Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445852   3 LTVYGAPLSPFVRKVRLCLAEKDLEYSLEIILPFG---QPAWYRELNPLGRIPALQDGDFSLADSSVICQYLEDNYPERt 79
Cdd:COG0625     2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKgeqKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPEP- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445852  80 ALLGRNAEQRARVRWLEKYSDYELGPLctFGVFRNRVLkqsmgqPCDEAAVQRALTEKLPAHFDYLEQTLGSAEYFVGDS 159
Cdd:COG0625    81 PLLPADPAARARVRQWLAWADGDLHPA--LRNLLERLA------PEKDPAAIARARAELARLLAVLEARLAGGPYLAGDR 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1222445852 160 LTLADLAFACQLINMEHGDehLDAQRWPNLAALHRRVKARPSVQALLAGEQKVLA 214
Cdd:COG0625   153 FSIADIALAPVLRRLDRLG--LDLADYPNLAAWLARLAARPAFQRALAAAEPDLA 205

Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445852   3 LTVYGAPLSPFVRKVRLCLAEKDLEYSLEIILPFG---QPAWYRELNPLGRIPALQDGDFSLADSSVICQYLEDNYPERt 79
Cdd:COG0625     2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKgeqKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPEP- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445852  80 ALLGRNAEQRARVRWLEKYSDYELGPLctFGVFRNRVLkqsmgqPCDEAAVQRALTEKLPAHFDYLEQTLGSAEYFVGDS 159
Cdd:COG0625    81 PLLPADPAARARVRQWLAWADGDLHPA--LRNLLERLA------PEKDPAAIARARAELARLLAVLEARLAGGPYLAGDR 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1222445852 160 LTLADLAFACQLINMEHGDehLDAQRWPNLAALHRRVKARPSVQALLAGEQKVLA 214
Cdd:COG0625   153 FSIADIALAPVLRRLDRLG--LDLADYPNLAAWLARLAARPAFQRALAAAEPDLA 205

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 1222445852   3 LTVYGAPLSPFVRKVRLCLAEKDLEYSLEII-LPFGQPAWYRELNPLGRIPALQDGDFSLADSSVICQYLE 72
Cdd:cd00570     1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVdLGEGEQEEFLALNPLGKVPVLEDGGLVLTESLAILEYLA 71

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 1222445852  16 KVRLCLAEKDLEYSLEII--LPFGQ---PAwYRELNPLGRIPALQDGDFSLADSSVICQYLEDNYPErTALLGRNAEQRA 90
Cdd:TIGR01262  13 RVRIALALKGIDYEYVPVnlLRDGEqrsPE-FLALNPQGLVPTLDIDGEVLTQSLAIIEYLEETYPD-PPLLPADPIKRA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445852  91 RVRWLEKYSDYELGPLCTFgvfrnRVLKQSMGQPCDEAAVQRALTEKL-PAHFDYLEQTLG--SAEYFVGDSLTLADLAF 167
Cdd:TIGR01262  91 RVRALALLIACDIHPLNNL-----RVLQYLREKLGVEEEARNRWYQHWiSKGFAALEALLQphAGRFCVGDTPTLADLCL 165

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1222445852 168 ACQLINMEHGdeHLDAQRWPNLAALHRRVKARPSVQA 204
Cdd:TIGR01262 166 VPQVYNAERF--GVDLTPYPTLRRIAAALAALPAFQR 200

Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445852   3 LTVYGAPLSPFVRKVRLCLAEKDLEYSLEIILPFG---QPAWYRELNPLGRIPALQDGDFSLADSSVICQYLEDNYPERt 79
Cdd:COG0625     2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKgeqKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPEP- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445852  80 ALLGRNAEQRARVRWLEKYSDYELGPLctFGVFRNRVLkqsmgqPCDEAAVQRALTEKLPAHFDYLEQTLGSAEYFVGDS 159
Cdd:COG0625    81 PLLPADPAARARVRQWLAWADGDLHPA--LRNLLERLA------PEKDPAAIARARAELARLLAVLEARLAGGPYLAGDR 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1222445852 160 LTLADLAFACQLINMEHGDehLDAQRWPNLAALHRRVKARPSVQALLAGEQKVLA 214
Cdd:COG0625   153 FSIADIALAPVLRRLDRLG--LDLADYPNLAAWLARLAARPAFQRALAAAEPDLA 205

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 1222445852   3 LTVYGAPLSPFVRKVRLCLAEKDLEYSLEII-LPFGQPAWYRELNPLGRIPALQDGDFSLADSSVICQYLE 72
Cdd:cd00570     1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVdLGEGEQEEFLALNPLGKVPVLEDGGLVLTESLAILEYLA 71

glutathione S-transferase

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445852   1 MSLTVYGAPLSPFVRKVRLCLAEKDLEYslEIIL----PFGQPAWYREL-NPLGRIPALQDGDFSLADSSVICQYLEDNY 75
Cdd:PLN02473    1 MVVKVYGQIKAANPQRVLLCFLEKGIEF--EVIHvdldKLEQKKPEHLLrQPFGQVPAIEDGDLKLFESRAIARYYATKY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445852  76 PER-TALLGRNAEQRARV-RW--LEKYSDYELG-PLCTfgvfrNRVLKQSMGQPCDEAAVQRaLTEKLPAHFDYLEQTLG 150
Cdd:PLN02473   79 ADQgTDLLGKTLEHRAIVdQWveVENNYFYAVAlPLVI-----NLVFKPRLGEPCDVALVEE-LKVKFDKVLDVYENRLA 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1222445852 151 SAEYFVGDSLTLADLAfacqlinmehgdeHLDAQRW-PNLAALHRRVKARPS 201
Cdd:PLN02473  153 TNRYLGGDEFTLADLT-------------HMPGMRYiMNETSLSGLVTSREN 191

glutathione transferase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445852  10 LSPFVRKVRLCLAEKDLEYSLEII-LPFGQ--PAWYRELNPLGRIPALQDGDFSLADSSVICQYLEDNY--PERTALLGR 84
Cdd:PRK15113   15 FSPYVMSAFVALQEKGLPFELKTVdLDAGEhlQPTYQGYSLTRRVPTLQHDDFELSESSAIAEYLEERFapPAWERIYPA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445852  85 NAEQRARVR----WLEkySDyeLGPL----CTFGVFrnrvLKQSMGqPCDEAAvqRALTEKLpahFDYLEQTLGSAEYFV 156
Cdd:PRK15113   95 DLQARARARqiqaWLR--SD--LMPLreerPTDVVF----AGAKKA-PLSEAG--KAAAEKL---FAVAERLLAPGQPNL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1222445852 157 GDSLTLADLAFACQLINM-EHGDEHLdaqrwPNLAALHRRVKARPSVQALLAGEQKVLA 214
Cdd:PRK15113  161 FGEWCIADTDLALMLNRLvLHGDEVP-----ERLADYATFQWQRASVQRWLALSAKRSG 214

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222445852  11 SPFVRKVRLCLAEKDLEYSLEII--LPFGQPAWYRELNPLGRIPALQDGD-FSLADSSVICQYLED 73
Cdd:pfam13409   2 SPFSHRVRLALEEKGLPYEIELVdlDPKDKPPELLALNPLGTVPVLVLPDgTVLTDSLVILEYLEE 67

GST_N family, unknown subfamily 2; 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. The sequence from Burkholderia cepacia was identified as part of a gene cluster involved in the degradation of 2,4,5-trichlorophenoxyacetic acid. Some GSTs (e.g. Class Zeta and Delta) are known to catalyze dechlorination reactions.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1222445852   3 LTVYGAPLSPFVRKVRLCLAEKDLEYSLEII-LPFG--QPAWYRELNPLGRIPALQDGDFSLADSSVICQYL 71
Cdd:cd03047     1 LTIWGRRSSINVQKVLWLLDELGLPYERIDAgGQFGglDTPEFLAMNPNGRVPVLEDGDFVLWESNAILRYL 72

putative glutathione S-transferase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445852   7 GAPLSPFVRKVRLCLAEKDLEYSLEIILPFGQPAWYRELNPLGRIPAL--QDGDFSLaDSSVICQYLEdNYPERTALLGR 84
Cdd:PRK10357    5 GSYTSPFVRKISILLLEKGITFEFVNELPYNADNGVAQYNPLGKVPALvtEEGECWF-DSPIIAEYIE-LLNVAPAMLPR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445852  85 NAEQRARVRWLEKYSDyelgPLCTFGVFRNRVLKQSMGQPC-DEAAVQRaltEKLPAHFDYLEQTLGSAEyFVGDSLTLA 163
Cdd:PRK10357   83 DPLAALRVRQLEALAD----GIMDAALVSVREQARPAAQQSeDELLRQR---EKINRSLDALEGYLVDGT-LKTDTVNLA 154

                  ....*...
gi 1222445852 164 DLAFACQL 171
Cdd:PRK10357  155 TIAIACAV 162

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 1222445852  92 VRWLEKYSDYELGPLctfgvFRNRVLKQSMGQPCDEAAVQRALtEKLPAHFDYLEQTLGSAEYFVGDSLTLADLAFACQL 171
Cdd:cd00299     1 VRALEDWADATLAPP-----LVRLLYLEKVPLPKDEAAVEAAR-EELPALLAALEQLLAGRPYLAGDQFSLADVALAPVL 74

                          90       100
                  ....*....|....*....|....*.
gi 1222445852 172 INME-HGDEHLDAQRWPNLAALHRRV 196
Cdd:cd00299    75 ARLEaLGPYYDLLDEYPRLKAWYDRL 100

GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly uncharacterized proteins with similarity to the S. cerevisiae GST protein, GTT1, and the Schizosaccharomyces pombe GST-III. 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. GTT1, a homodimer, exhibits GST activity with standard substrates and associates with the endoplasmic reticulum. Its expression is induced after diauxic shift and remains high throughout the stationary phase. S. pombe GST-III is implicated in the detoxification of various metals.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222445852   3 LTVYGAPLSPFVRkVRLCLAEKDLEYSLEIIL---PFGQPAWYRELNPLGRIPALQDGDFSLADSSVICQYLEDNYP 76
Cdd:cd03046     1 ITLYHLPRSRSFR-ILWLLEELGLPYELVLYDrgpGEQAPPEYLAINPLGKVPVLVDGDLVLTESAAIILYLAEKYG 76

C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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. 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-like members include the class II insect GSTs, S-crystallins from cephalopods, nematode-specific GSTs, 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. Members also include novel GSTs from the fungus Cunninghamella elegans, designated as class Gamma, and from the protozoan Blepharisma japonicum, described as a light-inducible GST.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445852 112 FRNRVLKQSMGQPCDEAAVQRA--LTEKLPAHFDYLEQTLGS--AEYFVGDSLTLADLAFACQLINMEHGDEHLDAQRWP 187
Cdd:cd03192    16 LRAEFAPYFYEPDGEEKKEKKKefLEEALPKFLGKFEKILKKsgGGYFVGDKLTWADLALFDVLDYLLYLLPKDLLEKYP 95

                  ....*....
gi 1222445852 188 NLAALHRRV 196
Cdd:cd03192    96 KLKALRERV 104

glutathione dehydrogenase (ascorbate)

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445852  12 PFVRKVRLCLAEKDLEYSLEIILPFGQPAWYRELNPLGRIPALQDGDFSLADSSVICQYLEDNYPERTalLGRNAEQRAr 91
Cdd:PLN02817   74 PFCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISPEGKVPVVKLDEKWVADSDVITQALEEKYPDPP--LATPPEKAS- 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445852  92 vrwlekysdyeLGP--LCTFGVFrnrvLKQSmgQPCDeaAVQRALTEKLPAHFDYLEQtlgSAEYFVGDSLTLADLAFAC 169
Cdd:PLN02817  151 -----------VGSkiFSTFIGF----LKSK--DPGD--GTEQALLDELTSFDDYIKE---NGPFINGEKISAADLSLGP 208

                  ....*.
gi 1222445852 170 QLINME 175
Cdd:PLN02817  209 KLYHLE 214

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 1222445852   6 YGAPLSPFVRKVRLCLAEKDLEYSL-EIILPFGQ--PAWYRELNPLGRIPALQ--DGDFsLADSSVICQYLE 72
Cdd:cd03051     4 YDSPTAPNPRRVRIFLAEKGIDVPLvTVDLAAGEqrSPEFLAKNPAGTVPVLEldDGTV-ITESVAICRYLE 74

GST_N family, Beta etherase LigE subfamily; composed of proteins similar to Sphingomonas paucimobilis beta etherase, LigE, a GST-like protein that catalyzes the cleavage of the beta-aryl ether linkages present in low-moleculer weight lignins using GSH as the hydrogen donor. This reaction is an essential step in the degradation of lignin, a complex phenolic polymer that is the most abundant aromatic material in the biosphere. The beta etherase activity of LigE is enantioselective and it complements the activity of the other GST family beta etherase, LigF.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1222445852   9 PLSPFVRKVRLCLAEKDLEYSLEiilPFGQPAWYRELNPLG-----RIPALQDGD-FSLADSSVICQYLEDNYP 76
Cdd:cd03038    14 AFSPNVWKTRLALNHKGLEYKTV---PVEFPDIPPILGELTsggfyTVPVIVDGSgEVIGDSFAIAEYLEEAYP 84

GST_N 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1222445852   2 SLTVYGAPLSPFVRKVRLCLAEKDLEYSLEIILPFGQPAWYRELNPLGRIPALQ-DGDFSLADSSVICQYLE 72
Cdd:cd03055    18 IIRLYSMRFCPYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPQGKVPALEiDEGKVVYESLIICEYLD 89

C-terminal, alpha helical domain of Class Theta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial dichloromethane (DCM) dehalogenase. 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. Mammalian class Theta GSTs show poor GSH conjugating activity towards the standard substrates, CDNB and ethacrynic acid, differentiating them from other mammalian GSTs. GSTT1-1 shows similar cataytic activity as bacterial DCM dehalogenase, catalyzing the GSH-dependent hydrolytic dehalogenation of dihalomethanes. This is an essential process in methylotrophic bacteria to enable them to use chloromethane and DCM as sole carbon and energy sources. The presence of polymorphisms in human GSTT1-1 and its relationship to the onset of diseases including cancer is the subject of many studies. Human GSTT2-2 exhibits a highly specific sulfatase activity, catalyzing the cleavage of sulfate ions from aralkyl sufate esters, but not from the aryl or alkyl sulfate esters.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445852 108 TFGVFRNRVLKQSM-GQPCDEAAVQRALtEKLPAHFDYLEQT-LGSAEYFVGDSLTLADLAFACQLINMEHGDeHLDAQR 185
Cdd:cd03183    20 CAAYFWQKVLLPLFgGTPVSPEKVKKAE-ENLEESLDLLENKfLKDKPFLAGDEISIADLSAICEIMQPEAAG-YDVFEG 97

                          90
                  ....*....|....
gi 1222445852 186 WPNLAALHRRVKAR 199
Cdd:cd03183    98 RPKLAAWRKRVKEA 111

glutathione S-transferase DHAR1

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222445852  12 PFVRKVRLCLAEKDLEYSLEIILPFGQPAWYRELNPLGRIPALQDGDFSLADSSVICQYLEDNYPE 77
Cdd:PLN02378   21 PFSQRALLTLEEKSLTYKIHLINLSDKPQWFLDISPQGKVPVLKIDDKWVTDSDVIVGILEEKYPD 86

C-terminal, alpha helical domain of Ure2p and related Glutathione S-transferase-like proteins; Glutathione S-transferase (GST) C-terminal domain family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p, YfcG and YghU from Escherichia coli, and related GST-like proteins. 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 thioredoxin-fold domain and a C-terminal alpha helical domain. The N-terminal thioredoxin-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. YfcG and YghU are two of the nine GST homologs in the genome of Escherichia coli. They display very low or no GSH transferase, but show very good disulfide bond oxidoreductase activity. YghU also shows modest organic hydroperoxide reductase activity. 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. 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445852 126 DEAAVQRALTE--KLpahFDYLEQTLGSAEYFVGDSLTLADLAFACQLINMEHGDEHlDAQRWPNLAALHRRVKARPSVQ 203
Cdd:cd03178    34 IPYAIERYTDEvkRL---YGVLDKRLSDRPYLAGEEYSIADIALYPWTHYADLGGFA-DLSEYPNVKRWLERIAARPAVQ 109

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1222445852 126 DEAAVQRALtEKLPAHFDYLEQTLGSAEYFVGDSLTLADLAFACQLINMEHGDEHLDAQRWPNLAALHRRVKARP 200
Cdd:pfam00043  20 KEPEVDEAL-EKVARVLSALEEVLKGQTYLVGDKLTLADIALAPALLWLYELDPACLREKFPNLKAWFERVAARP 93

GST_N family, Class Beta 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. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit limited GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they also bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445852  21 LAEKDLEYSLEII-LPFGQP--AWYRELNPLGRIPALQDGDFS-LADSSVICQYLEDNYP 76
Cdd:cd03057    18 LEELGLPFELVRVdLRTKTQkgADYLAINPKGQVPALVLDDGEvLTESAAILQYLADLHP 77

Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1222445852 132 RALTEKLPAHFDYLEQTLGSAEYFVGDSLTLADLAFACQLINMEHGDEHLD-AQRWPNLAALHRR 195
Cdd:pfam13410   3 ERAREQLRAALDALEARLADGPGLLGDRPTLADIALAPVLARLDAAYPGLDlREGYPRLRAWLER 67

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 1222445852 122 GQPCDEAAVqraltEKLPAHFDYLEQTLGSAEYFVGDSLTLADLAFACQLINMEHGDehLDAQRWPNLAALHRRVKARP 200
Cdd:cd03177    32 GAEPPEEKL-----DKLEEALEFLETFLEGSDYVAGDQLTIADLSLVATVSTLEVVG--FDLSKYPNVAAWYERLKALP 103

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
                  ....*....|....*....|....*....|....*....|....
gi 1222445852  31 EIILPFGQPAWYRELN---PLGRIPALQDGDFSLADSSVICQYL 71
Cdd:cd03043    29 EILVPLYTPDTRARILefsPTGKVPVLVDGGIVVWDSLAICEYL 72

Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of Elongation Factor 1B and similar proteins; Glutathione S-transferase (GST) C-terminal domain family, Gamma subunit of Elongation Factor 1B (EF1Bgamma) 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 thioredoxin-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 to 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. Also included in this subfamily is the GST_C-like domain at the N-terminus of human valyl-tRNA synthetase (ValRS) and its homologs. Metazoan ValRS forms a stable complex with Elongation Factor-1H (EF-1H), and together, they catalyze consecutive steps in protein biosynthesis, tRNA aminoacylation and its transfer to EF.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1222445852 124 PCDEAAVQRALtEKLPAHFDYLEQTLGSAEYFVGDSLTLADLAFACQL 171
Cdd:cd03181    32 PYNKKAVDKAK-EDLKRALGVLEEHLLTRTYLVGERITLADIFVASAL 78

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 1222445852   3 LTVYGAPLSPFVRKVRLCLAEKDL---EYSLEIILPFGQPAWYRELNPLGRIPALQDGDFSLADSSVICQYLE 72
Cdd:cd03052     1 LVLYHWTQSFSSQKVRLVIAEKGLrceEYDVSLPLSEHNEPWFMRLNPTGEVPVLIHGDNIICDPTQIIDYLE 73

C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 8; composed of Agrobacterium tumefaciens GST and other 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 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 three-dimensional structure of Agrobacterium tumefaciens GST has been determined but there is no information on its functional characterization.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445852 114 NRVLKQSMGQPCDEAAVQRAlTEKLPAHFDYLEQTLGSAEYFVGDSLTLADLAFACQLINMEHGDEhLDAqrWPNLAALH 193
Cdd:cd03207    18 NKALGRFFEPPWGEPAIAAA-YGDLDERLAALEAALAGRPYLVGERFSAADLLLASVLRWARAFGL-LPE--YPALRAYV 93

                  ....*...
gi 1222445852 194 RRVKARPS 201
Cdd:cd03207    94 ARCTARPA 101