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 11095990   7 VKLIGCSDDPFSIRPRVALHLKSIKYEYLEEpddDLGEKSQLLLKSNPIHKKTPVLIHGDLAICESLNIVQYLDEAW 83
Cdd:cd03058   1 VKLLGAWASPFVLRVRIALALKGVPYEYVEE---DLGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 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 11095990   7 VKLIGCSDDPFSIRPRVALHLKSIKYEYLEEpddDLGEKSQLLLKSNPIHKKTPVLIHGDLAICESLNIVQYLDEAW 83
Cdd:cd03058   1 VKLLGAWASPFVLRVRIALALKGVPYEYVEE---DLGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 74

Glutathione S-transferase, N-terminal domain;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11095990     9 LIGCSDDPFSIRPRVALHLKSIKYEYLEEPdddLGEKSQLLLKSNPiHKKTPVLIHGDLAICESLNIVQYLDEAWP 84
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIP---PGDHPPELLAKNP-LGKVPVLEDDGGILCESLAIIDYLEELYP 72

glutathione transferase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095990   23 VALHLKSIKYEyLEEPDDDLGEKSQLLLKSNPIHKKTPVLIHGDLAICESLNIVQYLDEAWPS--DPSILPSNAYDRASA 100
Cdd:PRK15113  24 VALQEKGLPFE-LKTVDLDAGEHLQPTYQGYSLTRRVPTLQHDDFELSESSAIAEYLEERFAPpaWERIYPADLQARARA 102

                 .
gi 11095990  101 R 101
Cdd:PRK15113 103 R 103

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 11095990   7 VKLIGCSDDPFSIRPRVALHLKSIKYEYLEEpddDLGEKSQLLLKSNPIHKKTPVLIHGDLAICESLNIVQYLDEAW 83
Cdd:cd03058   1 VKLLGAWASPFVLRVRIALALKGVPYEYVEE---DLGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 74

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 11095990   7 VKLIGCSDDPFSIRPRVALHLKSIKYEYLEEpddDLGEKSQLLLKSNPIHKKTPVLIHGDLAICESLNIVQYLD 80
Cdd:cd00570   1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPV---DLGEGEQEEFLALNPLGKVPVLEDGGLVLTESLAILEYLA 71

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 11095990     6 TVKLIGCSDDPFSIRPRVALHLKSIKYEYLEEPDDDLGEKSQLLLKSNPIhKKTPVLIHGDLAICESLNIVQYLDE 81
Cdd:pfam02798   2 VLTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGAGPEKSPELLKLNPL-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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11095990  18 SIRPRVALHLKSIKYEYLeePDDDL-GEKSQLLLKS-NPIhKKTPVLIHGDLAICESLNIVQYLD 80
Cdd:cd03042  12 SYRVRIALNLKGLDYEYV--PVNLLkGEQLSPAYRAlNPQ-GLVPTLVIDGLVLTQSLAIIEYLD 73

stringent starvation protein A; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11095990   13 SDDPFSIRPRVALHLKSIKYEYLEEPDDDLgekSQLLLKSNPiHKKTPVLIHGDLAICESLNIVQYLDEAWPSdPSILPS 92
Cdd:PRK09481  17 PTDIYSHQVRIVLAEKGVSVEIEQVEKDNL---PQDLIDLNP-YQSVPTLVDRELTLYESRIIMEYLDERFPH-PPLMPV 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 11095990   93 NAYDRASARFWAQYIDDKCFEAANALTGANNDEERiAATGKLTECLAILEETFQKSSkglgFFGGETIGYLDIACAALL 171
Cdd:PRK09481  92 YPVARGESRLMMHRIEKDWYSLMNKIVNGSASEAD-AARKQLREELLAIAPVFGEKP----YFMSEEFSLVDCYLAPLL 165

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 11095990  18 SIRPRVALHLKSIKYEYLEEPDDDLGEKSQLLLKSNPIhkKTPVLIHGDLAICESLNIVQYL 79
Cdd:cd03043  13 SLRPWLLLKAAGIPFEEILVPLYTPDTRARILEFSPTG--KVPVLVDGGIVVWDSLAICEYL 72

GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related fungal and bacterial 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. 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 Phi GST subfamily has experience extensive gene duplication. The Arabidopsis and Oryza genomes contain 13 and 16 Phi GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Tau GSTs, showing class specificity in substrate preference. Phi enzymes are highly reactive toward chloroacetanilide and thiocarbamate herbicides. Some Phi GSTs have other functions including transport of flavonoid pigments to the vacuole, shoot regeneration and GSH peroxidase activity.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11095990   6 TVKLIGCSDDPFSIRPRVALHLKSIKYEyLEEPDDDLGE-KSQLLLKSNPIhKKTPVLIHGDLAICESLNIVQYLDE 81
Cdd:cd03053   1 VLKLYGAAMSTCVRRVLLCLEEKGVDYE-LVPVDLTKGEhKSPEHLARNPF-GQIPALEDGDLKLFESRAITRYLAE 75

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 11095990  16 PFSIRPRVALHLKSIKYEYLEEPDDDLGEKSQLLLKsnpihKKTPVLIHGD-LAICESLNIVQYLDE 81
Cdd:cd03037  10 PFCVKARMIAGLKNIPVEQIILQNDDEATPIRMIGA-----KQVPILEKDDgSFMAESLDIVAFIDE 71