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 297826337   8 VKLIGSWASPFSRRVEMALKLKGVPYDYLDEDyLVVKSPLLLQLNPVYKKVPVLVHNGKILPESQLILEYIDQTW 82
Cdd:cd03058    1 VKLLGAWASPFVLRVRIALALKGVPYEYVEED-LGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 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 297826337   8 VKLIGSWASPFSRRVEMALKLKGVPYDYLDEDyLVVKSPLLLQLNPVYKKVPVLVHNGKILPESQLILEYIDQTW 82
Cdd:cd03058    1 VKLLGAWASPFVLRVRIALALKGVPYEYVEED-LGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 74

Glutathione S-transferase, N-terminal domain;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297826337   10 LIGSWASPFSRRVEMALKLKGVPYDYLDEDyLVVKSPLLLQLNPVYKkVPVLVHNGKILPESQLILEYIDQT 81
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIP-PGDHPPELLAKNPLGK-VPVLEDDGGILCESLAIIDYLEEL 70

stringent starvation protein A; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297826337  18 FSRRVEMALKLKGVPYDYLdedyLVVKSPL---LLQLNPvYKKVPVLVHNGKILPESQLILEYIDQTWTNNPILPQDPYE 94
Cdd:PRK09481  21 YSHQVRIVLAEKGVSVEIE----QVEKDNLpqdLIDLNP-YQSVPTLVDRELTLYESRIIMEYLDERFPHPPLMPVYPVA 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297826337  95 KAMARFWAKFVDEQVTLIGLRSLVKSEKRIDVAIEEVRELIMLLENQITEKKFFGGETIGFLD 157
Cdd:PRK09481  96 RGESRLMMHRIEKDWYSLMNKIVNGSASEADAARKQLREELLAIAPVFGEKPYFMSEEFSLVD 158

Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety of targets including S-crystallin from squid, the eukaryotic elongation factor 1-gamma, the HSP26 family of stress-related proteins and auxin-regulated proteins in plants. Stringent starvation proteins in E. coli are also included in the alignment but are not known to have GST activity. The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed to reside in the N-terminal domain. In plants, GSTs are encoded by a large gene family (48 GST genes in Arabidopsis) and can be divided into the phi, tau, theta, zeta, and lambda classes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297826337  119 KSEKRIDVAIEEVRELIMLLENQITEKKFFGGETIGFLDMVVgsmipFCLARGWEGMGIDmIPEEKFPELNRWIKNLKEI 198
Cdd:pfam00043  19 KKEPEVDEALEKVARVLSALEEVLKGQTYLVGDKLTLADIAL-----APALLWLYELDPA-CLREKFPNLKAWFERVAAR 92

                  .
gi 297826337  199 E 199
Cdd:pfam00043  93 P 93

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 297826337   8 VKLIGSWASPFSRRVEMALKLKGVPYDYLDEDyLVVKSPLLLQLNPVYKKVPVLVHNGKILPESQLILEYIDQTW 82
Cdd:cd03058    1 VKLLGAWASPFVLRVRIALALKGVPYEYVEED-LGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 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 297826337   8 VKLIGSWASPFSRRVEMALKLKGVPYDYLDEDYLVVKSPLLLQLNPvYKKVPVLVHNGKILPESQLILEYID 79
Cdd:cd00570    1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQEEFLALNP-LGKVPVLEDGGLVLTESLAILEYLA 71

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 297826337   15 ASPFSRRVEMALKLKGVPYDYLDEDYLVV-KSPLLLQLNPvYKKVPVLV-HNGKILPESQLILEYID 79
Cdd:pfam13409   1 FSPFSHRVRLALEEKGLPYEIELVDLDPKdKPPELLALNP-LGTVPVLVlPDGTVLTDSLVILEYLE 66

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 297826337   9 KLIGSWASPFSRRVEMALKLKGVPYDYLDEDyLVV---KSPLLLQLNPVyKKVPVLVHNGKILPESQLILEYID 79
Cdd:cd03042    2 ILYSYFRSSASYRVRIALNLKGLDYEYVPVN-LLKgeqLSPAYRALNPQ-GLVPTLVIDGLVLTQSLAIIEYLD 73

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 297826337   9 KLIGSWASPFSRRVEMALKLKGVPYDYLDEDYL--VVKSPLLLQLNPvYKKVPVLVHNGKILPESQLILEY 77
Cdd:cd03056    2 KLYGFPLSGNCYKVRLLLALLGIPYEWVEVDILkgETRTPEFLALNP-NGEVPVLELDGRVLAESNAILVY 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 297826337   9 KLIGSWASPFSRRVEMAL--KLKGVPYDYLDEDyLVVKSPLLLQLNPVyKKVPVLVHN-GKILPESQLILEYID 79
Cdd:cd03049    2 KLLYSPTSPYVRKVRVAAheTGLGDDVELVLVN-PWSDDESLLAVNPL-GKIPALVLDdGEALFDSRVICEYLD 73

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 297826337   8 VKLIGSWASPFSRRVEMALKLKGVPYDYLDEDYLVV--KSPLLLQLNPvYKKVPVLVHNGKILPESQLILEYID 79
Cdd:cd03053    2 LKLYGAAMSTCVRRVLLCLEEKGVDYELVPVDLTKGehKSPEHLARNP-FGQIPALEDGDLKLFESRAITRYLA 74

glutathione transferase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297826337  14 WASPFSRRVEMALKLKGVPYDYLDEDylvvkspllL----QLNPVY------KKVPVLVHNGKILPESQLILEYIDQTW- 82
Cdd:PRK15113  14 FFSPYVMSAFVALQEKGLPFELKTVD---------LdageHLQPTYqgysltRRVPTLQHDDFELSESSAIAEYLEERFa 84

                         90
                 ....*....|....*....
gi 297826337  83 --TNNPILPQDPYEKAMAR 99
Cdd:PRK15113  85 ppAWERIYPADLQARARAR 103

C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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 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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297826337 127 AIEEVRELIMLLENQITEK--KFFGGETIGFLDMvvgSMIPFCLARGWEGM-GIDMIPEEKFPELNRWIKNLKEIEIVKE 203
Cdd:cd03184   33 LKEELRSALENLEEELAKRgtPFFGGNSPGMVDY---MIWPWFERLEALKLlDGYELCLDRFPKLKKWMAAMKQDPAVKA 109

                         90
                 ....*....|..
gi 297826337 204 CIPDREKHIEHM 215
Cdd:cd03184  110 FYTDPETHAEFL 121

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        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297826337  13 SWASPFSRRVEMALKLKGVPYDY--LDEDYLVVKSPLLLQLNPvYKKVPVLV---HNGKILPESQLILEY 77
Cdd:cd03048    6 THGTPNGFKVSIMLEELGLPYEIhpVDISKGEQKKPEFLKINP-NGRIPAIVdhnGTPLTVFESGAILLY 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 297826337  15 ASPFSRRVEMALKLKGVPYDYLDEDYL--VVKSPLLLQLNPVyKKVPVLVHNGKILPESQLILEY 77
Cdd:cd03045    8 GSPPCRAVLLTAKALGLELNLKEVNLMkgEHLKPEFLKLNPQ-HTVPTLVDNGFVLWESHAILIY 71

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 297826337   9 KLIGSWASPFSRRVEMALKLKGVPYDYLDEDYLVV--KSPLLLQLNPvYKKVPVLV-HNGKILPESQLILEYID 79
Cdd:cd03051    2 KLYDSPTAPNPRRVRIFLAEKGIDVPLVTVDLAAGeqRSPEFLAKNP-AGTVPVLElDDGTVITESVAICRYLE 74

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

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297826337  17 PFSRRVEMALKLKGVPYD--YLDEDYlvVKSPLLLqlnpVYKK-VPVLVH-NGKILPESQLILEYIDQ 80
Cdd:COG2999   10 PFCVRARMIFGLKNIPVEliVLLNDD--EETPIRM----IGKKmVPILEKdDGSYMPESLDIVHYIDE 71

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        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297826337 123 RIDVAIE----EVRELIMLLENQITEKKFFGGETIGFLDMvvgSMIPFclARGWEGMGIDmipEEKFPELNRWIKNLKEI 198
Cdd:cd10291   33 KIPYAIKrytnETKRLYGVLDRRLAKSKYLAGDEYSIADI---AIWPW--VARHEWQGID---LADFPNLKRWFERLAAR 104

                 ....*
gi 297826337 199 EIVKE 203
Cdd:cd10291  105 PAVQK 109

GST_N family, Metaxin subfamily; composed of metaxins and related proteins. Metaxin 1 is a component of a preprotein import complex of the mitochondrial outer membrane. It extends to the cytosol and is anchored to the mitochondrial membrane through its C-terminal domain. In mice, metaxin is required for embryonic development. In humans, alterations in the metaxin gene may be associated with Gaucher disease. Metaxin 2 binds to metaxin 1 and may also play a role in protein translocation into the mitochondria. Genome sequencing shows that a third metaxin gene also exists in zebrafish, Xenopus, chicken and mammals. Sequence analysis suggests that all three metaxins share a common ancestry and that they possess similarity to GSTs. Also included in the subfamily are uncharacterized proteins with similarity to metaxins, including a novel GST from Rhodococcus with toluene o-monooxygenase and glutamylcysteine synthetase activities.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 297826337  15 ASPFSRRVEMALKLKGVPYDyldedyLVVKSPLLLQLNpvyKKVPVLVHNGKILPESQLILEYIDQT 81
Cdd:cd03054   15 LSPECLKVETYLRMAGIPYE------VVFSSNPWRSPT---GKLPFLELNGEKIADSEKIIEYLKKK 72

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 297826337  17 PFSRRVEMALKLKGVPYDYLDEDYLVVKSPLLLQlnpVYKKVPVLVHN-GKILPESQLILEYIDQ 80
Cdd:cd03037   10 PFCVKARMIAGLKNIPVEQIILQNDDEATPIRMI---GAKQVPILEKDdGSFMAESLDIVAFIDE 71