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 2484573965   2 QFFSFWRSLASFRVRVALNLKGVAADVVFVDLDAD-AHRTDAYRKINPQMALPALVtDDGTVLFQSLAIIDWLDETFPTP 80
Cdd:TIGR01262   1 KLYSYWRSSCSYRVRIALALKGIDYEYVPVNLLRDgEQRSPEFLALNPQGLVPTLD-IDGEVLTQSLAIIEYLEETYPDP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484573965  81 PLLPADALGRARVRGLALIVACEGHPLLTPRVRRYLDRELDLRDSQQNAWRRHWTVETLAALEGHLAGHkaTGRFCHGDA 160
Cdd:TIGR01262  80 PLLPADPIKRARVRALALLIACDIHPLNNLRVLQYLREKLGVEEEARNRWYQHWISKGFAALEALLQPH--AGRFCVGDT 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2484573965 161 PTLADICLVGHVTAAINQQISLSPWPTVKRIHETAMALPEFAKAHPSAQPDTP 213
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 2484573965   2 QFFSFWRSLASFRVRVALNLKGVAADVVFVDLDAD-AHRTDAYRKINPQMALPALVtDDGTVLFQSLAIIDWLDETFPTP 80
Cdd:TIGR01262   1 KLYSYWRSSCSYRVRIALALKGIDYEYVPVNLLRDgEQRSPEFLALNPQGLVPTLD-IDGEVLTQSLAIIEYLEETYPDP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484573965  81 PLLPADALGRARVRGLALIVACEGHPLLTPRVRRYLDRELDLRDSQQNAWRRHWTVETLAALEGHLAGHkaTGRFCHGDA 160
Cdd:TIGR01262  80 PLLPADPIKRARVRALALLIACDIHPLNNLRVLQYLREKLGVEEEARNRWYQHWISKGFAALEALLQPH--AGRFCVGDT 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2484573965 161 PTLADICLVGHVTAAINQQISLSPWPTVKRIHETAMALPEFAKAHPSAQPDTP 213
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 2484573965  90 RARVRGLALIVACEGHPLLTPRVRRYLDRELDLRDSQQNAWRRHWTVETLAALEGHLAGHkaTGRFCHGDAPTLADICLV 169
Cdd:cd03191     4 RARVRAIALIIACDIHPLQNLRVLKYLTEKLGVSEEEKLAWAQHWIERGFQALEKLLAST--AGKYCVGDEPTLADICLV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2484573965 170 GHVTAAINQQISLSPWPTVKRIHETAMALPEFAKAHPSAQ 209
Cdd:cd03191    82 PQVYNARRFGVDLSPYPTIVRINEACLELPAFQAAHPENQ 121

glutathione transferase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484573965   2 QFFSFWrslaSFRVRVALNLKGVAADVVFVDLDADAHRTDAYRKINPQMALPALVTDDGTvLFQSLAIIDWLDETFPTPP 81
Cdd:PRK15113   13 HFFSPY----VMSAFVALQEKGLPFELKTVDLDAGEHLQPTYQGYSLTRRVPTLQHDDFE-LSESSAIAEYLEERFAPPA 87

                          90
                  ....*....|....*.
gi 2484573965  82 ---LLPADALGRARVR 94
Cdd:PRK15113   88 werIYPADLQARARAR 103

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 2484573965   2 QFFSFWRSLASFRVRVALNLKGVAADVVFVDLDAD-AHRTDAYRKINPQMALPALVtDDGTVLFQSLAIIDWLDETFPTP 80
Cdd:TIGR01262   1 KLYSYWRSSCSYRVRIALALKGIDYEYVPVNLLRDgEQRSPEFLALNPQGLVPTLD-IDGEVLTQSLAIIEYLEETYPDP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484573965  81 PLLPADALGRARVRGLALIVACEGHPLLTPRVRRYLDRELDLRDSQQNAWRRHWTVETLAALEGHLAGHkaTGRFCHGDA 160
Cdd:TIGR01262  80 PLLPADPIKRARVRALALLIACDIHPLNNLRVLQYLREKLGVEEEARNRWYQHWISKGFAALEALLQPH--AGRFCVGDT 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2484573965 161 PTLADICLVGHVTAAINQQISLSPWPTVKRIHETAMALPEFAKAHPSAQPDTP 213
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 2484573965  90 RARVRGLALIVACEGHPLLTPRVRRYLDRELDLRDSQQNAWRRHWTVETLAALEGHLAGHkaTGRFCHGDAPTLADICLV 169
Cdd:cd03191     4 RARVRAIALIIACDIHPLQNLRVLKYLTEKLGVSEEEKLAWAQHWIERGFQALEKLLAST--AGKYCVGDEPTLADICLV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2484573965 170 GHVTAAINQQISLSPWPTVKRIHETAMALPEFAKAHPSAQ 209
Cdd:cd03191    82 PQVYNARRFGVDLSPYPTIVRINEACLELPAFQAAHPENQ 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 2484573965   1 MQFFSFWRSLASFRVRVALNLKGVAADVVFVDLDADAHrtDAYRKINPQMALPALVtDDGTVLFQSLAIIDWLD 74
Cdd:cd00570     1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQ--EEFLALNPLGKVPVLE-DGGLVLTESLAILEYLA 71

GST_N family, unknown subfamily 4; 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 2484573965   1 MQFFSFWRSLASFRVRVALNLKGVAADVVFVDLDADAHRTDAYRKINPQMALPALVtDDGTVLFQSLAIIDWL 73
Cdd:cd03056     1 MKLYGFPLSGNCYKVRLLLALLGIPYEWVEVDILKGETRTPEFLALNPNGEVPVLE-LDGRVLAESNAILVYL 72

Glutathione S-transferase, N-terminal domain;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2484573965  14 RVRVALNLKGVaaDVVFVDLDADAHRtDAYRKINPQMALPALVtDDGTVLFQSLAIIDWLDETFPTPP 81
Cdd:pfam13417  12 RVRIALNEKGL--PYEFVPIPPGDHP-PELLAKNPLGKVPVLE-DDGGILCESLAIIDYLEELYPGPP 75

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        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2484573965  12 SFRVRVALNLKGVAADVVFVDLDADAHRTDAYRKINPQMALPALVtDDGTVLFQSLAIIDWLDETFP 78
Cdd:cd03046    11 SFRILWLLEELGLPYELVLYDRGPGEQAPPEYLAINPLGKVPVLV-DGDLVLTESAAIILYLAEKYG 76

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 2484573965   4 FSFWRSLASFRVRVALNLKGVAADVVFVDLDADAHRTDAYRKINPQMALPALVtDDGTVLFQSLAIIDWLDE 75
Cdd:pfam02798   6 YGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGAGPEKSPELLKLNPLGKVPALE-DGGKKLTESRAILEYIAR 76

putative glutathione S-transferase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484573965  47 NPQMALPALVTDDGTVLFQSLAIIDWLDETFPTPPLLPADALGRARVRGL-ALIVACEGHPLLTPRVRRyldRELDLRDS 125
Cdd:PRK10357   44 NPLGKVPALVTEEGECWFDSPIIAEYIELLNVAPAMLPRDPLAALRVRQLeALADGIMDAALVSVREQA---RPAAQQSE 120

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2484573965 126 QQNAWRRHWTVETLAALEGHLAGHKatgrfCHGDAPTLADI---CLVGH 171
Cdd:PRK10357  121 DELLRQREKINRSLDALEGYLVDGT-----LKTDTVNLATIaiaCAVGY 164

GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related GSTs. 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The N-terminal TRX-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. Characterized GSTs in this subfamily include Aspergillus fumigatus GSTs 1 and 2, and Schizosaccharomyces pombe GST-I. 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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2484573965  13 FRVRVALNLKGVAADVVFVDLDADAHRTDAYRKINPQMALPALVTDDGT--VLFQSLAIIDWLDETFPT 79
Cdd:cd03048    13 FKVSIMLEELGLPYEIHPVDISKGEQKKPEFLKINPNGRIPAIVDHNGTplTVFESGAILLYLAEKYDK 81

GST_N family, Class Omega 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 Omega GSTs show little or no GSH-conjugating activity towards standard GST substrates. Instead, they catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins. They contain a conserved cysteine equivalent to the first cysteine in the CXXC motif of glutaredoxins, which is a redox active residue capable of reducing GSH mixed disulfides in a monothiol mechanism. Polymorphisms of the class Omega GST genes may be associated with the development of some types of cancer and the age-at-onset of both Alzheimer's and Parkinson's diseases.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2484573965  14 RVRVALNLKGVAADVVFVDLDadaHRTDAYRKINPQMALPALVTDDGTVLFQSLAIIDWLD 74
Cdd:cd03055    32 RARLVLAAKNIPHEVININLK---DKPDWFLEKNPQGKVPALEIDEGKVVYESLIICEYLD 89

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
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2484573965  12 SFRVRVALNLKGVAADVVFVDLdADAHRTDAYRKINPQMALPALVTDDGTVLFQSLAI 69
Cdd:cd03044    12 SLKILAAAKYNGLDVEIVDFQP-GKENKTPEFLKKFPLGKVPAFEGADGFCLFESNAI 68

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 2484573965   6 FWRSLASFRVRVALNLKGVAADVVFVDLDAdahRTDAYRKINP-QMALPALVTDDGTVLfQSLAIIDWLDETF 77
Cdd:cd03058     6 AWASPFVLRVRIALALKGVPYEYVEEDLGN---KSELLLASNPvHKKIPVLLHNGKPIC-ESLIIVEYIDEAW 74

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2484573965 137 ETLAALEGHLAGHKatgrFCHGDAPTLADICLVGHVTAAINQQISLSPWPTVKRIHETAMALPEFAKA 204
Cdd:cd03177    45 EALEFLETFLEGSD----YVAGDQLTIADLSLVATVSTLEVVGFDLSKYPNVAAWYERLKALPPGEEE 108

glutathione S-transferase

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484573965  14 RVRVALNLKGVAADVVFVDLDADAHRTDAYRKINPQMALPALVTDDGTvLFQSLAIIDWLDETFPT--PPLLPADALGRA 91
Cdd:PLN02395   15 RALVTLIEKGVEFETVPVDLMKGEHKQPEYLALQPFGVVPVIVDGDYK-IFESRAIMRYYAEKYRSqgPDLLGKTIEERG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484573965  92 RVRGLALIVACEGHP--------LLTPRVRRYLDRELDLRDSQQNawrrhwTVETLAALEGHLAGHKatgrFCHGDAPTL 163
Cdd:PLN02395   94 QVEQWLDVEATSYHPpllnltlhILFASKMGFPADEKVIKESEEK------LAKVLDVYEARLSKSK----YLAGDFVSL 163

                  ...
gi 2484573965 164 ADI 166
Cdd:PLN02395  164 ADL 166

C-terminal, alpha helical domain of an unknown subfamily 7 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 7; composed of uncharacterized 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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2484573965 139 LAALEGHLAGHkatgRFCHGDAPTLADICLVGHVTAAINQQISLSPWPTVKRIHETAMALPEF 201
Cdd:cd03206    42 LRLLDQHLAGR----DWLAGDRPTIADVACYPYIALAPEGGVSLEPYPAIRAWLARVEALPGF 100

GST_N family, Glutaredoxin 2 (GRX2) subfamily; composed of bacterial proteins similar to E. coli GRX2, an atypical GRX with a molecular mass of about 24kD, compared with other GRXs which are 9-12kD in size. GRX2 adopts a GST fold containing an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. It contains a redox active CXXC motif located in the N-terminal domain but is not able to reduce ribonucleotide reductase like other GRXs. However, it catalyzes GSH-dependent protein disulfide reduction of other substrates efficiently. GRX2 is thought to function primarily in catalyzing the reversible glutathionylation of proteins in cellular redox regulation including stress responses.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2484573965  14 RVRVALNLKGVAADVVFVDLDADAHRTdayRKINPQMaLPALVTDDGTVLFQSLAIIDWLDE 75
Cdd:cd03037    14 KARMIAGLKNIPVEQIILQNDDEATPI---RMIGAKQ-VPILEKDDGSFMAESLDIVAFIDE 71