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Conserved domains on  [gi|28973477|gb|AAO64063|]
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putative glutathione transferase [Arabidopsis thaliana]

Protein Classification

glutathione S-transferase( domain architecture ID 10122769)

glutathione S-transferase (GST) catalyzes the conjugation of reduced glutathione to a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress; such as plant tau class GSTs that are primarily responsible for herbicide detoxification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GST_C_Tau cd03185
C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione ...
 89-209 8.31e-55

C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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 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.


:

Pssm-ID: 198294 [Multi-domain]  Cd Length: 127  Bit Score: 171.21  E-value: 8.31e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28973477  89 PYQRAQAKFWGDFIDKKVYASARLIWGAKGEEHEAGKKEFIEILKTLESELGD-KTYFGGETFGYVDIALIGFYSWFEAY 167
Cdd:cd03185   1 PYERAQARFWAAYIDDKLFPAGRKVWAAKGEEQEKAVEEALEALKVLEEELKGgKPFFGGDTIGYLDIALGSFLGWFKAI 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 28973477 168 EKFGSFSI--EAECPKLIAWGKRCVERESVAKSLPDSEKIIKFV 209
Cdd:cd03185  81 EEVGGVKLldEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFL 124
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 5-78 2.58e-43

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.


:

Pssm-ID: 239356 [Multi-domain]  Cd Length: 74  Bit Score: 140.11  E-value: 2.58e-43
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28973477   5 VILLDFWPSMFGMRTRIALEEKNVKFDYREQDLWNKSPILLEMNPVHKKIPVLIHNGNPVCESLIQIEYIDEVW 78
Cdd:cd03058   1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 74
 
Name Accession Description Interval E-value
GST_C_Tau cd03185
C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione ...
 89-209 8.31e-55

C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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 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.


Pssm-ID: 198294 [Multi-domain]  Cd Length: 127  Bit Score: 171.21  E-value: 8.31e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28973477  89 PYQRAQAKFWGDFIDKKVYASARLIWGAKGEEHEAGKKEFIEILKTLESELGD-KTYFGGETFGYVDIALIGFYSWFEAY 167
Cdd:cd03185   1 PYERAQARFWAAYIDDKLFPAGRKVWAAKGEEQEKAVEEALEALKVLEEELKGgKPFFGGDTIGYLDIALGSFLGWFKAI 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 28973477 168 EKFGSFSI--EAECPKLIAWGKRCVERESVAKSLPDSEKIIKFV 209
Cdd:cd03185  81 EEVGGVKLldEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFL 124
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 5-78 2.58e-43

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.


Pssm-ID: 239356 [Multi-domain]  Cd Length: 74  Bit Score: 140.11  E-value: 2.58e-43
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28973477   5 VILLDFWPSMFGMRTRIALEEKNVKFDYREQDLWNKSPILLEMNPVHKKIPVLIHNGNPVCESLIQIEYIDEVW 78
Cdd:cd03058   1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 74
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
6-206 2.48e-42

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 141.96  E-value: 2.48e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28973477   6 ILLDFWPSMFGMRTRIALEEKNVKFDYREQDLW---NKSPILLEMNPVHkKIPVLIHNGNPVCESLIQIEYIDEVWPsKT 82
Cdd:COG0625   3 KLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAkgeQKSPEFLALNPLG-KVPVLVDDGLVLTESLAILEYLAERYP-EP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28973477  83 PLLPSDPYQRAQAKFWGDFIDKKVYASARLIW-----GAKGEEHEAGKKEFIEILKTLESELGDKTYFGGETFGYVDIAL 157
Cdd:COG0625  81 PLLPADPAARARVRQWLAWADGDLHPALRNLLerlapEKDPAAIARARAELARLLAVLEARLAGGPYLAGDRFSIADIAL 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 28973477 158 IGFYSWFEAYEkfgsFSIeAECPKLIAWGKRCVERESVAKSLPDSEKII 206
Cdd:COG0625 161 APVLRRLDRLG----LDL-ADYPNLAAWLARLAARPAFQRALAAAEPDL 204
sspA PRK09481
stringent starvation protein A; Provisional
 14-210 1.97e-19

stringent starvation protein A; Provisional


Pssm-ID: 236537 [Multi-domain]  Cd Length: 211  Bit Score: 82.84  E-value: 1.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28973477   14 MFGMRTRIALEEKNVKFDYREQDLWNKSPILLEMNPvHKKIPVLIHNGNPVCESLIQIEYIDEVWPsKTPLLPSDPYQRA 93
Cdd:PRK09481  20 IYSHQVRIVLAEKGVSVEIEQVEKDNLPQDLIDLNP-YQSVPTLVDRELTLYESRIIMEYLDERFP-HPPLMPVYPVARG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28973477   94 QAKFWGDFIDKKVYASARLIWGAKGEEHEAGKKEFIEILKTLESELGDKTYFGGETFGYVDIALiGFYSWfeayeKFGSF 173
Cdd:PRK09481  98 ESRLMMHRIEKDWYSLMNKIVNGSASEADAARKQLREELLAIAPVFGEKPYFMSEEFSLVDCYL-APLLW-----RLPVL 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 28973477  174 SIEAECP---KLIAWGKRCVERESVAKSLPDSEKIIKFVP 210
Cdd:PRK09481 172 GIELSGPgakELKGYMTRVFERDSFLASLTEAEREMRLGR 211
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 5-76 3.07e-14

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.


Pssm-ID: 460698 [Multi-domain]  Cd Length: 76  Bit Score: 65.40  E-value: 3.07e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28973477     5 VILLDFWPSMFGMRTRIALEEKNVKFDYREQDLW---NKSPILLEMNPVhKKIPVLIHNGNPVCESLIQIEYIDE 76
Cdd:pfam02798   3 LTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGagpEKSPELLKLNPL-GKVPALEDGGKKLTESRAILEYIAR 76
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 122-185 4.81e-09

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 51.17  E-value: 4.81e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28973477   122 EAGKKEFIEILKTLESELGDKTYFGGETFGYVDIALIGFYSWFEAYekFGSFSIEAECPKLIAW 185
Cdd:pfam13410   3 ERAREQLRAALDALEARLADGPGLLGDRPTLADIALAPVLARLDAA--YPGLDLREGYPRLRAW 64
PRK15113 PRK15113
glutathione transferase;
1-96 1.02e-04

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 41.87  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28973477    1 MADEVILL----DFWpSMFGMRTRIALEEKNVKFDYREQDL---WNKSPILLEMNPVhKKIPVLIHNGNPVCESLIQIEY 73
Cdd:PRK15113   1 MSKPAITLysdaHFF-SPYVMSAFVALQEKGLPFELKTVDLdagEHLQPTYQGYSLT-RRVPTLQHDDFELSESSAIAEY 78

                         90       100
                 ....*....|....*....|....*
gi 28973477   74 IDEVWPSKT--PLLPSDPYQRAQAK 96
Cdd:PRK15113  79 LEERFAPPAweRIYPADLQARARAR 103
 
Name Accession Description Interval E-value
GST_C_Tau cd03185
C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione ...
 89-209 8.31e-55

C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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 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.


Pssm-ID: 198294 [Multi-domain]  Cd Length: 127  Bit Score: 171.21  E-value: 8.31e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28973477  89 PYQRAQAKFWGDFIDKKVYASARLIWGAKGEEHEAGKKEFIEILKTLESELGD-KTYFGGETFGYVDIALIGFYSWFEAY 167
Cdd:cd03185   1 PYERAQARFWAAYIDDKLFPAGRKVWAAKGEEQEKAVEEALEALKVLEEELKGgKPFFGGDTIGYLDIALGSFLGWFKAI 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 28973477 168 EKFGSFSI--EAECPKLIAWGKRCVERESVAKSLPDSEKIIKFV 209
Cdd:cd03185  81 EEVGGVKLldEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFL 124
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 5-78 2.58e-43

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.


Pssm-ID: 239356 [Multi-domain]  Cd Length: 74  Bit Score: 140.11  E-value: 2.58e-43
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28973477   5 VILLDFWPSMFGMRTRIALEEKNVKFDYREQDLWNKSPILLEMNPVHKKIPVLIHNGNPVCESLIQIEYIDEVW 78
Cdd:cd03058   1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 74
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
6-206 2.48e-42

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 141.96  E-value: 2.48e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28973477   6 ILLDFWPSMFGMRTRIALEEKNVKFDYREQDLW---NKSPILLEMNPVHkKIPVLIHNGNPVCESLIQIEYIDEVWPsKT 82
Cdd:COG0625   3 KLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAkgeQKSPEFLALNPLG-KVPVLVDDGLVLTESLAILEYLAERYP-EP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28973477  83 PLLPSDPYQRAQAKFWGDFIDKKVYASARLIW-----GAKGEEHEAGKKEFIEILKTLESELGDKTYFGGETFGYVDIAL 157
Cdd:COG0625  81 PLLPADPAARARVRQWLAWADGDLHPALRNLLerlapEKDPAAIARARAELARLLAVLEARLAGGPYLAGDRFSIADIAL 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 28973477 158 IGFYSWFEAYEkfgsFSIeAECPKLIAWGKRCVERESVAKSLPDSEKII 206
Cdd:COG0625 161 APVLRRLDRLG----LDL-ADYPNLAAWLARLAARPAFQRALAAAEPDL 204
sspA PRK09481
stringent starvation protein A; Provisional
 14-210 1.97e-19

stringent starvation protein A; Provisional


Pssm-ID: 236537 [Multi-domain]  Cd Length: 211  Bit Score: 82.84  E-value: 1.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28973477   14 MFGMRTRIALEEKNVKFDYREQDLWNKSPILLEMNPvHKKIPVLIHNGNPVCESLIQIEYIDEVWPsKTPLLPSDPYQRA 93
Cdd:PRK09481  20 IYSHQVRIVLAEKGVSVEIEQVEKDNLPQDLIDLNP-YQSVPTLVDRELTLYESRIIMEYLDERFP-HPPLMPVYPVARG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28973477   94 QAKFWGDFIDKKVYASARLIWGAKGEEHEAGKKEFIEILKTLESELGDKTYFGGETFGYVDIALiGFYSWfeayeKFGSF 173
Cdd:PRK09481  98 ESRLMMHRIEKDWYSLMNKIVNGSASEADAARKQLREELLAIAPVFGEKPYFMSEEFSLVDCYL-APLLW-----RLPVL 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 28973477  174 SIEAECP---KLIAWGKRCVERESVAKSLPDSEKIIKFVP 210
Cdd:PRK09481 172 GIELSGPgakELKGYMTRVFERDSFLASLTEAEREMRLGR 211
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 5-76 3.07e-14

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.


Pssm-ID: 460698 [Multi-domain]  Cd Length: 76  Bit Score: 65.40  E-value: 3.07e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28973477     5 VILLDFWPSMFGMRTRIALEEKNVKFDYREQDLW---NKSPILLEMNPVhKKIPVLIHNGNPVCESLIQIEYIDE 76
Cdd:pfam02798   3 LTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGagpEKSPELLKLNPL-GKVPALEDGGKKLTESRAILEYIAR 76
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 5-75 3.70e-13

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.


Pssm-ID: 238319 [Multi-domain]  Cd Length: 71  Bit Score: 62.20  E-value: 3.70e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28973477   5 VILLDFWPSMFGMRTRIALEEKNVKFDYREQDLWNKSP-ILLEMNPvHKKIPVLIHNGNPVCESLIQIEYID 75
Cdd:cd00570   1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQeEFLALNP-LGKVPVLEDGGLVLTESLAILEYLA 71
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 95-189 1.18e-11

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.


Pssm-ID: 198286 [Multi-domain]  Cd Length: 100  Bit Score: 59.05  E-value: 1.18e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28973477  95 AKFWGDFIDKKVYASARLI-------WGAKGEEHEAGKKEFIEILKTLESELGDKTYFGGETFGYVDIALIGFYSWFEAY 167
Cdd:cd00299   1 VRALEDWADATLAPPLVRLlylekvpLPKDEAAVEAAREELPALLAALEQLLAGRPYLAGDQFSLADVALAPVLARLEAL 80

                        90       100
                ....*....|....*....|..
gi 28973477 168 EKFgsFSIEAECPKLIAWGKRC 189
Cdd:cd00299  81 GPY--YDLLDEYPRLKAWYDRL 100
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
13-76 8.37e-11

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 56.08  E-value: 8.37e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28973477    13 SMFGMRTRIALEEKNVKFDYREQDLWNKSPILLEMNPVhKKIPVLIHNGNPVCESLIQIEYIDE 76
Cdd:pfam13417   7 SPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNPL-GKVPVLEDDGGILCESLAIIDYLEE 69
GST_N_Zeta cd03042
GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 6-75 9.99e-11

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.


Pssm-ID: 239340 [Multi-domain]  Cd Length: 73  Bit Score: 55.65  E-value: 9.99e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28973477   6 ILLDFWPSMFGMRTRIALEEKNVKFDYREQDLWN---KSPILLEMNPVhKKIPVLIHNGNPVCESLIQIEYID 75
Cdd:cd03042   2 ILYSYFRSSASYRVRIALNLKGLDYEYVPVNLLKgeqLSPAYRALNPQ-GLVPTLVIDGLVLTQSLAIIEYLD 73
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 15-76 2.33e-10

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 54.56  E-value: 2.33e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28973477    15 FGMRTRIALEEKNVKFDYREQDL--WNKSPILLEMNPVHkKIPVL-IHNGNPVCESLIQIEYIDE 76
Cdd:pfam13409   4 FSHRVRLALEEKGLPYEIELVDLdpKDKPPELLALNPLG-TVPVLvLPDGTVLTDSLVILEYLEE 67
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 122-185 4.81e-09

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 51.17  E-value: 4.81e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28973477   122 EAGKKEFIEILKTLESELGDKTYFGGETFGYVDIALIGFYSWFEAYekFGSFSIEAECPKLIAW 185
Cdd:pfam13410   3 ERAREQLRAALDALEARLADGPGLLGDRPTLADIALAPVLARLDAA--YPGLDLREGYPRLRAW 64
GST_N_SspA cd03059
GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ...
 14-76 1.07e-08

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.


Pssm-ID: 239357 [Multi-domain]  Cd Length: 73  Bit Score: 50.40  E-value: 1.07e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28973477  14 MFGMRTRIALEEKNVKFDYREQDLWNKSPILLEMNPVHkKIPVLIHNGNPVCESLIQIEYIDE 76
Cdd:cd03059  10 VYSHRVRIVLAEKGVSVEIIDVDPDNPPEDLAELNPYG-TVPTLVDRDLVLYESRIIMEYLDE 71
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 107-193 2.64e-06

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.


Pssm-ID: 459647 [Multi-domain]  Cd Length: 93  Bit Score: 44.20  E-value: 2.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28973477   107 YASARLIWGAKGEEHEA--GKKEFIEILKTLESELGDKTYFGGETFGYVDIALIGFYSWfeaYEKFGSFSIEAECPKLIA 184
Cdd:pfam00043   8 IALLPYVPPEEKKEPEVdeALEKVARVLSALEEVLKGQTYLVGDKLTLADIALAPALLW---LYELDPACLREKFPNLKA 84


                  ....*....
gi 28973477   185 WGKRCVERE 193
Cdd:pfam00043  85 WFERVAARP 93
GST_C_GTT2_like cd03182
C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione ...
 122-195 1.09e-05

C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly uncharacterized proteins with similarity to the Saccharomyces 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 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. GTT2, a homodimer, exhibits GST activity with standard substrates. Strains with deleted GTT2 genes are viable but exhibit increased sensitivity to heat shock.


Pssm-ID: 198291 [Multi-domain]  Cd Length: 116  Bit Score: 43.08  E-value: 1.09e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28973477 122 EAGKKEFIEILKTLESELGDKTYFGGETFGYVDIALIGFYSwfeaYEKFGSFSIEAECPKLIAWGKRCVERESV 195
Cdd:cd03182  47 ERNKKRVIDFLPVLDKRLAESPYVAGDRFSIADITAFVALD----FAKNLKLPVPEELTALRRWYERMAARPSA 116
GST_C_Beta cd03188
C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ...
 92-199 1.90e-05

C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they are involved in the protection against oxidative stress and are able to bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs, contributing to antibiotic resistance. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH. One member of this subfamily is a GST from Burkholderia xenovorans LB400 that is encoded by the bphK gene and is part of the biphenyl catabolic pathway.


Pssm-ID: 198297 [Multi-domain]  Cd Length: 113  Bit Score: 42.62  E-value: 1.90e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28973477  92 RAQAKFWGDFIDKKVYASAR-LIWGAK---GEEHEAGKKEFIEILKT----LESELGDKTYFGGETFGYVDIALIGFYSW 163
Cdd:cd03188   3 RARLLEWLNFIASELHKAFGpLFYPARwadDALAEEVKAAARERLERrlayLDAQLAGGPYLLGDQFSVADAYLFVVLRW 82

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 28973477 164 FEAYEKFgsfsiEAECPKLIAWGKRCVERESVAKSL 199
Cdd:cd03188  83 ARAVGLD-----LSDWPHLAAYLARVAARPAVQAAL 113
GST_N_Omega_like cd03060
GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to ...
 6-68 7.54e-05

GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to class Omega 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. 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. Like Omega enzymes, proteins in this subfamily 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.


Pssm-ID: 239358 [Multi-domain]  Cd Length: 71  Bit Score: 39.65  E-value: 7.54e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28973477   6 ILLDFWPSMFGMRTRIALEEKNVKFDYREQDLWNKSPILLEMNPvHKKIPVLIHNGNPVC-ESL 68
Cdd:cd03060   2 ILYSFRRCPYAMRARMALLLAGITVELREVELKNKPAEMLAASP-KGTVPVLVLGNGTVIeESL 64
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
 15-206 9.03e-05

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 42.29  E-value: 9.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28973477   15 FGMRTRIALEEKNVKFDYREQDLWNKSPILLEMNPvHKKIPVLIHNGNPVCESLIQIEYIDEVWPSktPLLPSDPYQRAq 94
Cdd:PLN02817  75 FCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISP-EGKVPVVKLDEKWVADSDVITQALEEKYPD--PPLATPPEKAS- 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28973477   95 akfwgdfIDKKVYASarLIWGAKGEEHEAGKKE-FIEILKTLESELGDKTYF-GGETFGYVDIALI-GFYSWFEAYEKFG 171
Cdd:PLN02817 151 -------VGSKIFST--FIGFLKSKDPGDGTEQaLLDELTSFDDYIKENGPFiNGEKISAADLSLGpKLYHLEIALGHYK 221

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 28973477  172 SFSIEAECPKLIAWGKRCVERESVAKSLPDSEKII 206
Cdd:PLN02817 222 NWSVPDSLPFVKSYMKNIFSMESFVKTRALPEDVI 256
PRK15113 PRK15113
glutathione transferase;
1-96 1.02e-04

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 41.87  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28973477    1 MADEVILL----DFWpSMFGMRTRIALEEKNVKFDYREQDL---WNKSPILLEMNPVhKKIPVLIHNGNPVCESLIQIEY 73
Cdd:PRK15113   1 MSKPAITLysdaHFF-SPYVMSAFVALQEKGLPFELKTVDLdagEHLQPTYQGYSLT-RRVPTLQHDDFELSESSAIAEY 78

                         90       100
                 ....*....|....*....|....*
gi 28973477   74 IDEVWPSKT--PLLPSDPYQRAQAK 96
Cdd:PRK15113  79 LEERFAPPAweRIYPADLQARARAR 103
GST_N_Delta_Epsilon cd03045
GST_N family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved ...
 27-67 2.15e-04

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.


Pssm-ID: 239343 [Multi-domain]  Cd Length: 74  Bit Score: 38.36  E-value: 2.15e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 28973477  27 NVKFDYREQDLWNK---SPILLEMNPVHKkIPVLIHNGNPVCES 67
Cdd:cd03045  23 GLELNLKEVNLMKGehlKPEFLKLNPQHT-VPTLVDNGFVLWES 65
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 15-75 3.97e-04

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.


Pssm-ID: 239353 [Multi-domain]  Cd Length: 89  Bit Score: 38.10  E-value: 3.97e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28973477  15 FGMRTRIALEEKNVKFDYREQDLWNKSPILLEMNPVhKKIPVLIHNGNPVC-ESLIQIEYID 75
Cdd:cd03055  29 YAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPQ-GKVPALEIDEGKVVyESLIICEYLD 89
GST_C_Omega cd03184
C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione ...
 90-208 2.36e-03

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.


Pssm-ID: 198293 [Multi-domain]  Cd Length: 124  Bit Score: 36.92  E-value: 2.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28973477  90 YQRAQAKFwgdFIDK--KVYASARLIWGAKGEEhEAGKKEFIEILKTLESELGDK--TYFGGETFGYVDIALigfYSWFE 165
Cdd:cd03184   1 YEKAQQKM---LIERfsKVPSAFYKFLRSGEDR-KGLKEELRSALENLEEELAKRgtPFFGGNSPGMVDYMI---WPWFE 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 28973477 166 AYEKFGSFSIEAEC----PKLIAWGKRCVERESVAKSLPDSEKIIKF 208
Cdd:cd03184  74 RLEALKLLDGYELCldrfPKLKKWMAAMKQDPAVKAFYTDPETHAEF 120
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
 18-76 2.70e-03

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.


Pssm-ID: 239351 [Multi-domain]  Cd Length: 76  Bit Score: 35.70  E-value: 2.70e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28973477  18 RTRIALEEKNVKFDYREQDLW---NKSPILLEMNPVhKKIPVLIHNGNPVCESLIQIEYIDE 76
Cdd:cd03053  15 RVLLCLEEKGVDYELVPVDLTkgeHKSPEHLARNPF-GQIPALEDGDLKLFESRAITRYLAE 75
GST_C_2 cd03180
C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; ...
 122-192 2.77e-03

C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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.


Pssm-ID: 198289 [Multi-domain]  Cd Length: 110  Bit Score: 36.10  E-value: 2.77e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28973477 122 EAGKKEFIEILKTLESELGDKTYFGGETFGYVDIALIGF-YSWFEayekfgsFSIE-AECPKLIAWGKRCVER 192
Cdd:cd03180  42 AASLAACNKLMAILDAQLARQAYLAGDRFTLADIALGCSvYRWLE-------LPIErPALPHLERWYARLSQR 107
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
 16-74 4.03e-03

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.


Pssm-ID: 239344 [Multi-domain]  Cd Length: 76  Bit Score: 35.17  E-value: 4.03e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28973477  16 GMRTRIALEEKNVKFDYREQDL---WNKSPILLEMNPvHKKIPVLIHNGNPVCESLIQIEYI 74
Cdd:cd03046  11 SFRILWLLEELGLPYELVLYDRgpgEQAPPEYLAINP-LGKVPVLVDGDLVLTESAAIILYL 71
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
 18-75 9.90e-03

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.


Pssm-ID: 239349 [Multi-domain]  Cd Length: 74  Bit Score: 33.81  E-value: 9.90e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28973477  18 RTRIALEEKNVKFDYREQDLW---NKSPILLEMNPvHKKIPVL-IHNGNPVCESLIQIEYID 75
Cdd:cd03051  14 RVRIFLAEKGIDVPLVTVDLAageQRSPEFLAKNP-AGTVPVLeLDDGTVITESVAICRYLE 74
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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