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 460369073   12 QLYSYWRSSCAFRVRIALNLKGLDYEYKAVNLLK-GEQRDPEYLKLNPLGYVPTLVDGDAVIADSFAILMYLEEKYPQRA 90
Cdd:TIGR01262   1 KLYSYWRSSCSYRVRIALALKGIDYEYVPVNLLRdGEQRSPEFLALNPQGLVPTLDIDGEVLTQSLAIIEYLEETYPDPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460369073   91 LLPQDCQKRAINYQAANIVSANIQPLQNLAVLKYIQEKIG--PDETTPWVQGHITKGFEALEKLLKDYAGKYATGDEVYM 168
Cdd:TIGR01262  81 LLPADPIKRARVRALALLIACDIHPLNNLRVLQYLREKLGveEEARNRWYQHWISKGFAALEALLQPHAGRFCVGDTPTL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 460369073  169 ADLFLAPQIHAAIkRFEVDMNQFPTLLRVFEAYQELPAFQDAMPEKQPDAT 219
Cdd:TIGR01262 161 ADLCLVPQVYNAE-RFGVDLTPYPTLRRIAAALAALPAFQRAHPENQPDTP 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 460369073   12 QLYSYWRSSCAFRVRIALNLKGLDYEYKAVNLLK-GEQRDPEYLKLNPLGYVPTLVDGDAVIADSFAILMYLEEKYPQRA 90
Cdd:TIGR01262   1 KLYSYWRSSCSYRVRIALALKGIDYEYVPVNLLRdGEQRSPEFLALNPQGLVPTLDIDGEVLTQSLAIIEYLEETYPDPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460369073   91 LLPQDCQKRAINYQAANIVSANIQPLQNLAVLKYIQEKIG--PDETTPWVQGHITKGFEALEKLLKDYAGKYATGDEVYM 168
Cdd:TIGR01262  81 LLPADPIKRARVRALALLIACDIHPLNNLRVLQYLREKLGveEEARNRWYQHWISKGFAALEALLQPHAGRFCVGDTPTL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 460369073  169 ADLFLAPQIHAAIkRFEVDMNQFPTLLRVFEAYQELPAFQDAMPEKQPDAT 219
Cdd:TIGR01262 161 ADLCLVPQVYNAE-RFGVDLTPYPTLRRIAAALAALPAFQRAHPENQPDTP 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 460369073  97 QKRAINYQAANIVSANIQPLQNLAVLKYIQEKIG--PDETTPWVQGHITKGFEALEKLLKDYAGKYATGDEVYMADLFLA 174
Cdd:cd03191    2 KKRARVRAIALIIACDIHPLQNLRVLKYLTEKLGvsEEEKLAWAQHWIERGFQALEKLLASTAGKYCVGDEPTLADICLV 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 460369073 175 PQIHAAIkRFEVDMNQFPTLLRVFEAYQELPAFQDAMPEKQ 215
Cdd:cd03191   82 PQVYNAR-RFGVDLSPYPTIVRINEACLELPAFQAAHPENQ 121

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 460369073   11 LQLYSYWRSSCAFRVRIALNLKGLDYEYKAVNLLKGEQRDPEYLKLNPLGYVPTLVDGDAVIADSFAILMYLEE 84
Cdd:pfam02798   3 LTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGAGPEKSPELLKLNPLGKVPALEDGGKKLTESRAILEYIAR 76

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 460369073   12 QLYSYWRSSCAFRVRIALNLKGLDYEYKAVNLLK-GEQRDPEYLKLNPLGYVPTLVDGDAVIADSFAILMYLEEKYPQRA 90
Cdd:TIGR01262   1 KLYSYWRSSCSYRVRIALALKGIDYEYVPVNLLRdGEQRSPEFLALNPQGLVPTLDIDGEVLTQSLAIIEYLEETYPDPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460369073   91 LLPQDCQKRAINYQAANIVSANIQPLQNLAVLKYIQEKIG--PDETTPWVQGHITKGFEALEKLLKDYAGKYATGDEVYM 168
Cdd:TIGR01262  81 LLPADPIKRARVRALALLIACDIHPLNNLRVLQYLREKLGveEEARNRWYQHWISKGFAALEALLQPHAGRFCVGDTPTL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 460369073  169 ADLFLAPQIHAAIkRFEVDMNQFPTLLRVFEAYQELPAFQDAMPEKQPDAT 219
Cdd:TIGR01262 161 ADLCLVPQVYNAE-RFGVDLTPYPTLRRIAAALAALPAFQRAHPENQPDTP 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 460369073  97 QKRAINYQAANIVSANIQPLQNLAVLKYIQEKIG--PDETTPWVQGHITKGFEALEKLLKDYAGKYATGDEVYMADLFLA 174
Cdd:cd03191    2 KKRARVRAIALIIACDIHPLQNLRVLKYLTEKLGvsEEEKLAWAQHWIERGFQALEKLLASTAGKYCVGDEPTLADICLV 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 460369073 175 PQIHAAIkRFEVDMNQFPTLLRVFEAYQELPAFQDAMPEKQ 215
Cdd:cd03191   82 PQVYNAR-RFGVDLSPYPTIVRINEACLELPAFQAAHPENQ 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 460369073  11 LQLYSYWRSSCAFRVRIALNLKGLDYEYKAVNLLKGEQRdpEYLKLNPLGYVPTLVDGDAVIADSFAILMYLE 83
Cdd:cd00570    1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQE--EFLALNPLGKVPVLEDGGLVLTESLAILEYLA 71

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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460369073  11 LQLYSyWRSSCAFRVRIALNLKGLDYEYKAVNLLKGEQRDPEYLKLNPLGYVPTLVD---GDAVIADSFAILMYLEEKYP 87
Cdd:cd03048    2 ITLYT-HGTPNGFKVSIMLEELGLPYEIHPVDISKGEQKKPEFLKINPNGRIPAIVDhngTPLTVFESGAILLYLAEKYD 80

                 .
gi 460369073  88 Q 88
Cdd:cd03048   81 K 81

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 460369073  11 LQLYSYWRSSCAFRVRIALNLKGLDYEYKAVNLLKGEQRDPEYLKLNPLGYVPTLVDGDAVIADSFAILMYL 82
Cdd:cd03056    1 MKLYGFPLSGNCYKVRLLLALLGIPYEWVEVDILKGETRTPEFLALNPNGEVPVLELDGRVLAESNAILVYL 72

glutathione S-transferase

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460369073  20 SCAFRVRIALNLKGLDYEYKAVNLLKGEQRDPEYLKLNPLGYVPTLVDGDAVIADSFAILMYLEEKYPQRA--LLPQDCQ 97
Cdd:PLN02395  11 ASPKRALVTLIEKGVEFETVPVDLMKGEHKQPEYLALQPFGVVPVIVDGDYKIFESRAIMRYYAEKYRSQGpdLLGKTIE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460369073  98 KRAINYQAANIVSANIQP-LQNLAVLKYIQEKIG--PDETTpwvqghITKGFEALEKLLKDY-----AGKYATGDEVYMA 169
Cdd:PLN02395  91 ERGQVEQWLDVEATSYHPpLLNLTLHILFASKMGfpADEKV------IKESEEKLAKVLDVYearlsKSKYLAGDFVSLA 164

                 ..
gi 460369073 170 DL 171
Cdd:PLN02395 165 DL 166

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 460369073   11 LQLYSYWRSSCAFRVRIALNLKGLDYEYKAVNLLKGEQRDPEYLKLNPLGYVPTLVDGDAVIADSFAILMYLEE 84
Cdd:pfam02798   3 LTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGAGPEKSPELLKLNPLGKVPALEDGGKKLTESRAILEYIAR 76

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 460369073   19 SSCAFRVRIALNLKGLDYEYKAVNLlKGEQRDPEYLKLNPLGYVPTLVDGDA-VIADSFAILMYLEEK 85
Cdd:pfam13409   2 SPFSHRVRLALEEKGLPYEIELVDL-DPKDKPPELLALNPLGTVPVLVLPDGtVLTDSLVILEYLEEL 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 460369073  11 LQLYSYWRSSCAFRVRIALNLKGLDYEYKAVNLLKGEQRDPEYLKLNPLGYVPTLV-DGDAVIADSFAILMYLE 83
Cdd:cd03051    1 MKLYDSPTAPNPRRVRIFLAEKGIDVPLVTVDLAAGEQRSPEFLAKNPAGTVPVLElDDGTVITESVAICRYLE 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 460369073  11 LQLYSYWRSSCAFRVRIALNLKGLDYEYKAVNLlkgEQRDPEYLKLNPL-GYVPTLVDGDAVIADSFAILMYLEE 84
Cdd:cd03058    1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDL---GNKSELLLASNPVhKKIPVLLHNGKPICESLIIVEYIDE 72

GST_N family, Ganglioside-induced differentiation-associated protein 1 (GDAP1) subfamily; GDAP1 was originally identified as a highly expressed gene at the differentiated stage of GD3 synthase-transfected cells. More recently, mutations in GDAP1 have been reported to cause both axonal and demyelinating autosomal-recessive Charcot-Marie-Tooth (CMT) type 4A neuropathy. CMT is characterized by slow and progressive weakness and atrophy of muscles. Sequence analysis of GDAP1 shows similarities and differences with GSTs; it appears to contain both N-terminal TRX-fold and C-terminal alpha helical domains of GSTs, however, it also contains additional C-terminal transmembrane domains unlike GSTs. GDAP1 is mainly expressed in neuronal cells and is localized in the mitochondria through its transmembrane domains. It does not exhibit GST activity using standard substrates.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 460369073  11 LQLYSYWRSSCAFRVRIALNLKGLDYEYKAVNLLKGEQRDPEYLKLNPLGYVPTLVDGDAVIADSFAILMYLE 83
Cdd:cd03052    1 LVLYHWTQSFSSQKVRLVIAEKGLRCEEYDVSLPLSEHNEPWFMRLNPTGEVPVLIHGDNIICDPTQIIDYLE 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 460369073  24 RVRIALNLKGLDYEYKAVNLlkgeQRDPEYL-KLNPLGYVPTLVDGDAVIADSFAILMYLEEKY 86
Cdd:cd03059   14 RVRIVLAEKGVSVEIIDVDP----DNPPEDLaELNPYGTVPTLVDRDLVLYESRIIMEYLDERF 73

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 460369073  14 YSYWrsscAFRVRIALNLKGLDYEYKAVNLLKGEQRDpEYLKLNPLGYVPTLVDGDAVIADSFAILMYL 82
Cdd:cd03043    9 YSSW----SLRPWLLLKAAGIPFEEILVPLYTPDTRA-RILEFSPTGKVPVLVDGGIVVWDSLAICEYL 72

glutathione dehydrogenase (ascorbate)

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460369073  21 CAFRVRIALNL--KGLDYEYKAVNLlkgeQRDPE-YLKLNPLGYVPTLVDGDAVIADSFAILMYLEEKYPQRALlpqdcq 97
Cdd:PLN02817  73 CPFCQRVLLTLeeKHLPYDMKLVDL----TNKPEwFLKISPEGKVPVVKLDEKWVADSDVITQALEEKYPDPPL------ 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460369073  98 krAINYQAANiVSANIQPlqnlAVLKYIQEKIGPDETTPWVQGHITkgfeALEKLLKDyAGKYATGDEVYMADLFLAPQI 177
Cdd:PLN02817 143 --ATPPEKAS-VGSKIFS----TFIGFLKSKDPGDGTEQALLDELT----SFDDYIKE-NGPFINGEKISAADLSLGPKL 210

                 .
gi 460369073 178 H 178
Cdd:PLN02817 211 Y 211

glutathione S-transferase DHAR1

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460369073  21 CAFRVRIALNLKGLDYEYKaVNLLKGEQRDPEYLKLNPLGYVPTLVDGDAVIADSFAILMYLEEKYPQRALlpqdcqKRA 100
Cdd:PLN02378  20 CPFSQRALLTLEEKSLTYK-IHLINLSDKPQWFLDISPQGKVPVLKIDDKWVTDSDVIVGILEEKYPDPPL------KTP 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 460369073 101 INYQAaniVSANIQPlqnlAVLKYIQEKIGPDETtpwvQGHITKGFEALEKLLKDYAGKYATGDEVYMADLFLAPQIH 178
Cdd:PLN02378  93 AEFAS---VGSNIFG----TFGTFLKSKDSNDGS----EHALLVELEALENHLKSHDGPFIAGERVSAVDLSLAPKLY 159

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 460369073  25 VRIALNLKGL--DYEYKAVNLLKgeqRDPEYLKLNPLGYVPTLV-DGDAVIADSFAILMYLE 83
Cdd:cd03049   15 VRVAAHETGLgdDVELVLVNPWS---DDESLLAVNPLGKIPALVlDDGEALFDSRVICEYLD 73

putative S-transferase; Provisional

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 460369073  27 IALNLKGLDYEYKAVNLLKGEQRDPEYLKLNPLGYVPTLVD--GDAVIA--DSFAILMYLEEKYpqRALLPQDCQKRA 100
Cdd:PRK11752  66 LALGVKGAEYDAWLIRIGEGDQFSSGFVEINPNSKIPALLDrsGNPPIRvfESGAILLYLAEKF--GAFLPKDLAART 141

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.

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gi 460369073  11 LQLYSYWRSSCAFRVRIALNLKGLDYEYKAvNLLKGEQRDPEYLKLNPLGYVPTLVDGDA-VIADSFAILMYL 82
Cdd:cd03044    1 GTLYTYPGNPRSLKILAAAKYNGLDVEIVD-FQPGKENKTPEFLKKFPLGKVPAFEGADGfCLFESNAIAYYV 72

GST_N family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, including GSTs from class Mu, Pi and Alpha. 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. Vertebrate class Sigma GSTs are characterized as GSH-dependent hematopoietic prostaglandin (PG) D synthases and are responsible for the production of PGD2 by catalyzing the isomerization of PGH2. The functions of PGD2 include the maintenance of body temperature, inhibition of platelet aggregation, bronchoconstriction, vasodilation and mediation of allergy and inflammation. Other class Sigma members include the class II insect GSTs, S-crystallins from cephalopods and 28-kDa GSTs from parasitic flatworms. Drosophila GST2 is associated with indirect flight muscle and exhibits preference for catalyzing GSH conjugation to lipid peroxidation products, indicating an anti-oxidant role. S-crystallin constitutes the major lens protein in cephalopod eyes and is responsible for lens transparency and proper refractive index. The 28-kDa GST from Schistosoma is a multifunctional enzyme, exhibiting GSH transferase, GSH peroxidase and PGD2 synthase activities, and may play an important role in host-parasite interactions. Also members are novel GSTs from the fungus Cunninghamella elegans, designated as class Gamma, and from the protozoan Blepharisma japonicum, described as a light-inducible GST.

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                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 460369073  25 VRIALNLKGLDYEYKAVNllKGEQRDPEYLKLNPLGYVPTLVDGDAVIADSFAILMYL 82
Cdd:cd03039   15 IRLLLADAGVEYEDVRIT--YEEWPELDLKPTLPFGQLPVLEIDGKKLTQSNAILRYL 70

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.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 460369073 149 LEKLLKDyaGKYATGDEVYMADLFLAPQIhAAIKRFEVDMNQFPTLLRVFEAYQELPAFQ 208
Cdd:cd10291   52 LDRRLAK--SKYLAGDEYSIADIAIWPWV-ARHEWQGIDLADFPNLKRWFERLAARPAVQ 108

glutathione s-transferase; Provisional

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460369073  55 KLNPLGYVPTLVDGDAVIADSFAILMYLEEKYpqrallpQDCQKRAINYQAANIVSANIQPLQnlavLKYIQEKIGPDET 134
Cdd:PTZ00057  52 KDTPFEQVPILEMDNIIFAQSQAIVRYLSKKY-------KICGESELNEFYADMIFCGVQDIH----YKFNNTNLFKQNE 120

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460369073 135 TPWVQGHITKGFEALEKLLKDYAGKYATGDEVYMADLFLAPQIHAAIKRFEVDMNQFPTLLRVFEAYQELPAFQDAMPEK 214
Cdd:PTZ00057 121 TTFLNEELPKWSGYFENILKKNHCNYFVGDNLTYADLAVFNLYDDIETKYPNSLKNFPLLKAHNEFISNLPNIKNYISNR 200

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gi 460369073 215 Q 215
Cdd:PTZ00057 201 K 201