDLTPYPTLRRIAAALAALPAFQRAHPENQPDTP 210

C-terminal, alpha helical domain of Class Zeta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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 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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506941867  90 PSDRAFVRAVAMQVACEIHPLDNLRVLKYLKHQVKVPDETKDAWYRHWVEAGFDSLEKRLASDKrvGALTFGDTPTVADL 169
Cdd:cd03191    1 PKKRARVRAIALIIACDIHPLQNLRVLKYLTEKLGVSEEEKLAWAQHWIERGFQALEKLLASTA--GKYCVGDEPTLADI 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 506941867 170 CIVPQVFNARRFGIDTSRFPTIERIADHACTIDAFARAAPGQQ 212
Cdd:cd03191   79 CLVPQVYNARRFGVDLSPYPTIVRINEACLELPAFQAAHPENQ 121

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 506941867   3 MKLYSYFRSSAAYRVRIALNLKGLDYEYAAVHLlrdgGQQLKPEYRALNPDGIVPTLVDGDDVLTQSLAIIEYLE 77
Cdd:cd00570    1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDL----GEGEQEEFLALNPLGKVPVLEDGGLVLTESLAILEYLA 71

Glutathione S-transferase, N-terminal domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506941867    5 LYSYFRSSAAYRVRIALNLKGLDYEYAAVHLlrdggQQLKPEYRALNPDGIVPTLVDGDDVLTQSLAIIEYLEETHPEPP 84
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPP-----GDHPPELLAKNPLGKVPVLEDDGGILCESLAIIDYLEELYPGPP 75

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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506941867   3 MKLYsYFRSSAAYRVRIALNLKGLDYEYAAVHLlrDGGQQLKPEYRALNPDGIVPTLVDGDD-VLTQSLAIIEYLEETHP 81
Cdd:cd03057    1 MKLY-YSPGACSLAPHIALEELGLPFELVRVDL--RTKTQKGADYLAINPKGQVPALVLDDGeVLTESAAILQYLADLHP 77

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 506941867    1 MNMKLYSYFRSSAAYRVRIALNLKGLDYEYaaVHLLRDGGQQLKPEYRALNPDGIVPTLVDGDDVLTQSLAIIEYLEE 78
Cdd:pfam02798   1 MVLTLYGIRGSPRAHRIRWLLAEKGVEYEI--VPLDFGAGPEKSPELLKLNPLGKVPALEDGGKKLTESRAILEYIAR 76

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 506941867   3 MKLYSYFRSSAAYRVRIALNLKGLDYEYAAVHLLrdGGQQLKPEYRALNPDGIVPTLV-DGDDVLTQSLAIIEYLE 77
Cdd:cd03051    1 MKLYDSPTAPNPRRVRIFLAEKGIDVPLVTVDLA--AGEQRSPEFLAKNPAGTVPVLElDDGTVITESVAICRYLE 74

GST_N family, Class Delta and Epsilon 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. 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 class Delta and Epsilon subfamily is made up primarily of insect GSTs, which play major roles in insecticide resistance by facilitating reductive dehydrochlorination of insecticides or conjugating them with GSH to produce water-soluble metabolites that are easily excreted. They are also implicated in protection against cellular damage by oxidative stress.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506941867   3 MKLYsYFRSSAAYR-VRIALNLKGLDYEYAAVHLLRdgGQQLKPEYRALNPDGIVPTLVDGDDVLTQSLAIIEYLEE 78
Cdd:cd03045    1 IDLY-YLPGSPPCRaVLLTAKALGLELNLKEVNLMK--GEHLKPEFLKLNPQHTVPTLVDNGFVLWESHAILIYLVE 74

stringent starvation protein A; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506941867   3 MKLYSYFRSSAAYRVRIALNLKGLDYEYAAVHLlrdggQQLKPEYRALNPDGIVPTLVDGDDVLTQSLAIIEYLEETHPE 82
Cdd:PRK09481  11 MTLFSGPTDIYSHQVRIVLAEKGVSVEIEQVEK-----DNLPQDLIDLNPYQSVPTLVDRELTLYESRIIMEYLDERFPH 85

                         90
                 ....*....|.
gi 506941867  83 PPLLPKNPSDR 93
Cdd:PRK09481  86 PPLMPVYPVAR 96

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 506941867   3 MKLYSYFRSSAAYRVRIALNLKGLDYEYAAVHLLRDGGQQLKpeyraLNP-DGIVPTLVDGDDVLTQSLAIIEYLEET 79
Cdd:cd03058    1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLA-----SNPvHKKIPVLLHNGKPICESLIIVEYIDEA 73

GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP)-associated protein required for the lytic development of phage P1 and for stationary phase-induced acid tolerance of E. coli. It is implicated in survival during nutrient starvation. SspA adopts the GST fold with an N-terminal TRX-fold domain and a C-terminal alpha helical domain, but it does not bind glutathione (GSH) and lacks GST activity. SspA is highly conserved among gram-negative bacteria. Related proteins found in Neisseria (called RegF), Francisella and Vibrio regulate the expression of virulence factors necessary for pathogenesis.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506941867   3 MKLYSYFRSSAAYRVRIALNLKGLDYEYAAVHLlrdggqQLKPEYRA-LNPDGIVPTLVDGDDVLTQSLAIIEYLEE 78
Cdd:cd03059    1 MTLYSGPDDVYSHRVRIVLAEKGVSVEIIDVDP------DNPPEDLAeLNPYGTVPTLVDRDLVLYESRIIMEYLDE 71

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 506941867  15 YRVRIALNLKGLDYEYAAVHLlrdggqqlkPEYRAL------NPDGIVPTLVDGDD-VLTQSLAIIEYLEETHP 81
Cdd:cd03038   20 WKTRLALNHKGLEYKTVPVEF---------PDIPPIlgeltsGGFYTVPVIVDGSGeVIGDSFAIAEYLEEAYP 84

GST_N family, unknown subfamily 1; composed of uncharacterized proteins, predominantly from bacteria, 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506941867  11 SSAAYRVRIALNLKGLDYEYAAVHLLRDGGQQlkpEYRALNPDGIVPTLVDGDDVLTQSLAIIEYL 76
Cdd:cd03043   10 SSWSLRPWLLLKAAGIPFEEILVPLYTPDTRA---RILEFSPTGKVPVLVDGGIVVWDSLAICEYL 72

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 506941867   4 KLYSYFRSSAAYRVRIALNLKGLDYEYAAVHLlrdGGQQLKPEYRALNPDGIVPTLVdGDD--VLTQSLAIIEYL 76
Cdd:cd03044    2 TLYTYPGNPRSLKILAAAKYNGLDVEIVDFQP---GKENKTPEFLKKFPLGKVPAFE-GADgfCLFESNAIAYYV 72

glutathione S-transferase

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506941867   1 MNMKLYSYFRSSAAYRVRIALNLKGLDYEyaAVHLLRDGGQQLKPEYRALNPDGIVPTLVDGDDVLTQSLAIIEYLEETH 80
Cdd:PLN02473   1 MVVKVYGQIKAANPQRVLLCFLEKGIEFE--VIHVDLDKLEQKKPEHLLRQPFGQVPAIEDGDLKLFESRAIARYYATKY 78

                         90
                 ....*....|....*...
gi 506941867  81 PE--PPLLPKNPSDRAFV 96
Cdd:PLN02473  79 ADqgTDLLGKTLEHRAIV 96

glutathione dehydrogenase (ascorbate)

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506941867  16 RVRIALNLKGLDYEYAAVHLLRdggqqlKPE-YRALNPDGIVPTL------VDGDDVLTQSLaiieylEETHPEPPLlpK 88
Cdd:PLN02817  78 RVLLTLEEKHLPYDMKLVDLTN------KPEwFLKISPEGKVPVVkldekwVADSDVITQAL------EEKYPDPPL--A 143

                 ....*...
gi 506941867  89 NPSDRAFV 96
Cdd:PLN02817 144 TPPEKASV 151

C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Delta and Epsilon 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. 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 class Delta and Epsilon subfamily is made up primarily of insect GSTs, which play major roles in insecticide resistance by facilitating reductive dehydrochlorination of insecticides or conjugating them with GSH to produce water-soluble metabolites that are easily excreted. They are also implicated in protection against cellular damage by oxidative stress.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506941867 118 YLKHQVKVPDETKDAwyrhwVEAGFDSLEKRLASDKRVGaltfGDTPTVADLCIVPQVFNARRFGIDTSRFPTIER 193
Cdd:cd03177   28 ILFGGAEPPEEKLDK-----LEEALEFLETFLEGSDYVA----GDQLTIADLSLVATVSTLEVVGFDLSKYPNVAA 94

glutathione S-transferase DHAR1

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506941867  16 RVRIALNLKGLDYEyaaVHLLRDGGqqlKPE-YRALNPDGIVPTLVDGDDVLTQSLAIIEYLEETHPEPPLlpKNPSDRA 94
Cdd:PLN02378  25 RALLTLEEKSLTYK---IHLINLSD---KPQwFLDISPQGKVPVLKIDDKWVTDSDVIVGILEEKYPDPPL--KTPAEFA 96

                 ..
gi 506941867  95 FV 96
Cdd:PLN02378  97 SV 98

GST_N 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. 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.

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gi 506941867  57 PTLVDGDDVLTQSLAIIEYLEETH 80
Cdd:cd03075   59 PYYIDGDVKLTQSNAILRYIARKH 82