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 15222499  13 VKLLGAWPSPFVLRTRIALNLKNVAYEYLEEEDTLSSESVLNYNPVHKQIPILIHGNKPIRESLNIVMYVDETW 86
Cdd:cd03058   1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 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 15222499  13 VKLLGAWPSPFVLRTRIALNLKNVAYEYLEEEDTLSSESVLNYNPVHKQIPILIHGNKPIRESLNIVMYVDETW 86
Cdd:cd03058   1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 74

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 15222499    14 KLLGAWPSPFVLRTRIALNLKNVAYEY----LEEEDTLSSESVLNYNPVhKQIPILIHGNKPIRESLNIVMYVDETWlSG 89
Cdd:TIGR01262   1 KLYSYWRSSCSYRVRIALALKGIDYEYvpvnLLRDGEQRSPEFLALNPQ-GLVPTLDIDGEVLTQSLAIIEYLEETY-PD 78

                          90
                  ....*....|....*
gi 15222499    90 PPILPSDPFDRAVAR 104
Cdd:TIGR01262  79 PPLLPADPIKRARVR 93

putative glutathione S-transferase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222499   14 KLLGAWPSPFVLRTRIALNLKNVAYEYLEEEDTLSSESVLNYNPVHKqIPILIHG------NKPIreslnIVMYVDETWL 87
Cdd:PRK10357   2 KLIGSYTSPFVRKISILLLEKGITFEFVNELPYNADNGVAQYNPLGK-VPALVTEegecwfDSPI-----IAEYIELLNV 75

                         90
                 ....*....|
gi 15222499   88 SgPPILPSDP 97
Cdd:PRK10357  76 A-PAMLPRDP 84

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 15222499  13 VKLLGAWPSPFVLRTRIALNLKNVAYEYLEEEDTLSSESVLNYNPVHKQIPILIHGNKPIRESLNIVMYVDETW 86
Cdd:cd03058   1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 74

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 15222499    14 KLLGAWPSPFVLRTRIALNLKNVAYEY----LEEEDTLSSESVLNYNPVhKQIPILIHGNKPIRESLNIVMYVDETWlSG 89
Cdd:TIGR01262   1 KLYSYWRSSCSYRVRIALALKGIDYEYvpvnLLRDGEQRSPEFLALNPQ-GLVPTLDIDGEVLTQSLAIIEYLEETY-PD 78

                          90
                  ....*....|....*
gi 15222499    90 PPILPSDPFDRAVAR 104
Cdd:TIGR01262  79 PPLLPADPIKRARVR 93

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 15222499    13 VKLLGAWPSPFVLRTRIALNLKNVAYEYLEEEDTLS---SESVLNYNPVhKQIPILIHGNKPIRESLNIVMYVDE 84
Cdd:pfam02798   3 LTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGAGpekSPELLKLNPL-GKVPALEDGGKKLTESRAILEYIAR 76

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        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15222499  14 KLLGAWPSPFVLRTRIALNLKNVAYEY----LEEEDTLSSEsvlnY---NPVhKQIPILIHGNKPIRESLNIVMYVD 83
Cdd:cd03042   2 ILYSYFRSSASYRVRIALNLKGLDYEYvpvnLLKGEQLSPA----YralNPQ-GLVPTLVIDGLVLTQSLAIIEYLD 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 15222499 100 RAVARFWDVYIDEHCFTSINGVAVAKG--EENINAAIAKLEQCMALLEETFQecskGRGFFGGENIGFIDIGFGSMLGPL 177
Cdd:cd00299   2 RALEDWADATLAPPLVRLLYLEKVPLPkdEAAVEAAREELPALLAALEQLLA----GRPYLAGDQFSLADVALAPVLARL 77

                        90       100
                ....*....|....*....|....*.
gi 15222499 178 tvleKFTGVKFIHPENTPGLFHWADR 203
Cdd:cd00299  78 ----EALGPYYDLLDEYPRLKAWYDR 99

Glutaredoxin 2 [Posttranslational modification, protein turnover, chaperones];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222499  22 PFVLRTRIALNLKNVAYEyleeedtlssESVLNYNPVH--------KQIPILIHGN-KPIRESLNIVMYVDEtwLSGPPI 92
Cdd:COG2999  10 PFCVRARMIFGLKNIPVE----------LIVLLNDDEEtpirmigkKMVPILEKDDgSYMPESLDIVHYIDE--LDGKPI 77

                ....*
gi 15222499  93 LPSDP 97
Cdd:COG2999  78 LTGPV 82

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 15222499  22 PFVLRTRIALNLKNVAYE--YLEEEDTLSSESVLNYnpvhKQIPILIHGN-KPIRESLNIVMYVDE 84
Cdd:cd03037  10 PFCVKARMIAGLKNIPVEqiILQNDDEATPIRMIGA----KQVPILEKDDgSFMAESLDIVAFIDE 71

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 15222499  14 KLLGAWPSPFVLRTRIAL--NLKNVAYEYLEEEDTLSSESVLNYNPVHKqIPILI-HGNKPIRESLNIVMYVD 83
Cdd:cd03049   2 KLLYSPTSPYVRKVRVAAheTGLGDDVELVLVNPWSDDESLLAVNPLGK-IPALVlDDGEALFDSRVICEYLD 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
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15222499  22 PFVLRTRIALNLKNVAYEYLEEEDTLSSESVLNYNPVHkQIPILIHGNKPIRESlNIVM-YVDE 84
Cdd:cd03059  10 VYSHRVRIVLAEKGVSVEIIDVDPDNPPEDLAELNPYG-TVPTLVDRDLVLYES-RIIMeYLDE 71