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Conserved domains on  [gi|1502825457|ref|WP_122366996|]
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glutathione S-transferase family protein [Pseudomonas coronafaciens]

Protein Classification

glutathione S-transferase family protein( domain architecture ID 11427749)

glutathione S-transferase (GST) family protein may catalyze 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:  1.20.1050.10|3.40.30.10
EC:  2.5.1.-
Gene Ontology:  GO:0006749|GO:0005515
PubMed:  11035031
SCOP:  4000976|4000472

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
4-216 1.93e-17

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


:

Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 79.17  E-value: 1.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502825457   4 LILHHYPTSLFAEKARLMLGFKGLAWRSVTI---PSIMPKPDLTALTgGYRRTPVLQAGADIYCDTALMARRLEQEKASP 80
Cdd:COG0625     2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVdlaKGEQKSPEFLALN-PLGKVPVLVDDGLVLTESLAILEYLAERYPEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502825457  81 AFFPQG-QEFAVA-GLAAWADSVlFMHAVSLVFQpesmavRFAKVPADAAkafiadrstlfnggtasrppVEQVKHQWPT 158
Cdd:COG0625    81 PLLPADpAARARVrQWLAWADGD-LHPALRNLLE------RLAPEKDPAA--------------------IARARAELAR 133

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1502825457 159 LMSRLELQLSrGGAFLFGE-PSIADFSVAHTLWFLKQTPVTAPfvyDYPSVSVWLDRVL 216
Cdd:COG0625   134 LLAVLEARLA-GGPYLAGDrFSIADIALAPVLRRLDRLGLDLA---DYPNLAAWLARLA 188
 
Name Accession Description Interval E-value
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
4-216 1.93e-17

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 79.17  E-value: 1.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502825457   4 LILHHYPTSLFAEKARLMLGFKGLAWRSVTI---PSIMPKPDLTALTgGYRRTPVLQAGADIYCDTALMARRLEQEKASP 80
Cdd:COG0625     2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVdlaKGEQKSPEFLALN-PLGKVPVLVDDGLVLTESLAILEYLAERYPEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502825457  81 AFFPQG-QEFAVA-GLAAWADSVlFMHAVSLVFQpesmavRFAKVPADAAkafiadrstlfnggtasrppVEQVKHQWPT 158
Cdd:COG0625    81 PLLPADpAARARVrQWLAWADGD-LHPALRNLLE------RLAPEKDPAA--------------------IARARAELAR 133

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1502825457 159 LMSRLELQLSrGGAFLFGE-PSIADFSVAHTLWFLKQTPVTAPfvyDYPSVSVWLDRVL 216
Cdd:COG0625   134 LLAVLEARLA-GGPYLAGDrFSIADIALAPVLRRLDRLGLDLA---DYPNLAAWLARLA 188
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
6-75 1.13e-10

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 56.85  E-value: 1.13e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502825457   6 LHHYPTSLFAEKARLMLGFKGLAWRSVTIPSIMPKPDLTALTgGYRRTPVLQAGADIYCDTALMARRLEQ 75
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKN-PLGKVPVLEDDGGILCESLAIIDYLEE 69
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 125-215 2.96e-08

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: 50.58  E-value: 2.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502825457 125 ADAAKAFIADRSTLFNGGTASRPPVEQVKHQWPTLMSRLELQLSRGGAFLFGEPSIADFSVAHTLWFLKQTPVTAPFVYD 204
Cdd:cd00299    10 ATLAPPLVRLLYLEKVPLPKDEAAVEAAREELPALLAALEQLLAGRPYLAGDQFSLADVALAPVLARLEALGPYYDLLDE 89

                          90
                  ....*....|.
gi 1502825457 205 YPSVSVWLDRV 215
Cdd:cd00299    90 YPRLKAWYDRL 100
 
Name Accession Description Interval E-value
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
4-216 1.93e-17

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 79.17  E-value: 1.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502825457   4 LILHHYPTSLFAEKARLMLGFKGLAWRSVTI---PSIMPKPDLTALTgGYRRTPVLQAGADIYCDTALMARRLEQEKASP 80
Cdd:COG0625     2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVdlaKGEQKSPEFLALN-PLGKVPVLVDDGLVLTESLAILEYLAERYPEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502825457  81 AFFPQG-QEFAVA-GLAAWADSVlFMHAVSLVFQpesmavRFAKVPADAAkafiadrstlfnggtasrppVEQVKHQWPT 158
Cdd:COG0625    81 PLLPADpAARARVrQWLAWADGD-LHPALRNLLE------RLAPEKDPAA--------------------IARARAELAR 133

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1502825457 159 LMSRLELQLSrGGAFLFGE-PSIADFSVAHTLWFLKQTPVTAPfvyDYPSVSVWLDRVL 216
Cdd:COG0625   134 LLAVLEARLA-GGPYLAGDrFSIADIALAPVLRRLDRLGLDLA---DYPNLAAWLARLA 188
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
6-75 1.13e-10

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 56.85  E-value: 1.13e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502825457   6 LHHYPTSLFAEKARLMLGFKGLAWRSVTIPSIMPKPDLTALTgGYRRTPVLQAGADIYCDTALMARRLEQ 75
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKN-PLGKVPVLEDDGGILCESLAIIDYLEE 69
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 125-215 2.96e-08

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: 50.58  E-value: 2.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502825457 125 ADAAKAFIADRSTLFNGGTASRPPVEQVKHQWPTLMSRLELQLSRGGAFLFGEPSIADFSVAHTLWFLKQTPVTAPFVYD 204
Cdd:cd00299    10 ATLAPPLVRLLYLEKVPLPKDEAAVEAAREELPALLAALEQLLAGRPYLAGDQFSLADVALAPVLARLEALGPYYDLLDE 89

                          90
                  ....*....|.
gi 1502825457 205 YPSVSVWLDRV 215
Cdd:cd00299    90 YPRLKAWYDRL 100
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 160-214 2.47e-05

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 41.54  E-value: 2.47e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1502825457 160 MSRLELQLSRGGAFLFGEPSIADFSVAHTLWFLKQTPVTAPFVYDYPSVSVWLDR 214
Cdd:pfam13410  13 LDALEARLADGPGLLGDRPTLADIALAPVLARLDAAYPGLDLREGYPRLRAWLER 67
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 4-74 1.35e-04

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: 39.48  E-value: 1.35e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1502825457   4 LILHHYPTSLFAEKARLMLGFKGLAWRSVTI-PSIMPKPDLTALTgGYRRTPVLQAGADIYCDTALMARRLE 74
Cdd:cd00570     1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVdLGEGEQEEFLALN-PLGKVPVLEDGGLVLTESLAILEYLA 71
 
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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