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Conserved domains on  [gi|13928688|ref|NP_113697|]
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glutathione S-transferase alpha-3 [Rattus norvegicus]

Protein Classification

glutathione S-transferase alpha( domain architecture ID 10122945)

class-alpha 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GST_C_Alpha cd03208
C-terminal, alpha helical domain of Class Alpha Glutathione S-transferases; Glutathione ...
 86-220 2.19e-75

C-terminal, alpha helical domain of Class Alpha Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Alpha 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 class Alpha subfamily is composed of vertebrate GSTs which can form homodimer and heterodimers. There are at least six types of class Alpha GST subunits in rats, four of which have human counterparts, resulting in many possible isoenzymes with different activities, tissue distribution and substrate specificities. Human GSTA1-1 and GSTA2-2 show high GSH peroxidase activity. GSTA3-3 catalyzes the isomerization of intermediates in steroid hormone biosynthesis. GSTA4-4 preferentially catalyzes the GSH conjugation of alkenals.


:

Pssm-ID: 198317 [Multi-domain]  Cd Length: 135  Bit Score: 223.75  E-value: 2.19e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928688  86 MKERALIDMYAEGVADLDEIVLHYPYIPPGEKEASLAKIKDKARNRYFPAFEKVLKSHGQDYLVGNRLSRADVYLVQVLY 165
Cdd:cd03208   1 LKERALIDMYVEGTADLMEMIMMLPFLPPEEKEAKLALIKEKAKNRYFPVFEKVLKDHGQDFLVGNKLSRADVQLLEAIL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 13928688 166 HVEELDPSALANFPLLKALRTRVSNLPTVKKFLQPGSQRKPLEDEKCVESAVKIF 220
Cdd:cd03208  81 MVEELDPSILSDFPLLQAFKTRISNIPTIKKFLQPGSKRKPPPDEKYVETVRKVF 135
GST_N_Alpha cd03077
GST_N family, Class Alpha subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 4-82 3.44e-50

GST_N family, Class Alpha 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 class Alpha subfamily is composed of eukaryotic GSTs which can form homodimer and heterodimers. There are at least six types of class Alpha GST subunits in rats, four of which have human counterparts, resulting in many possible isoenzymes with different activities, tissue distribution and substrate specificities. Human GSTA1-1 and GSTA2-2 show high GSH peroxidase activity. GSTA3-3 catalyzes the isomerization of intermediates in steroid hormone biosynthesis. GSTA4-4 preferentially catalyzes the GSH conjugation of alkenals.


:

Pssm-ID: 239375  Cd Length: 79  Bit Score: 157.69  E-value: 3.44e-50
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13928688   4 KPVLHYFDGRGRMEPIRWLLAAAGVEFEEQFLKTRDDLARLRNDGSLMFQQVPMVEIDGMKLVQTRAILNYIATKYNLY 82
Cdd:cd03077   1 KPVLHYFNGRGRMESIRWLLAAAGVEFEEKFIESAEDLEKLKKDGSLMFQQVPMVEIDGMKLVQTRAILNYIAGKYNLY 79
 
Name Accession Description Interval E-value
GST_C_Alpha cd03208
C-terminal, alpha helical domain of Class Alpha Glutathione S-transferases; Glutathione ...
 86-220 2.19e-75

C-terminal, alpha helical domain of Class Alpha Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Alpha 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 class Alpha subfamily is composed of vertebrate GSTs which can form homodimer and heterodimers. There are at least six types of class Alpha GST subunits in rats, four of which have human counterparts, resulting in many possible isoenzymes with different activities, tissue distribution and substrate specificities. Human GSTA1-1 and GSTA2-2 show high GSH peroxidase activity. GSTA3-3 catalyzes the isomerization of intermediates in steroid hormone biosynthesis. GSTA4-4 preferentially catalyzes the GSH conjugation of alkenals.


Pssm-ID: 198317 [Multi-domain]  Cd Length: 135  Bit Score: 223.75  E-value: 2.19e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928688  86 MKERALIDMYAEGVADLDEIVLHYPYIPPGEKEASLAKIKDKARNRYFPAFEKVLKSHGQDYLVGNRLSRADVYLVQVLY 165
Cdd:cd03208   1 LKERALIDMYVEGTADLMEMIMMLPFLPPEEKEAKLALIKEKAKNRYFPVFEKVLKDHGQDFLVGNKLSRADVQLLEAIL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 13928688 166 HVEELDPSALANFPLLKALRTRVSNLPTVKKFLQPGSQRKPLEDEKCVESAVKIF 220
Cdd:cd03208  81 MVEELDPSILSDFPLLQAFKTRISNIPTIKKFLQPGSKRKPPPDEKYVETVRKVF 135
GST_N_Alpha cd03077
GST_N family, Class Alpha subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 4-82 3.44e-50

GST_N family, Class Alpha 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 class Alpha subfamily is composed of eukaryotic GSTs which can form homodimer and heterodimers. There are at least six types of class Alpha GST subunits in rats, four of which have human counterparts, resulting in many possible isoenzymes with different activities, tissue distribution and substrate specificities. Human GSTA1-1 and GSTA2-2 show high GSH peroxidase activity. GSTA3-3 catalyzes the isomerization of intermediates in steroid hormone biosynthesis. GSTA4-4 preferentially catalyzes the GSH conjugation of alkenals.


Pssm-ID: 239375  Cd Length: 79  Bit Score: 157.69  E-value: 3.44e-50
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13928688   4 KPVLHYFDGRGRMEPIRWLLAAAGVEFEEQFLKTRDDLARLRNDGSLMFQQVPMVEIDGMKLVQTRAILNYIATKYNLY 82
Cdd:cd03077   1 KPVLHYFNGRGRMESIRWLLAAAGVEFEEKFIESAEDLEKLKKDGSLMFQQVPMVEIDGMKLVQTRAILNYIAGKYNLY 79
PTZ00057 PTZ00057
glutathione s-transferase; Provisional
 6-198 3.66e-28

glutathione s-transferase; Provisional


Pssm-ID: 173353 [Multi-domain]  Cd Length: 205  Bit Score: 105.45  E-value: 3.66e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928688    6 VLHYFDGRGRMEPIRWLLAAAGVEF-EEQFLKTRDDLARLRN---DGSLMFQQVPMVEIDGMKLVQTRAILNYIATKYNL 81
Cdd:PTZ00057   6 VLYYFDARGKAELIRLIFAYLGIEYtDKRFGENGDAFIEFKNfkkEKDTPFEQVPILEMDNIIFAQSQAIVRYLSKKYKI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928688   82 YGKDMKERALIDMYAEGVADLdeivlHYPYIPPGEKEASLAKIKDKARNRYFPAFEKVLKSHGQDYLVGNRLSRADVYLV 161
Cdd:PTZ00057  86 CGESELNEFYADMIFCGVQDI-----HYKFNNTNLFKQNETTFLNEELPKWSGYFENILKKNHCNYFVGDNLTYADLAVF 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 13928688  162 QVLYHVEELDPSALANFPLLKALRTRVSNLPTVKKFL 198
Cdd:PTZ00057 161 NLYDDIETKYPNSLKNFPLLKAHNEFISNLPNIKNYI 197
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 101-199 3.67e-22

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


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 86.84  E-value: 3.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928688   101 DLDEIVLHYPYIPPGEKEASLAK-IKDKARNRYFPAFEKVLKSHGQDYLVGNRLSRADVYLVQVLYHVEE-LDPSALANF 178
Cdd:pfam14497   2 DLHHPIASSLYYEDEKKKAKRRKeFREERLPKFLGYFEKVLNKNGGGYLVGDKLTYADLALFQVLDGLLYpKAPDALDKY 81

                          90       100
                  ....*....|....*....|.
gi 13928688   179 PLLKALRTRVSNLPTVKKFLQ 199
Cdd:pfam14497  82 PKLKALHERVAARPNIKAYLA 102
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
7-201 8.26e-19

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 80.71  E-value: 8.26e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928688   7 LHYFDGRGRMEPIRWLLAAAGVEFEEQFLK------TRDDLARLrNDgslmFQQVPMVEIDGMKLVQTRAILNYIATKY- 79
Cdd:COG0625   4 LYGSPPSPNSRRVRIALEEKGLPYELVPVDlakgeqKSPEFLAL-NP----LGKVPVLVDDGLVLTESLAILEYLAERYp 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928688  80 --NLYGKDMKERALIDM---YAEGVADlDEIVLHYPYIPPGEKEASLAKIKDKARnRYFPAFEKVLKshGQDYLVGNRLS 154
Cdd:COG0625  79 epPLLPADPAARARVRQwlaWADGDLH-PALRNLLERLAPEKDPAAIARARAELA-RLLAVLEARLA--GGPYLAGDRFS 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 13928688 155 RADVYLVQVLYHVEELDPSaLANFPLLKALRTRVSNLPTVKKFLQPG 201
Cdd:COG0625 155 IADIALAPVLRRLDRLGLD-LADYPNLAAWLARLAARPAFQRALAAA 200
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 5-76 1.40e-17

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: 74.26  E-value: 1.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928688     5 PVLHYFDGRG--RMEPIRWLLAAAGVEFEEQFLKT------RDDLARLRNdgslmFQQVPMVEIDGMKLVQTRAILNYIA 76
Cdd:pfam02798   1 MVLTLYGIRGspRAHRIRWLLAEKGVEYEIVPLDFgagpekSPELLKLNP-----LGKVPALEDGGKKLTESRAILEYIA 75
PLN02473 PLN02473
glutathione S-transferase
 52-97 9.80e-07

glutathione S-transferase


Pssm-ID: 166114 [Multi-domain]  Cd Length: 214  Bit Score: 47.68  E-value: 9.80e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 13928688   52 FQQVPMVEIDGMKLVQTRAILNYIATKY-----NLYGKDMKERALIDMYAE 97
Cdd:PLN02473  51 FGQVPAIEDGDLKLFESRAIARYYATKYadqgtDLLGKTLEHRAIVDQWVE 101
 
Name Accession Description Interval E-value
GST_C_Alpha cd03208
C-terminal, alpha helical domain of Class Alpha Glutathione S-transferases; Glutathione ...
 86-220 2.19e-75

C-terminal, alpha helical domain of Class Alpha Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Alpha 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 class Alpha subfamily is composed of vertebrate GSTs which can form homodimer and heterodimers. There are at least six types of class Alpha GST subunits in rats, four of which have human counterparts, resulting in many possible isoenzymes with different activities, tissue distribution and substrate specificities. Human GSTA1-1 and GSTA2-2 show high GSH peroxidase activity. GSTA3-3 catalyzes the isomerization of intermediates in steroid hormone biosynthesis. GSTA4-4 preferentially catalyzes the GSH conjugation of alkenals.


Pssm-ID: 198317 [Multi-domain]  Cd Length: 135  Bit Score: 223.75  E-value: 2.19e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928688  86 MKERALIDMYAEGVADLDEIVLHYPYIPPGEKEASLAKIKDKARNRYFPAFEKVLKSHGQDYLVGNRLSRADVYLVQVLY 165
Cdd:cd03208   1 LKERALIDMYVEGTADLMEMIMMLPFLPPEEKEAKLALIKEKAKNRYFPVFEKVLKDHGQDFLVGNKLSRADVQLLEAIL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 13928688 166 HVEELDPSALANFPLLKALRTRVSNLPTVKKFLQPGSQRKPLEDEKCVESAVKIF 220
Cdd:cd03208  81 MVEELDPSILSDFPLLQAFKTRISNIPTIKKFLQPGSKRKPPPDEKYVETVRKVF 135
GST_N_Alpha cd03077
GST_N family, Class Alpha subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 4-82 3.44e-50

GST_N family, Class Alpha 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 class Alpha subfamily is composed of eukaryotic GSTs which can form homodimer and heterodimers. There are at least six types of class Alpha GST subunits in rats, four of which have human counterparts, resulting in many possible isoenzymes with different activities, tissue distribution and substrate specificities. Human GSTA1-1 and GSTA2-2 show high GSH peroxidase activity. GSTA3-3 catalyzes the isomerization of intermediates in steroid hormone biosynthesis. GSTA4-4 preferentially catalyzes the GSH conjugation of alkenals.


Pssm-ID: 239375  Cd Length: 79  Bit Score: 157.69  E-value: 3.44e-50
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13928688   4 KPVLHYFDGRGRMEPIRWLLAAAGVEFEEQFLKTRDDLARLRNDGSLMFQQVPMVEIDGMKLVQTRAILNYIATKYNLY 82
Cdd:cd03077   1 KPVLHYFNGRGRMESIRWLLAAAGVEFEEKFIESAEDLEKLKKDGSLMFQQVPMVEIDGMKLVQTRAILNYIAGKYNLY 79
PTZ00057 PTZ00057
glutathione s-transferase; Provisional
 6-198 3.66e-28

glutathione s-transferase; Provisional


Pssm-ID: 173353 [Multi-domain]  Cd Length: 205  Bit Score: 105.45  E-value: 3.66e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928688    6 VLHYFDGRGRMEPIRWLLAAAGVEF-EEQFLKTRDDLARLRN---DGSLMFQQVPMVEIDGMKLVQTRAILNYIATKYNL 81
Cdd:PTZ00057   6 VLYYFDARGKAELIRLIFAYLGIEYtDKRFGENGDAFIEFKNfkkEKDTPFEQVPILEMDNIIFAQSQAIVRYLSKKYKI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928688   82 YGKDMKERALIDMYAEGVADLdeivlHYPYIPPGEKEASLAKIKDKARNRYFPAFEKVLKSHGQDYLVGNRLSRADVYLV 161
Cdd:PTZ00057  86 CGESELNEFYADMIFCGVQDI-----HYKFNNTNLFKQNETTFLNEELPKWSGYFENILKKNHCNYFVGDNLTYADLAVF 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 13928688  162 QVLYHVEELDPSALANFPLLKALRTRVSNLPTVKKFL 198
Cdd:PTZ00057 161 NLYDDIETKYPNSLKNFPLLKAHNEFISNLPNIKNYI 197
GST_N_Sigma_like cd03039
GST_N family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, ...
 5-76 1.38e-26

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.


Pssm-ID: 239337 [Multi-domain]  Cd Length: 72  Bit Score: 97.23  E-value: 1.38e-26
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13928688   5 PVLHYFDGRGRMEPIRWLLAAAGVEFEEQFLkTRDDLARLRNDGSLMFQQVPMVEIDGMKLVQTRAILNYIA 76
Cdd:cd03039   1 YKLTYFNIRGRGEPIRLLLADAGVEYEDVRI-TYEEWPELDLKPTLPFGQLPVLEIDGKKLTQSNAILRYLA 71
GST_C_Sigma_like cd03192
C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione ...
 88-188 2.84e-23

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.


Pssm-ID: 198301 [Multi-domain]  Cd Length: 104  Bit Score: 89.60  E-value: 2.84e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928688  88 ERALIDMYAEGVADLDEIVLHYPYIP-PGEKEASLAKIKDKARNRYFPAFEKVLKSHGQDYLVGNRLSRADVYLVQVLYH 166
Cdd:cd03192   2 EEARVDAIVDTIADLRAEFAPYFYEPdGEEKKEKKKEFLEEALPKFLGKFEKILKKSGGGYFVGDKLTWADLALFDVLDY 81

                        90       100
                ....*....|....*....|...
gi 13928688 167 VEELDPSALA-NFPLLKALRTRV 188
Cdd:cd03192  82 LLYLLPKDLLeKYPKLKALRERV 104
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 101-199 3.67e-22

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


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 86.84  E-value: 3.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928688   101 DLDEIVLHYPYIPPGEKEASLAK-IKDKARNRYFPAFEKVLKSHGQDYLVGNRLSRADVYLVQVLYHVEE-LDPSALANF 178
Cdd:pfam14497   2 DLHHPIASSLYYEDEKKKAKRRKeFREERLPKFLGYFEKVLNKNGGGYLVGDKLTYADLALFQVLDGLLYpKAPDALDKY 81

                          90       100
                  ....*....|....*....|.
gi 13928688   179 PLLKALRTRVSNLPTVKKFLQ 199
Cdd:pfam14497  82 PKLKALHERVAARPNIKAYLA 102
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 99-192 1.07e-21

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: 85.42  E-value: 1.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928688    99 VADLDEIVLHYPYIPPGEKEASLAKIKDKARNRYFPAFEKVLKshGQDYLVGNRLSRADVYLVQVLYHVEELDPSAL-AN 177
Cdd:pfam00043   1 LMDLRMQIALLPYVPPEEKKEPEVDEALEKVARVLSALEEVLK--GQTYLVGDKLTLADIALAPALLWLYELDPACLrEK 78

                          90
                  ....*....|....*
gi 13928688   178 FPLLKALRTRVSNLP 192
Cdd:pfam00043  79 FPNLKAWFERVAARP 93
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
7-201 8.26e-19

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 80.71  E-value: 8.26e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928688   7 LHYFDGRGRMEPIRWLLAAAGVEFEEQFLK------TRDDLARLrNDgslmFQQVPMVEIDGMKLVQTRAILNYIATKY- 79
Cdd:COG0625   4 LYGSPPSPNSRRVRIALEEKGLPYELVPVDlakgeqKSPEFLAL-NP----LGKVPVLVDDGLVLTESLAILEYLAERYp 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928688  80 --NLYGKDMKERALIDM---YAEGVADlDEIVLHYPYIPPGEKEASLAKIKDKARnRYFPAFEKVLKshGQDYLVGNRLS 154
Cdd:COG0625  79 epPLLPADPAARARVRQwlaWADGDLH-PALRNLLERLAPEKDPAAIARARAELA-RLLAVLEARLA--GGPYLAGDRFS 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 13928688 155 RADVYLVQVLYHVEELDPSaLANFPLLKALRTRVSNLPTVKKFLQPG 201
Cdd:COG0625 155 IADIALAPVLRRLDRLGLD-LADYPNLAAWLARLAARPAFQRALAAA 200
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 5-76 1.40e-17

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: 74.26  E-value: 1.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928688     5 PVLHYFDGRG--RMEPIRWLLAAAGVEFEEQFLKT------RDDLARLRNdgslmFQQVPMVEIDGMKLVQTRAILNYIA 76
Cdd:pfam02798   1 MVLTLYGIRGspRAHRIRWLLAEKGVEYEIVPLDFgagpekSPELLKLNP-----LGKVPALEDGGKKLTESRAILEYIA 75
GST_C_Pi cd03210
C-terminal, alpha helical domain of Class Pi Glutathione S-transferases; Glutathione ...
 87-199 4.81e-15

C-terminal, alpha helical domain of Class Pi Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Pi 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 Pi GST is a homodimeric eukaryotic protein. The human GSTP1 is mainly found in erythrocytes, kidney, placenta and fetal liver. It is involved in stress responses and in cellular proliferation pathways as an inhibitor of JNK (c-Jun N-terminal kinase). Following oxidative stress, monomeric GSTP1 dissociates from JNK and dimerizes, losing its ability to bind JNK and causing an increase in JNK activity, thereby promoting apoptosis. GSTP1 is expressed in various tumors and is the predominant GST in a wide range of cancer cells. It has been implicated in the development of multidrug-resistant tumors.


Pssm-ID: 198319 [Multi-domain]  Cd Length: 126  Bit Score: 68.88  E-value: 4.81e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928688  87 KERALIDMYAEGVADLDEIVLHYPYIppgEKEASLAK-IKDKARNryFPAFEKVLKSH-GQDYLVGNRLSRADVYLVQVL 164
Cdd:cd03210   2 KEAALIDMVNDGVEDLRLKYVRMIYQ---NYEAGKDDyIKDLPEQ--LKPFEKLLAKNnGKGFIVGDKISFADYNLFDLL 76

                        90       100       110
                ....*....|....*....|....*....|....*
gi 13928688 165 YHVEELDPSALANFPLLKALRTRVSNLPTVKKFLQ 199
Cdd:cd03210  77 DIHLVLAPGCLDAFPLLKAFVERLSARPKLKAYLE 111
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 5-76 2.71e-12

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: 59.89  E-value: 2.71e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13928688   5 PVLHYFDGRGRMEPIRWLLAAAGVEFEEQFLKTRDDLARLRNDGSLmFQQVPMVEIDGMKLVQTRAILNYIA 76
Cdd:cd00570   1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQEEFLALNP-LGKVPVLEDGGLVLTESLAILEYLA 71
GST_N_Pi cd03076
GST_N family, Class Pi subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 4-78 3.19e-10

GST_N family, Class Pi 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 Pi GST is a homodimeric eukaryotic protein. The human GSTP1 is mainly found in erythrocytes, kidney, placenta and fetal liver. It is involved in stress responses and in cellular proliferation pathways as an inhibitor of JNK (c-Jun N-terminal kinase). Following oxidative stress, monomeric GSTP1 dissociates from JNK and dimerizes, losing its ability to bind JNK and causing an increase in JNK activity, thereby promoting apoptosis. GSTP1 is expressed in various tumors and is the predominant GST in a wide range of cancer cells. It has been implicated in the development of multidrug-resistant tumours.


Pssm-ID: 239374 [Multi-domain]  Cd Length: 73  Bit Score: 54.63  E-value: 3.19e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13928688   4 KPVLHYFDGRGRMEPIRWLLAAAGVEFEEQFLkTRDDLARLRNDgSLMFQQVPMVEIDGMKLVQTRAILNYIATK 78
Cdd:cd03076   1 PYTLTYFPVRGRAEAIRLLLADQGISWEEERV-TYEEWQESLKP-KMLFGQLPCFKDGDLTLVQSNAILRHLGRK 73
GST_C_Mu cd03209
C-terminal, alpha helical domain of Class Mu Glutathione S-transferases; Glutathione ...
 87-204 5.47e-09

C-terminal, alpha helical domain of Class Mu Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Mu 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 class Mu subfamily is composed of eukaryotic GSTs. In rats, at least six distinct class Mu subunits have been identified, with homologous genes in humans for five of these subunits. Class Mu GSTs can form homodimers and heterodimers, giving a large number of possible isoenzymes that can be formed, all with overlapping activities but different substrate specificities. They are the most abundant GSTs in human liver, skeletal muscle and brain, and are believed to provide protection against diseases including cancer and neurodegenerative disorders. Some isoenzymes have additional specific functions. Human GST M1-1 acts as an endogenous inhibitor of ASK1 (apoptosis signal-regulating kinase 1) thereby suppressing ASK1-mediated cell death. Human GSTM2-2 and 3-3 have been identified as prostaglandin E2 synthases in the brain and may play crucial roles in temperature and sleep-wake regulation.


Pssm-ID: 198318 [Multi-domain]  Cd Length: 121  Bit Score: 52.25  E-value: 5.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928688  87 KERALIDMYAEGVADLDEIVLHYPYIPPGE--KEASLAKIKDKarnryFPAFEKVLKSHgqDYLVGNRLSRADVYLVQVL 164
Cdd:cd03209   1 KERIRVDMLEQQAMDLRMGLIRICYSPDFEklKPDYLEKLPDK-----LKLFSEFLGDR--PWFAGDKITYVDFLLYEAL 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 13928688 165 YHVEELDPSALANFPLLKALRTRVSNLPTVKKFLQpgSQR 204
Cdd:cd03209  74 DQHRIFEPDCLDAFPNLKDFLERFEALPKISAYMK--SDR 111
GST_N_Mu cd03075
GST_N family, Class Mu subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 5-79 5.71e-07

GST_N family, Class Mu 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 class Mu subfamily is composed of eukaryotic GSTs. In rats, at least six distinct class Mu subunits have been identified, with homologous genes in humans for five of these subunits. Class Mu GSTs can form homodimers and heterodimers, giving a large number of possible isoenzymes that can be formed, all with overlapping activities but different substrate specificities. They are the most abundant GSTs in human liver, skeletal muscle and brain, and are believed to provide protection against diseases including cancer and neurodegenerative disorders. Some isoenzymes have additional specific functions. Human GST M1-1 acts as an endogenous inhibitor of ASK1 (apoptosis signal-regulating kinase 1), thereby suppressing ASK1-mediated cell death. Human GSTM2-2 and 3-3 have been identified as prostaglandin E2 synthases in the brain and may play crucial roles in temperature and sleep-wake regulation.


Pssm-ID: 239373 [Multi-domain]  Cd Length: 82  Bit Score: 45.84  E-value: 5.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928688   5 PVLHYFDGRGRMEPIRWLLAAAGVEFEEQFLKTRD----DLARLRNDGS---LMFQQVPMVEIDGMKLVQTRAILNYIAT 77
Cdd:cd03075   1 PTLGYWDIRGLAQPIRLLLEYTGEKYEEKRYELGDapdyDRSQWLNEKFklgLDFPNLPYYIDGDVKLTQSNAILRYIAR 80


                ..
gi 13928688  78 KY 79
Cdd:cd03075  81 KH 82
PLN02473 PLN02473
glutathione S-transferase
 52-97 9.80e-07

glutathione S-transferase


Pssm-ID: 166114 [Multi-domain]  Cd Length: 214  Bit Score: 47.68  E-value: 9.80e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 13928688   52 FQQVPMVEIDGMKLVQTRAILNYIATKY-----NLYGKDMKERALIDMYAE 97
Cdd:PLN02473  51 FGQVPAIEDGDLKLFESRAIARYYATKYadqgtDLLGKTLEHRAIVDQWVE 101
GST_C_Beta cd03188
C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ...
 119-198 1.04e-06

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: 46.09  E-value: 1.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928688 119 ASLAKIKDKARNRYFPAF---EKVLKshGQDYLVGNRLSRADVYLVqVLYHVEELDPSALANFPLLKALRTRVSNLPTVK 195
Cdd:cd03188  34 ALAEEVKAAARERLERRLaylDAQLA--GGPYLLGDQFSVADAYLF-VVLRWARAVGLDLSDWPHLAAYLARVAARPAVQ 110


                ...
gi 13928688 196 KFL 198
Cdd:cd03188 111 AAL 113
GST_C_EF1Bgamma_like cd03181
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ...
 88-198 9.13e-06

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.


Pssm-ID: 198290 [Multi-domain]  Cd Length: 123  Bit Score: 43.70  E-value: 9.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928688  88 ERALIDMYA-----EGVADLDEIVL----HYPYIPPGEKEAslakiKDKArNRYFPAFEKVLKSHGqdYLVGNRLSRADV 158
Cdd:cd03181   1 EAAQVLQWIsfansELLPAAATWVLpllgIAPYNKKAVDKA-----KEDL-KRALGVLEEHLLTRT--YLVGERITLADI 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 13928688 159 YLVQVLYHVEE--LDPSALANFPLLKALRTRVSNLPTVKKFL 198
Cdd:cd03181  73 FVASALLRGFEtvLDPEFRKKYPNVTRWFNTVVNQPKFKAVF 114
GST_C_Zeta cd03191
C-terminal, alpha helical domain of Class Zeta Glutathione S-transferases; Glutathione ...
 133-196 1.81e-05

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.


Pssm-ID: 198300 [Multi-domain]  Cd Length: 121  Bit Score: 42.57  E-value: 1.81e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13928688 133 FPAFEKVLKSHGQDYLVGNRLSRADVYLVQVLYHVEELDPSaLANFPLLKALRTRVSNLPTVKK 196
Cdd:cd03191  53 FQALEKLLASTAGKYCVGDEPTLADICLVPQVYNARRFGVD-LSPYPTIVRINEACLELPAFQA 115
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 89-188 5.88e-05

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: 40.95  E-value: 5.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928688  89 RALIDMYAEGVADLDEIVLHYPYIPPGEKEASLAKIKDKARnRYFPAFEKVLKshGQDYLVGNRLSRADVYLVQVLYHVE 168
Cdd:cd00299   2 RALEDWADATLAPPLVRLLYLEKVPLPKDEAAVEAAREELP-ALLAALEQLLA--GRPYLAGDQFSLADVALAPVLARLE 78

                        90       100
                ....*....|....*....|..
gi 13928688 169 ELDPSA--LANFPLLKALRTRV 188
Cdd:cd00299  79 ALGPYYdlLDEYPRLKAWYDRL 100
PLN02395 PLN02395
glutathione S-transferase
 52-158 1.28e-04

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 41.77  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928688   52 FQQVPMVEIDGMKLVQTRAILNYIATKY-----NLYGKDMKERALIDMYAEGVAD-----LDEIVLHYPY-----IPPGE 116
Cdd:PLN02395  50 FGVVPVIVDGDYKIFESRAIMRYYAEKYrsqgpDLLGKTIEERGQVEQWLDVEATsyhppLLNLTLHILFaskmgFPADE 129

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 13928688  117 K-----EASLAKIKDKARnryfpafEKVLKShgqDYLVGNRLSRADV 158
Cdd:PLN02395 130 KvikesEEKLAKVLDVYE-------ARLSKS---KYLAGDFVSLADL 166
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
 19-76 3.50e-04

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.


Pssm-ID: 239354 [Multi-domain]  Cd Length: 73  Bit Score: 37.94  E-value: 3.50e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13928688  19 IRWLLAAAGVEFEEQFL-----KTRDDLARLRNDgslmFQQVPMVEIDGMKLVQTRAILNYIA 76
Cdd:cd03056  15 VRLLLALLGIPYEWVEVdilkgETRTPEFLALNP----NGEVPVLELDGRVLAESNAILVYLA 73
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
 5-79 5.03e-04

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: 37.48  E-value: 5.03e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13928688   5 PVLHYFDgRGRMEPIRWLLAAAGVEFEEQFLKTRDDlaRLRNDGSLMFQ---QVPMVEIDGMKLVQTRAILNYIATKY 79
Cdd:cd03046   1 ITLYHLP-RSRSFRILWLLEELGLPYELVLYDRGPG--EQAPPEYLAINplgKVPVLVDGDLVLTESAAIILYLAEKY 75
AcetylCoA_hyd_C pfam13336
Acetyl-CoA hydrolase/transferase C-terminal domain; This family contains several enzymes which ...
 55-93 3.36e-03

Acetyl-CoA hydrolase/transferase C-terminal domain; This family contains several enzymes which take part in pathways involving acetyl-CoA. Acetyl-CoA hydrolase EC:3.1.2.1 catalyzes the formation of acetate from acetyl-CoA, CoA transferase (CAT1) EC:2.8.3.- produces succinyl-CoA, and acetate-CoA transferase EC:2.8.3.8 utilizes acyl-CoA and acetate to form acetyl-CoA.


Pssm-ID: 433126 [Multi-domain]  Cd Length: 154  Bit Score: 36.65  E-value: 3.36e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 13928688    55 VPMVEiDGMKLVQTRAILNYIATKY---NLYGKDMKERA--LID 93
Cdd:pfam13336  98 VPMLS-PGAHVTTTRHDVDYVVTEYgiaDLRGKSLRERAeaLIS 140
GST_C_Ure2p cd10293
C-terminal, alpha helical domain of fungal Ure2p Glutathione S-transferases; Glutathione ...
 130-196 5.48e-03

C-terminal, alpha helical domain of fungal Ure2p Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Ure2p subfamily; composed of the Saccharomyces cerevisiae Ure2p and related fungal 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. 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.


Pssm-ID: 198326 [Multi-domain]  Cd Length: 117  Bit Score: 35.48  E-value: 5.48e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13928688 130 NRYFPAFEKVLKSHGQDYLVGNRLSRADV------YLVQVLYHVEELDPSalANFPLLKALRTRVSNLPTVKK 196
Cdd:cd10293  46 RRVLGVLETALAERYRVWLVGDKFTIADLafvpwnNVVDMIFIDPELDIK--KEFPHVYKWLKRMLARPAVKK 116
GST_C_Omega_like cd03190
C-terminal, alpha helical domain of Class Omega-like Glutathione S-transferases; Glutathione ...
 126-196 9.37e-03

C-terminal, alpha helical domain of Class Omega-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae Omega-like subfamily; composed of three Saccharomyces cerevisiae GST omega-like (Gto) proteins, Gto1p, Gto2p (also known as Extracellular mutant protein 4 or ECM4p), and Gto3p, as well as similar uncharacterized proteins from fungi and bacteria. The three Saccharomyces cerevisiae Gto proteins are omega-class GSTs with low or no GST activity against standard substrates, but have glutaredoxin/thiol oxidoreductase and dehydroascorbate reductase activity through a single cysteine residue in the active site. Gto1p is located in the peroxisomes while Gto2p and Gto3p are cytosolic. The gene encoding Gto2p, called ECM4, is involved in cell surface biosynthesis and architecture. S. cerevisiae ECM4 mutants show increased amounts of the cell wall hexose, N-acetylglucosamine. More recently, global gene expression analysis shows that ECM4 is upregulated during genotoxic conditions and together with the expression profiles of 18 other genes could potentially differentiate between genotoxic and cytotoxic insults in yeast.


Pssm-ID: 198299 [Multi-domain]  Cd Length: 142  Bit Score: 35.24  E-value: 9.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928688 126 DKARNRYFPAF---EKVLKShgQDYLVGNRLSRADVYLVQVLYhveELDP----------SALANFPLLKALRTRVSNLP 192
Cdd:cd03190  36 DKAVKELFEALdklEKRLSK--QPYLLGDRLTEADIRLFTTLI---RFDPvyhqhfkcnlKTIRDYPNLWRYLRRLYQNP 110


                ....
gi 13928688 193 TVKK 196
Cdd:cd03190 111 GVFE 114
 
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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