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Conserved domains on  [gi|7705704|ref|NP_057001|]
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glutathione S-transferase kappa 1 isoform a [Homo sapiens]

Protein Classification

glutathione S-transferase; glutathione S-transferase omega family protein( domain architecture ID 10122488)

glutathione S-transferase 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| glutathione S-transferase (GST) omega family protein such as class-omega GSTs, which catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins than GSTs

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DsbA_GSTK cd03021
DsbA family, Glutathione (GSH) S-transferase Kappa (GSTK) subfamily; GSTK is a member of the ...
 6-211 5.21e-112

DsbA family, Glutathione (GSH) S-transferase Kappa (GSTK) subfamily; GSTK is a member of the GST family of enzymes which catalyzes the transfer of the thiol of GSH to electrophilic substrates. It is specifically located in the mitochondria and peroxisomes, unlike other members of the canonical GST family, which are mainly cytosolic. The biological substrates of GSTK are not yet known. It is presumed to have a protective role during respiration when large amounts of reactive oxygen species are generated. GSTK has the same general fold as DsbA, consisting of a thioredoxin domain interrupted by an alpha-helical domain and its biological unit is a homodimer. GSTK is closely related to the bacterial enzyme, 2-hydroxychromene-2-carboxylate (HCCA) isomerase. It shows little sequence similarity to the other members of the GST family.


:

Pssm-ID: 239319 [Multi-domain]  Cd Length: 209  Bit Score: 319.30  E-value: 5.21e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705704    6 RTVELFYDVLSPYSWLGFEILCRYQNIWNINLQLRPSLITGIMKDSGNKPPGLLPRKGLYMANDLKLLRHHLQIPIHFPK 85
Cdd:cd03021   1 PKIELYYDVVSPYSYLAFEVLCRYQTAWNVDITYVPVFLGGIMKDSGNKPPIMLPNKAKYMAKDRKRSAEFFGVPIRQPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705704   86 DFLSVmlEKGSLSAMRFLTAVNLEHPE----MLEKASRELWMRVWSRNEDITEPQSILAAAEKAGMSAEQAQGLLEKIAT 161
Cdd:cd03021  81 DFFFM--KKGTLTAQRFLTAISEQHPEstltALEALFREFWVRPWSLTEPITESQSISVAADKLGGSAEQAEKLLKAAST 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 7705704  162 PKVKNQLKETTEAACRYGAFGLPITVAHVD-GQTHMLFGSDRMELLAHLLG 211
Cdd:cd03021 159 PEVKNRLKENTDEALKYGAFGLPWIVVTNDkGKTEMFFGSDRFEQVADFLG 209
 
Name Accession Description Interval E-value
DsbA_GSTK cd03021
DsbA family, Glutathione (GSH) S-transferase Kappa (GSTK) subfamily; GSTK is a member of the ...
 6-211 5.21e-112

DsbA family, Glutathione (GSH) S-transferase Kappa (GSTK) subfamily; GSTK is a member of the GST family of enzymes which catalyzes the transfer of the thiol of GSH to electrophilic substrates. It is specifically located in the mitochondria and peroxisomes, unlike other members of the canonical GST family, which are mainly cytosolic. The biological substrates of GSTK are not yet known. It is presumed to have a protective role during respiration when large amounts of reactive oxygen species are generated. GSTK has the same general fold as DsbA, consisting of a thioredoxin domain interrupted by an alpha-helical domain and its biological unit is a homodimer. GSTK is closely related to the bacterial enzyme, 2-hydroxychromene-2-carboxylate (HCCA) isomerase. It shows little sequence similarity to the other members of the GST family.


Pssm-ID: 239319 [Multi-domain]  Cd Length: 209  Bit Score: 319.30  E-value: 5.21e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705704    6 RTVELFYDVLSPYSWLGFEILCRYQNIWNINLQLRPSLITGIMKDSGNKPPGLLPRKGLYMANDLKLLRHHLQIPIHFPK 85
Cdd:cd03021   1 PKIELYYDVVSPYSYLAFEVLCRYQTAWNVDITYVPVFLGGIMKDSGNKPPIMLPNKAKYMAKDRKRSAEFFGVPIRQPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705704   86 DFLSVmlEKGSLSAMRFLTAVNLEHPE----MLEKASRELWMRVWSRNEDITEPQSILAAAEKAGMSAEQAQGLLEKIAT 161
Cdd:cd03021  81 DFFFM--KKGTLTAQRFLTAISEQHPEstltALEALFREFWVRPWSLTEPITESQSISVAADKLGGSAEQAEKLLKAAST 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 7705704  162 PKVKNQLKETTEAACRYGAFGLPITVAHVD-GQTHMLFGSDRMELLAHLLG 211
Cdd:cd03021 159 PEVKNRLKENTDEALKYGAFGLPWIVVTNDkGKTEMFFGSDRFEQVADFLG 209
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 7-211 1.77e-63

DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a thioredoxin-like structure pfam00085. This family also includes 2-hydroxychromene-2-carboxylate (HCCA) isomerase enzymes catalyze one step in prokaryotic polyaromatic hydrocarbon (PAH) catabolic pathways. This family also contains members with functions other than HCCA isomerization, such as Kappa family GSTs, whose similarity to HCCA isomerases was not previously recognized. The sequence Swiss:O07298 has been annotated as a dioxygenase but is almost certainly an HCCA isomerase enzyme. Similarly, the sequence Swiss:Q9ZI67 has been annotated as a dehydrogenase, but is most probably also an HCCA isomerase enzyme. In addition, the Rhizobium leguminosarum Swiss:Q52782 protein has been annotated as a putative glycerol-3-phosphate transfer protein, but is also most likely to be an HCCA isomerase enzyme.


Pssm-ID: 426200 [Multi-domain]  Cd Length: 191  Bit Score: 195.72  E-value: 1.77e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705704      7 TVELFYDVLSPYSWLGFEILCRYQNIW-NINLQLRPSLITGIMKdSGNKPPGLLPRKGLYMANDLKLLRHHLQIPIHFPK 85
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYgDVKVVYRPFPLAGAKK-IGNVGPSNLPVKLKYMMADLERWAALYGIPLRFPA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705704     86 DFLsvmleKGSLSAMRFLTAVNLEHpeMLEKASRELWMRVWSRNEDITEPQSILAAAEKAGMSAEQaqgLLEKIATPKVK 165
Cdd:pfam01323  80 NFL-----GNSTRANRLALAAGAEG--LAEKVVRELFNALWGEGAAITDDSVLREVAEKAGLDAEE---FDEFLDSPAVK 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 7705704    166 NQLKETTEAACRYGAFGLPITVahVDGQthMLFGSDRMELLAHLLG 211
Cdd:pfam01323 150 EAVRENTAAAISLGVFGVPTFV--VGGK--MVFGADRLDTLADALA 191
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
 7-214 7.25e-08

Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442047 [Multi-domain]  Cd Length: 205  Bit Score: 51.04  E-value: 7.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705704    7 TVELFYDVLSPYSWLGFEILCRYQNIWNINLQL--RPSLITGIMKDSGNKPPGLLPRKGLY-----MANDLKLLRHHLQI 79
Cdd:COG2761   3 KIDIFSDVVCPWCYIGKRRLEKALAEFGDDVEIrwRPFELNPDMPPEGEDRREYLLAKGSPeqaeqMRAHVEEAAAEEGL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705704   80 PIHFPKdflsvMLEKGSLSAMRFLTAVNLE--HPEMLEKasreLWMRVWSRNEDITEPQSILAAAEKAGMSAEQAQGLLE 157
Cdd:COG2761  83 PFDFDR-----IKPPNTFDAHRLLKAAELQgkQDALLEA----LFEAYFTEGRDIGDREVLLDLAAEVGLDAEEFRADLE 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 7705704  158 kiaTPKVKNQLKETTEAACRYGAFGLPITVahVDGQtHMLFGSDRMELLAHLLGEKW 214
Cdd:COG2761 154 ---SDEAAAAVRADEAEARELGVTGVPTFV--FDGK-YAVSGAQPYEVFEQALRQAL 204
 
Name Accession Description Interval E-value
DsbA_GSTK cd03021
DsbA family, Glutathione (GSH) S-transferase Kappa (GSTK) subfamily; GSTK is a member of the ...
 6-211 5.21e-112

DsbA family, Glutathione (GSH) S-transferase Kappa (GSTK) subfamily; GSTK is a member of the GST family of enzymes which catalyzes the transfer of the thiol of GSH to electrophilic substrates. It is specifically located in the mitochondria and peroxisomes, unlike other members of the canonical GST family, which are mainly cytosolic. The biological substrates of GSTK are not yet known. It is presumed to have a protective role during respiration when large amounts of reactive oxygen species are generated. GSTK has the same general fold as DsbA, consisting of a thioredoxin domain interrupted by an alpha-helical domain and its biological unit is a homodimer. GSTK is closely related to the bacterial enzyme, 2-hydroxychromene-2-carboxylate (HCCA) isomerase. It shows little sequence similarity to the other members of the GST family.


Pssm-ID: 239319 [Multi-domain]  Cd Length: 209  Bit Score: 319.30  E-value: 5.21e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705704    6 RTVELFYDVLSPYSWLGFEILCRYQNIWNINLQLRPSLITGIMKDSGNKPPGLLPRKGLYMANDLKLLRHHLQIPIHFPK 85
Cdd:cd03021   1 PKIELYYDVVSPYSYLAFEVLCRYQTAWNVDITYVPVFLGGIMKDSGNKPPIMLPNKAKYMAKDRKRSAEFFGVPIRQPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705704   86 DFLSVmlEKGSLSAMRFLTAVNLEHPE----MLEKASRELWMRVWSRNEDITEPQSILAAAEKAGMSAEQAQGLLEKIAT 161
Cdd:cd03021  81 DFFFM--KKGTLTAQRFLTAISEQHPEstltALEALFREFWVRPWSLTEPITESQSISVAADKLGGSAEQAEKLLKAAST 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 7705704  162 PKVKNQLKETTEAACRYGAFGLPITVAHVD-GQTHMLFGSDRMELLAHLLG 211
Cdd:cd03021 159 PEVKNRLKENTDEALKYGAFGLPWIVVTNDkGKTEMFFGSDRFEQVADFLG 209
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 7-211 1.77e-63

DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a thioredoxin-like structure pfam00085. This family also includes 2-hydroxychromene-2-carboxylate (HCCA) isomerase enzymes catalyze one step in prokaryotic polyaromatic hydrocarbon (PAH) catabolic pathways. This family also contains members with functions other than HCCA isomerization, such as Kappa family GSTs, whose similarity to HCCA isomerases was not previously recognized. The sequence Swiss:O07298 has been annotated as a dioxygenase but is almost certainly an HCCA isomerase enzyme. Similarly, the sequence Swiss:Q9ZI67 has been annotated as a dehydrogenase, but is most probably also an HCCA isomerase enzyme. In addition, the Rhizobium leguminosarum Swiss:Q52782 protein has been annotated as a putative glycerol-3-phosphate transfer protein, but is also most likely to be an HCCA isomerase enzyme.


Pssm-ID: 426200 [Multi-domain]  Cd Length: 191  Bit Score: 195.72  E-value: 1.77e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705704      7 TVELFYDVLSPYSWLGFEILCRYQNIW-NINLQLRPSLITGIMKdSGNKPPGLLPRKGLYMANDLKLLRHHLQIPIHFPK 85
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYgDVKVVYRPFPLAGAKK-IGNVGPSNLPVKLKYMMADLERWAALYGIPLRFPA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705704     86 DFLsvmleKGSLSAMRFLTAVNLEHpeMLEKASRELWMRVWSRNEDITEPQSILAAAEKAGMSAEQaqgLLEKIATPKVK 165
Cdd:pfam01323  80 NFL-----GNSTRANRLALAAGAEG--LAEKVVRELFNALWGEGAAITDDSVLREVAEKAGLDAEE---FDEFLDSPAVK 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 7705704    166 NQLKETTEAACRYGAFGLPITVahVDGQthMLFGSDRMELLAHLLG 211
Cdd:pfam01323 150 EAVRENTAAAISLGVFGVPTFV--VGGK--MVFGADRLDTLADALA 191
DsbA_HCCA_Iso cd03022
DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a ...
 8-210 3.71e-35

DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a glutathione (GSH) dependent enzyme involved in the naphthalene catabolic pathway. It converts HCCA, a hemiketal formed spontaneously after ring cleavage of 1,2-dihydroxynapthalene by a dioxygenase, into cis-o-hydroxybenzylidenepyruvate (cHBPA). This is the fourth reaction in a six-step pathway that converts napthalene into salicylate. HCCA isomerase is unique to bacteria that degrade polycyclic aromatic compounds. It is closely related to the eukaryotic protein, GSH transferase kappa (GSTK).


Pssm-ID: 239320 [Multi-domain]  Cd Length: 192  Bit Score: 123.12  E-value: 3.71e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705704    8 VELFYDVLSPYSWLGFE----ILCRYqniwNINLQLRPSLITGIMKDSGNKPPG-LLPRKGLYMANDLKLLRHHLQIPIH 82
Cdd:cd03022   1 IDFYFDFSSPYSYLAHErlpaLAARH----GATVRYRPILLGGVFKATGNVPPAnRPPAKGRYRLRDLERWARRYGIPLR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705704   83 FPKDFlsvmlEKGSLSAMRFLTAVNLEHPEMLEKAsRELWMRVWSRNEDITEPQSILAAAEKAGMSAEQaqgLLEKIATP 162
Cdd:cd03022  77 FPPRF-----PPNTLRAMRAALAAQAEGDAAEAFA-RAVFRALWGEGLDIADPAVLAAVAAAAGLDADE---LLAAADDP 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 7705704  163 KVKNQLKETTEAACRYGAFGLPITVahVDGQthMLFGSDRMELLAHLL 210
Cdd:cd03022 148 AVKAALRANTEEAIARGVFGVPTFV--VDGE--MFWGQDRLDMLEEAL 191
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
 7-214 7.25e-08

Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442047 [Multi-domain]  Cd Length: 205  Bit Score: 51.04  E-value: 7.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705704    7 TVELFYDVLSPYSWLGFEILCRYQNIWNINLQL--RPSLITGIMKDSGNKPPGLLPRKGLY-----MANDLKLLRHHLQI 79
Cdd:COG2761   3 KIDIFSDVVCPWCYIGKRRLEKALAEFGDDVEIrwRPFELNPDMPPEGEDRREYLLAKGSPeqaeqMRAHVEEAAAEEGL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705704   80 PIHFPKdflsvMLEKGSLSAMRFLTAVNLE--HPEMLEKasreLWMRVWSRNEDITEPQSILAAAEKAGMSAEQAQGLLE 157
Cdd:COG2761  83 PFDFDR-----IKPPNTFDAHRLLKAAELQgkQDALLEA----LFEAYFTEGRDIGDREVLLDLAAEVGLDAEEFRADLE 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 7705704  158 kiaTPKVKNQLKETTEAACRYGAFGLPITVahVDGQtHMLFGSDRMELLAHLLGEKW 214
Cdd:COG2761 154 ---SDEAAAAVRADEAEARELGVTGVPTFV--FDGK-YAVSGAQPYEVFEQALRQAL 204
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 8-49 2.00e-03

DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) S-transferase kappa (GSTK), 2-hydroxychromene-2-carboxylate (HCCA) isomerase, an oxidoreductase (FrnE) presumed to be involved in frenolicin biosynthesis, a 27-kDa outer membrane protein, and similar proteins. Members of this family contain a redox active CXXC motif (except GSTK and HCCA isomerase) imbedded in a TRX fold, and an alpha helical insert of about 75 residues (shorter in DsbC and DsbG) relative to TRX. DsbA is involved in the oxidative protein folding pathway in prokaryotes, catalyzing disulfide bond formation of proteins secreted into the bacterial periplasm. DsbC and DsbG function as protein disulfide isomerases and chaperones to correct non-native disulfide bonds formed by DsbA and prevent aggregation of incorrectly folded proteins.


Pssm-ID: 239270 [Multi-domain]  Cd Length: 98  Bit Score: 36.61  E-value: 2.00e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 7705704    8 VELFYDVLSPYSWLGFEILCRYQNI--WNINLQLRPSLITGIMK 49
Cdd:cd02972   1 IVEFFDPLCPYCYLFEPELEKLLYAddGGVRVVYRPFPLLGGMP 44
 
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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