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Conserved domains on  [gi|1653017127|pdb|6J3H|C]
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Chain C, Glutathione S-transferase

Protein Classification

glutathione S-transferase family protein( domain architecture ID 11627280)

glutathione S-transferase family protein such as glutathione S-transferase, which 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

CATH:  3.40.30.10|1.20.1050.10
EC:  2.5.1.-
Gene Ontology:  GO:0016740
PubMed:  15822171|16839810|9074797
SCOP:  4000976|4000472

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 13-110 1.37e-24

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member cd03038:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 84  Bit Score: 93.56  E-value: 1.37e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J3H_C       13 IHFYDIPrNRDEDdRTWNPNTSKTRLTLTYKRLPYKTIWVEYPDIERVCKEIGAEPSafgllkegkpyYSLPVIHDPNtG 92
Cdd:cd03038   1 ITLYDLA-GKDPV-RAFSPNVWKTRLALNHKGLEYKTVPVEFPDIPPILGELTSGGF-----------YTVPVIVDGS-G 66

                        90
                ....*....|....*...
6J3H_C       93 TTISDSIRIARYLDKTYP 110
Cdd:cd03038  67 EVIGDSFAIAEYLEEAYP 84
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
31-229 6.34e-09

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


:

Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 54.52  E-value: 6.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J3H_C       31 PNTSKTRLTLTYKRLPYKTIWVEYPDIErvckEIGAEPSAFGLLkeGKpyysLPVIHDpnTGTTISDSIRIARYLDKTYP 110
Cdd:COG0625  11 PNSRRVRIALEEKGLPYELVPVDLAKGE----QKSPEFLALNPL--GK----VPVLVD--DGLVLTESLAILEYLAERYP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J3H_C      111 DtPAVIPAELEAFHAVFEDAFW-DTIFMPLfpflvpaacpqlnprseayfretregkfgsiLGGKMENWAPTG--PVRDD 187
Cdd:COG0625  79 E-PPLLPADPAARARVRQWLAWaDGDLHPA-------------------------------LRNLLERLAPEKdpAAIAR 126

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
6J3H_C      188 RWKALQAGFTKMAGWLSadgqERPFFMGEKLCYTDIVVGAWL 229
Cdd:COG0625 127 ARAELARLLAVLEARLA----GGPYLAGDRFSIADIALAPVL 164
 
Name Accession Description Interval E-value
GST_N_etherase_LigE cd03038
GST_N family, Beta etherase LigE subfamily; composed of proteins similar to Sphingomonas ...
 13-110 1.37e-24

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


Pssm-ID: 239336 [Multi-domain]  Cd Length: 84  Bit Score: 93.56  E-value: 1.37e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J3H_C       13 IHFYDIPrNRDEDdRTWNPNTSKTRLTLTYKRLPYKTIWVEYPDIERVCKEIGAEPSafgllkegkpyYSLPVIHDPNtG 92
Cdd:cd03038   1 ITLYDLA-GKDPV-RAFSPNVWKTRLALNHKGLEYKTVPVEFPDIPPILGELTSGGF-----------YTVPVIVDGS-G 66

                        90
                ....*....|....*...
6J3H_C       93 TTISDSIRIARYLDKTYP 110
Cdd:cd03038  67 EVIGDSFAIAEYLEEAYP 84
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 31-108 1.87e-09

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 52.63  E-value: 1.87e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
6J3H_C         31 PNTSKTRLTLTYKRLPYKTIWVEYPDIERvckeiGAEpsafglLKEGKPYYSLPVIHDPNtGTTISDSIRIARYLDKT 108
Cdd:pfam13409   3 PFSHRVRLALEEKGLPYEIELVDLDPKDK-----PPE------LLALNPLGTVPVLVLPD-GTVLTDSLVILEYLEEL 68
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
31-229 6.34e-09

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 54.52  E-value: 6.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J3H_C       31 PNTSKTRLTLTYKRLPYKTIWVEYPDIErvckEIGAEPSAFGLLkeGKpyysLPVIHDpnTGTTISDSIRIARYLDKTYP 110
Cdd:COG0625  11 PNSRRVRIALEEKGLPYELVPVDLAKGE----QKSPEFLALNPL--GK----VPVLVD--DGLVLTESLAILEYLAERYP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J3H_C      111 DtPAVIPAELEAFHAVFEDAFW-DTIFMPLfpflvpaacpqlnprseayfretregkfgsiLGGKMENWAPTG--PVRDD 187
Cdd:COG0625  79 E-PPLLPADPAARARVRQWLAWaDGDLHPA-------------------------------LRNLLERLAPEKdpAAIAR 126

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
6J3H_C      188 RWKALQAGFTKMAGWLSadgqERPFFMGEKLCYTDIVVGAWL 229
Cdd:COG0625 127 ARAELARLLAVLEARLA----GGPYLAGDRFSIADIALAPVL 164
GST_C_etherase_LigE cd03202
C-terminal, alpha helical domain of Beta etherase LigE; Glutathione S-transferase (GST) ...
 131-232 4.02e-04

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


Pssm-ID: 198311  Cd Length: 124  Bit Score: 39.17  E-value: 4.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J3H_C      131 FWDTIFMPLFPFLVPAACPQLNPRSEAYFRETREGKFGSilggKMENWAPTgpvRDDRWKALQAGFTKMAGWLsadgQER 210
Cdd:cd03202   9 SDLTLHPALARLILLDIHDRLDPADRDYFRQSREARFGR----TLEEVAAG---REERLAAFRAALEPLRLTL----AGQ 77

                        90       100
                ....*....|....*....|....*
6J3H_C      211 PFFMGEKLCYTD-IVVGA--WLISV 232
Cdd:cd03202  78 PFLGGAAPNYADyIVFGAfqWARSV 102
 
Name Accession Description Interval E-value
GST_N_etherase_LigE cd03038
GST_N family, Beta etherase LigE subfamily; composed of proteins similar to Sphingomonas ...
 13-110 1.37e-24

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


Pssm-ID: 239336 [Multi-domain]  Cd Length: 84  Bit Score: 93.56  E-value: 1.37e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J3H_C       13 IHFYDIPrNRDEDdRTWNPNTSKTRLTLTYKRLPYKTIWVEYPDIERVCKEIGAEPSafgllkegkpyYSLPVIHDPNtG 92
Cdd:cd03038   1 ITLYDLA-GKDPV-RAFSPNVWKTRLALNHKGLEYKTVPVEFPDIPPILGELTSGGF-----------YTVPVIVDGS-G 66

                        90
                ....*....|....*...
6J3H_C       93 TTISDSIRIARYLDKTYP 110
Cdd:cd03038  67 EVIGDSFAIAEYLEEAYP 84
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 31-108 1.87e-09

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 52.63  E-value: 1.87e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
6J3H_C         31 PNTSKTRLTLTYKRLPYKTIWVEYPDIERvckeiGAEpsafglLKEGKPYYSLPVIHDPNtGTTISDSIRIARYLDKT 108
Cdd:pfam13409   3 PFSHRVRLALEEKGLPYEIELVDLDPKDK-----PPE------LLALNPLGTVPVLVLPD-GTVLTDSLVILEYLEEL 68
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
31-229 6.34e-09

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 54.52  E-value: 6.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J3H_C       31 PNTSKTRLTLTYKRLPYKTIWVEYPDIErvckEIGAEPSAFGLLkeGKpyysLPVIHDpnTGTTISDSIRIARYLDKTYP 110
Cdd:COG0625  11 PNSRRVRIALEEKGLPYELVPVDLAKGE----QKSPEFLALNPL--GK----VPVLVD--DGLVLTESLAILEYLAERYP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J3H_C      111 DtPAVIPAELEAFHAVFEDAFW-DTIFMPLfpflvpaacpqlnprseayfretregkfgsiLGGKMENWAPTG--PVRDD 187
Cdd:COG0625  79 E-PPLLPADPAARARVRQWLAWaDGDLHPA-------------------------------LRNLLERLAPEKdpAAIAR 126

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
6J3H_C      188 RWKALQAGFTKMAGWLSadgqERPFFMGEKLCYTDIVVGAWL 229
Cdd:COG0625 127 ARAELARLLAVLEARLA----GGPYLAGDRFSIADIALAPVL 164
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 29-106 2.19e-05

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: 41.40  E-value: 2.19e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
6J3H_C       29 WNPNTSKTRLTLTYKRLPYKTIWVEYPDIERvckeigaepsafGLLKEGKPYYSLPVIHDPntGTTISDSIRIARYLD 106
Cdd:cd00570   8 GSPRSLRVRLALEEKGLPYELVPVDLGEGEQ------------EEFLALNPLGKVPVLEDG--GLVLTESLAILEYLA 71
GST_C_etherase_LigE cd03202
C-terminal, alpha helical domain of Beta etherase LigE; Glutathione S-transferase (GST) ...
 131-232 4.02e-04

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


Pssm-ID: 198311  Cd Length: 124  Bit Score: 39.17  E-value: 4.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J3H_C      131 FWDTIFMPLFPFLVPAACPQLNPRSEAYFRETREGKFGSilggKMENWAPTgpvRDDRWKALQAGFTKMAGWLsadgQER 210
Cdd:cd03202   9 SDLTLHPALARLILLDIHDRLDPADRDYFRQSREARFGR----TLEEVAAG---REERLAAFRAALEPLRLTL----AGQ 77

                        90       100
                ....*....|....*....|....*
6J3H_C      211 PFFMGEKLCYTD-IVVGA--WLISV 232
Cdd:cd03202  78 PFLGGAAPNYADyIVFGAfqWARSV 102
GST_N_2GST_N cd03041
GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed ...
 82-109 1.69e-03

GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed of uncharacterized proteins. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST 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: 239339 [Multi-domain]  Cd Length: 77  Bit Score: 36.56  E-value: 1.69e-03
                        10        20
                ....*....|....*....|....*...
6J3H_C       82 SLPVIHDPNTGTTISDSIRIARYLDKTY 109
Cdd:cd03041  50 QVPYLVDPNTGVQMFESADIVKYLFKTY 77
 
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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