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 2507643307   9 LYSFFASSCCQRVIIAAHLKSIPLTFSFIDLSAK-QQLDDDYQRsLNPSRSVPTLVItskDGKktIIRQSLSILEYFEER 87
Cdd:TIGR01262   2 LYSYWRSSCSYRVRIALALKGIDYEYVPVNLLRDgEQRSPEFLA-LNPQGLVPTLDI---DGE--VLTQSLAIIEYLEET 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507643307  88 FPEPsPLLPprDKLEERARVRDFVNIITSDVAPPTNSRITQRVRD-IRDGRDDQHDFAKACFTDGFKAYEALLTETrema 166
Cdd:TIGR01262  76 YPDP-PLLP--ADPIKRARVRALALLIACDIHPLNNLRVLQYLREkLGVEEEARNRWYQHWISKGFAALEALLQPH---- 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2507643307 167 aSGGFTVGEAVTMADVCLVPTVDQAFMYKMDLAFVPKVQKLYESLKAMPAFQAADWRKQPDTP 229
Cdd:TIGR01262 149 -AGRFCVGDTPTLADLCLVPQVYNAERFGVDLTPYPTLRRIAAALAALPAFQRAHPENQPDTP 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 2507643307   9 LYSFFASSCCQRVIIAAHLKSIPLTFSFIDLSAK-QQLDDDYQRsLNPSRSVPTLVItskDGKktIIRQSLSILEYFEER 87
Cdd:TIGR01262   2 LYSYWRSSCSYRVRIALALKGIDYEYVPVNLLRDgEQRSPEFLA-LNPQGLVPTLDI---DGE--VLTQSLAIIEYLEET 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507643307  88 FPEPsPLLPprDKLEERARVRDFVNIITSDVAPPTNSRITQRVRD-IRDGRDDQHDFAKACFTDGFKAYEALLTETrema 166
Cdd:TIGR01262  76 YPDP-PLLP--ADPIKRARVRALALLIACDIHPLNNLRVLQYLREkLGVEEEARNRWYQHWISKGFAALEALLQPH---- 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2507643307 167 aSGGFTVGEAVTMADVCLVPTVDQAFMYKMDLAFVPKVQKLYESLKAMPAFQAADWRKQPDTP 229
Cdd:TIGR01262 149 -AGRFCVGDTPTLADLCLVPQVYNAERFGVDLTPYPTLRRIAAALAALPAFQRAHPENQPDTP 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 2507643307 103 ERARVRDFVNIITSDVAPPTNSRITQRVR-DIRDGRDDQHDFAKACFTDGFKAYEALLTETremaaSGGFTVGEAVTMAD 181
Cdd:cd03191     3 KRARVRAIALIIACDIHPLQNLRVLKYLTeKLGVSEEEKLAWAQHWIERGFQALEKLLAST-----AGKYCVGDEPTLAD 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2507643307 182 VCLVPTVDQAFMYKMDLAFVPKVQKLYESLKAMPAFQAADWRKQ 225
Cdd:cd03191    78 ICLVPQVYNARRFGVDLSPYPTIVRINEACLELPAFQAAHPENQ 121

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2507643307  14 ASSCCQRVIIAAHLKSIPLTFSFIDLSAKqQLDDDYqRSLNPSRSVPTLVItsKDGkkTIIRQSLSILEYFEER 87
Cdd:pfam13409   1 FSPFSHRVRLALEEKGLPYEIELVDLDPK-DKPPEL-LALNPLGTVPVLVL--PDG--TVLTDSLVILEYLEEL 68

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 2507643307   9 LYSFFASSCCQRVIIAAHLKSIPLTFSFIDLSAK-QQLDDDYQRsLNPSRSVPTLVItskDGKktIIRQSLSILEYFEER 87
Cdd:TIGR01262   2 LYSYWRSSCSYRVRIALALKGIDYEYVPVNLLRDgEQRSPEFLA-LNPQGLVPTLDI---DGE--VLTQSLAIIEYLEET 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507643307  88 FPEPsPLLPprDKLEERARVRDFVNIITSDVAPPTNSRITQRVRD-IRDGRDDQHDFAKACFTDGFKAYEALLTETrema 166
Cdd:TIGR01262  76 YPDP-PLLP--ADPIKRARVRALALLIACDIHPLNNLRVLQYLREkLGVEEEARNRWYQHWISKGFAALEALLQPH---- 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2507643307 167 aSGGFTVGEAVTMADVCLVPTVDQAFMYKMDLAFVPKVQKLYESLKAMPAFQAADWRKQPDTP 229
Cdd:TIGR01262 149 -AGRFCVGDTPTLADLCLVPQVYNAERFGVDLTPYPTLRRIAAALAALPAFQRAHPENQPDTP 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 2507643307 103 ERARVRDFVNIITSDVAPPTNSRITQRVR-DIRDGRDDQHDFAKACFTDGFKAYEALLTETremaaSGGFTVGEAVTMAD 181
Cdd:cd03191     3 KRARVRAIALIIACDIHPLQNLRVLKYLTeKLGVSEEEKLAWAQHWIERGFQALEKLLAST-----AGKYCVGDEPTLAD 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2507643307 182 VCLVPTVDQAFMYKMDLAFVPKVQKLYESLKAMPAFQAADWRKQ 225
Cdd:cd03191    78 ICLVPQVYNARRFGVDLSPYPTIVRINEACLELPAFQAAHPENQ 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 2507643307   9 LYSFFASSCCQRVIIAAHLKSIPLTFSFIDLSAKQQLDDdyqRSLNPSRSVPTLVItskDGkkTIIRQSLSILEYFE 85
Cdd:cd00570     3 LYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQEEF---LALNPLGKVPVLED---GG--LVLTESLAILEYLA 71

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2507643307  14 ASSCCQRVIIAAHLKSIPLTFSFIDLSAKqQLDDDYqRSLNPSRSVPTLVItsKDGkkTIIRQSLSILEYFEER 87
Cdd:pfam13409   1 FSPFSHRVRLALEEKGLPYEIELVDLDPK-DKPPEL-LALNPLGTVPVLVL--PDG--TVLTDSLVILEYLEEL 68

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 2507643307   9 LYSFFASSCCQRVIIAAHLKSIPLTFSFIDLSAKQQLDDDYqRSLNPSRSVPTLVItsKDGkkTIIRQSLSILEYFE 85
Cdd:cd03051     3 LYDSPTAPNPRRVRIFLAEKGIDVPLVTVDLAAGEQRSPEF-LAKNPAGTVPVLEL--DDG--TVITESVAICRYLE 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        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2507643307 153 KAYEAL---LTETRemaasggFTVGEAVTMADVCLVPTVDQAFMYKMDLAFVPKVQKLYESLKAMPAFQAADWR 223
Cdd:cd03177    45 EALEFLetfLEGSD-------YVAGDQLTIADLSLVATVSTLEVVGFDLSKYPNVAAWYERLKALPPGEEENGE 111

glutathione dehydrogenase (ascorbate)

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507643307  18 CQRVIIAAHLKSIPLTFSFIDLSAKQqlddDYQRSLNPSRSVPTLVITSKdgkktIIRQSLSILEYFEERFPEPSPLLPP 97
Cdd:PLN02817   76 CQRVLLTLEEKHLPYDMKLVDLTNKP----EWFLKISPEGKVPVVKLDEK-----WVADSDVITQALEEKYPDPPLATPP 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507643307  98 rdkleERARV-----RDFVNIITSdvapptnsritqrvRDIRDGRDDqhdfakaCFTDGFKAYEALLTEtremaaSGGFT 172
Cdd:PLN02817  147 -----EKASVgskifSTFIGFLKS--------------KDPGDGTEQ-------ALLDELTSFDDYIKE------NGPFI 194

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2507643307 173 VGEAVTMADVCLVPTvdqafMYKMDLAF-----------VPKVQKLYESLKAMPAF 217
Cdd:PLN02817  195 NGEKISAADLSLGPK-----LYHLEIALghyknwsvpdsLPFVKSYMKNIFSMESF 245

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507643307   9 LYSFFASSCCQRVIIAAHLKSIPLTFSFIDLSAKQQLdddyQRSLNP-SRSVPTLVITSKDgkktiIRQSLSILEYFEER 87
Cdd:cd03058     3 LLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSEL----LLASNPvHKKIPVLLHNGKP-----ICESLIIVEYIDEA 73

                  .
gi 2507643307  88 F 88
Cdd:cd03058    74 W 74

C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and related uncharacterized proteins; Glutathione S-transferase (GST) C-terminal domain family, YfcG-like subfamily; composed of the Escherichia coli YfcG and related proteins. 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 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. YfcG is one of nine GST homologs in Escherichia coli. It is expressed predominantly during the late stationary phase where the predominant form of GSH is glutathionylspermidine (GspSH), suggesting that YfcG might interact with GspSH. It has very low or no GSH transferase or peroxidase activity, but displays a unique disulfide bond reductase activity that is comparable to thioredoxins (TRXs) and glutaredoxins (GRXs). However, unlike TRXs and GRXs, YfcG does not contain a redox active cysteine residue and may use a bound thiol disulfide couple such as 2GSH/GSSG for activity. The crystal structure of YcfG reveals a bound GSSG molecule in its active site. The actual physiological substrates for YfcG are yet to be identified.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2507643307 167 ASGGFTVGEAVTMADVCLVPTVDQAFMYKMDLAFVPKVQKLYESLKAMPAFQAA 220
Cdd:cd10291    57 AKSKYLAGDEYSIADIAIWPWVARHEWQGIDLADFPNLKRWFERLAARPAVQKG 110