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Conserved domains on  [gi|528504353|ref|XP_005158401|]
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glutathione S-transferase kappa 1 isoform X1 [Danio rerio]

Protein Classification

DsbA_GSTK domain-containing protein( domain architecture ID 10122488)

DsbA_GSTK domain-containing protein

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 ...
 6-214 7.09e-109

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: 311.59  E-value: 7.09e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504353   6 KVVELFYDVVSPYSWLAFEVLCRYRNVWNIDLKLKPAFLGAVMHDSGNRPPGMIPNKFLYMTSDLKHVSEYFGVPVRQPS 85
Cdd:cd03021    1 PKIELYYDVVSPYSYLAFEVLCRYQTAWNVDITYVPVFLGGIMKDSGNKPPIMLPNKAKYMAKDRKRSAEFFGVPIRQPK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504353  86 NVFETmfEKGSLKAMRFVTAVAEKEKEGDV-KLERVSRELWNRIWSNDQDITLPASFAEAGLKAGLTASEVDELLTLATS 164
Cdd:cd03021   81 DFFFM--KKGTLTAQRFLTAISEQHPESTLtALEALFREFWVRPWSLTEPITESQSISVAADKLGGSAEQAEKLLKAAST 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528504353 165 QPIKDKLKSVTSEAIKYKCFGFPTIVCHVD-GKPEIFFGSDRFEVMAHIIG 214
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 ...
 6-214 7.09e-109

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: 311.59  E-value: 7.09e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504353   6 KVVELFYDVVSPYSWLAFEVLCRYRNVWNIDLKLKPAFLGAVMHDSGNRPPGMIPNKFLYMTSDLKHVSEYFGVPVRQPS 85
Cdd:cd03021    1 PKIELYYDVVSPYSYLAFEVLCRYQTAWNVDITYVPVFLGGIMKDSGNKPPIMLPNKAKYMAKDRKRSAEFFGVPIRQPK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504353  86 NVFETmfEKGSLKAMRFVTAVAEKEKEGDV-KLERVSRELWNRIWSNDQDITLPASFAEAGLKAGLTASEVDELLTLATS 164
Cdd:cd03021   81 DFFFM--KKGTLTAQRFLTAISEQHPESTLtALEALFREFWVRPWSLTEPITESQSISVAADKLGGSAEQAEKLLKAAST 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528504353 165 QPIKDKLKSVTSEAIKYKCFGFPTIVCHVD-GKPEIFFGSDRFEVMAHIIG 214
Cdd:cd03021  159 PEVKNRLKENTDEALKYGAFGLPWIVVTNDkGKTEMFFGSDRFEQVADFLG 209
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 7-214 6.81e-45

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: 148.35  E-value: 6.81e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504353    7 VVELFYDVVSPYSWLAFEVLCRYRNVW-NIDLKLKPAFLGAVMhDSGNRPPGMIPNKFLYMTSDLKHVSEYFGVPVRqps 85
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYgDVKVVYRPFPLAGAK-KIGNVGPSNLPVKLKYMMADLERWAALYGIPLR--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504353   86 nvFETMFEKGSLKAMRFVTAVAEKEKegdvkLERVSRELWNRIWSNDQDITLPASFAEAGLKAGLTASEVDELLtlaTSQ 165
Cdd:pfam01323  77 --FPANFLGNSTRANRLALAAGAEGL-----AEKVVRELFNALWGEGAAITDDSVLREVAEKAGLDAEEFDEFL---DSP 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 528504353  166 PIKDKLKSVTSEAIKYKCFGFPTIVchVDGKpeIFFGSDRFEVMAHIIG 214
Cdd:pfam01323 147 AVKEAVRENTAAAISLGVFGVPTFV--VGGK--MVFGADRLDTLADALA 191
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
 8-196 1.48e-05

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: 44.49  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504353   8 VELFYDVVSPYSWLAFEVLCRYRNVWNIDLKL--KPAFLGAVMHDSGNRPP-----GMIPNKFLYMTSDLKHVSEYFGVP 80
Cdd:COG2761    4 IDIFSDVVCPWCYIGKRRLEKALAEFGDDVEIrwRPFELNPDMPPEGEDRReyllaKGSPEQAEQMRAHVEEAAAEEGLP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504353  81 VRqpsnvFETMFEKGSLKAMRFVTAVAEKEKEGDVKlervsRELWNRIWSNDQDITLPASFAEAGLKAGLTASEVDELLt 160
Cdd:COG2761   84 FD-----FDRIKPPNTFDAHRLLKAAELQGKQDALL-----EALFEAYFTEGRDIGDREVLLDLAAEVGLDAEEFRADL- 152

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 528504353 161 laTSQPIKDKLKSVTSEAIKYKCFGFPTIVchVDGK 196
Cdd:COG2761  153 --ESDEAAAAVRADEAEARELGVTGVPTFV--FDGK 184
 
Name Accession Description Interval E-value
DsbA_GSTK cd03021
DsbA family, Glutathione (GSH) S-transferase Kappa (GSTK) subfamily; GSTK is a member of the ...
 6-214 7.09e-109

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: 311.59  E-value: 7.09e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504353   6 KVVELFYDVVSPYSWLAFEVLCRYRNVWNIDLKLKPAFLGAVMHDSGNRPPGMIPNKFLYMTSDLKHVSEYFGVPVRQPS 85
Cdd:cd03021    1 PKIELYYDVVSPYSYLAFEVLCRYQTAWNVDITYVPVFLGGIMKDSGNKPPIMLPNKAKYMAKDRKRSAEFFGVPIRQPK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504353  86 NVFETmfEKGSLKAMRFVTAVAEKEKEGDV-KLERVSRELWNRIWSNDQDITLPASFAEAGLKAGLTASEVDELLTLATS 164
Cdd:cd03021   81 DFFFM--KKGTLTAQRFLTAISEQHPESTLtALEALFREFWVRPWSLTEPITESQSISVAADKLGGSAEQAEKLLKAAST 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528504353 165 QPIKDKLKSVTSEAIKYKCFGFPTIVCHVD-GKPEIFFGSDRFEVMAHIIG 214
Cdd:cd03021  159 PEVKNRLKENTDEALKYGAFGLPWIVVTNDkGKTEMFFGSDRFEQVADFLG 209
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 7-214 6.81e-45

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: 148.35  E-value: 6.81e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504353    7 VVELFYDVVSPYSWLAFEVLCRYRNVW-NIDLKLKPAFLGAVMhDSGNRPPGMIPNKFLYMTSDLKHVSEYFGVPVRqps 85
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYgDVKVVYRPFPLAGAK-KIGNVGPSNLPVKLKYMMADLERWAALYGIPLR--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504353   86 nvFETMFEKGSLKAMRFVTAVAEKEKegdvkLERVSRELWNRIWSNDQDITLPASFAEAGLKAGLTASEVDELLtlaTSQ 165
Cdd:pfam01323  77 --FPANFLGNSTRANRLALAAGAEGL-----AEKVVRELFNALWGEGAAITDDSVLREVAEKAGLDAEEFDEFL---DSP 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 528504353  166 PIKDKLKSVTSEAIKYKCFGFPTIVchVDGKpeIFFGSDRFEVMAHIIG 214
Cdd:pfam01323 147 AVKEAVRENTAAAISLGVFGVPTFV--VGGK--MVFGADRLDTLADALA 191
DsbA_HCCA_Iso cd03022
DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a ...
 8-211 1.81e-39

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: 134.68  E-value: 1.81e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504353   8 VELFYDVVSPYSWLA---FEVLCRYRNVwniDLKLKPAFLGAVMHDSGNRPPGMIP-NKFLYMTSDLKHVSEYFGVPVRQ 83
Cdd:cd03022    1 IDFYFDFSSPYSYLAherLPALAARHGA---TVRYRPILLGGVFKATGNVPPANRPpAKGRYRLRDLERWARRYGIPLRF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504353  84 PSNvfetmFEKGSLKAMRFVTAVAEKekegDVKLERVSRELWNRIWSNDQDITLPASFAEAGLKAGLTAsevDELLTLAT 163
Cdd:cd03022   78 PPR-----FPPNTLRAMRAALAAQAE----GDAAEAFARAVFRALWGEGLDIADPAVLAAVAAAAGLDA---DELLAAAD 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 528504353 164 SQPIKDKLKSVTSEAIKYKCFGFPTIVchVDGkpEIFFGSDRFEVMAH 211
Cdd:cd03022  146 DPAVKAALRANTEEAIARGVFGVPTFV--VDG--EMFWGQDRLDMLEE 189
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
 8-196 1.48e-05

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: 44.49  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504353   8 VELFYDVVSPYSWLAFEVLCRYRNVWNIDLKL--KPAFLGAVMHDSGNRPP-----GMIPNKFLYMTSDLKHVSEYFGVP 80
Cdd:COG2761    4 IDIFSDVVCPWCYIGKRRLEKALAEFGDDVEIrwRPFELNPDMPPEGEDRReyllaKGSPEQAEQMRAHVEEAAAEEGLP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504353  81 VRqpsnvFETMFEKGSLKAMRFVTAVAEKEKEGDVKlervsRELWNRIWSNDQDITLPASFAEAGLKAGLTASEVDELLt 160
Cdd:COG2761   84 FD-----FDRIKPPNTFDAHRLLKAAELQGKQDALL-----EALFEAYFTEGRDIGDREVLLDLAAEVGLDAEEFRADL- 152

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 528504353 161 laTSQPIKDKLKSVTSEAIKYKCFGFPTIVchVDGK 196
Cdd:COG2761  153 --ESDEAAAAVRADEAEARELGVTGVPTFV--FDGK 184
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 8-49 2.82e-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: 36.23  E-value: 2.82e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 528504353   8 VELFYDVVSPYSWLAFEVLCR--YRNVWNIDLKLKPAFLGAVMH 49
Cdd:cd02972    1 IVEFFDPLCPYCYLFEPELEKllYADDGGVRVVYRPFPLLGGMP 44
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
 138-213 7.28e-03

DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein containing a redox active CXXC motif imbedded in a TRX fold. It is involved in the oxidative protein folding pathway in prokaryotes, and is the strongest thiol oxidant known, due to the unusual stability of the thiolate anion form of the first cysteine in the CXXC motif. The highly unstable oxidized form of DsbA directly donates disulfide bonds to reduced proteins secreted into the bacterial periplasm. This rapid and unidirectional process helps to catalyze the folding of newly-synthesized polypeptides. To regain catalytic activity, reduced DsbA is then reoxidized by the membrane protein DsbB, which generates its disulfides from oxidized quinones, which in turn are reoxidized by the electron transport chain.


Pssm-ID: 239317 [Multi-domain]  Cd Length: 178  Bit Score: 36.11  E-value: 7.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504353 138 PASFAEAGLKAGLTASEVDELLTlatSQPIKDKLKSVTSEAIKYKCFGFPTIVchVDGK----PEIFFGSDRFEVMAHII 213
Cdd:cd03019   99 PDDIRKIFLSQGVDKKKFDAAYN---SFSVKALVAKAEKLAKKYKITGVPAFV--VNGKyvvnPSAIGGDDTLQVLDELI 173
 
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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