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Conserved domains on  [gi|225205307|gb|EEG87661|]
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hypothetical protein PROPEN_00204 [Proteus penneri ATCC 35198]

Protein Classification

glutathione S-transferase family protein( domain architecture ID 2054)

glutathione S-transferase (GST) family protein similar to Lactiplantibacillus plantarum glutathione S-transferase that 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_family super family cl02776
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 11-75 5.20e-07

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.


The actual alignment was detected with superfamily member cd03207:

Pssm-ID: 470672 [Multi-domain]  Cd Length: 101  Bit Score: 43.82  E-value: 5.20e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225205307  11 EQQKSSGFGSFERAFHCLETGIAsANPYICGKNLTAVDVYVGYFLIFLCKYALIQPTPLINQYLD 75
Cdd:cd03207   31 EPAIAAAYGDLDERLAALEAALA-GRPYLVGERFSAADLLLASVLRWARAFGLLPEYPALRAYVA 94
 
Name Accession Description Interval E-value
GST_C_8 cd03207
C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; ...
 11-75 5.20e-07

C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 8; composed of Agrobacterium tumefaciens GST and other 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 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 three-dimensional structure of Agrobacterium tumefaciens GST has been determined but there is no information on its functional characterization.


Pssm-ID: 198316 [Multi-domain]  Cd Length: 101  Bit Score: 43.82  E-value: 5.20e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225205307  11 EQQKSSGFGSFERAFHCLETGIAsANPYICGKNLTAVDVYVGYFLIFLCKYALIQPTPLINQYLD 75
Cdd:cd03207   31 EPAIAAAYGDLDERLAALEAALA-GRPYLVGERFSAADLLLASVLRWARAFGLLPEYPALRAYVA 94
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
21-78 9.90e-03

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 33.33  E-value: 9.90e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 225205307  21 FERAFHCLETGIAsANPYICGKNLTAVDVYVGYFLIFLCKYAL-IQPTPLINQYLDSLA 78
Cdd:COG0625  131 LARLLAVLEARLA-GGPYLAGDRFSIADIALAPVLRRLDRLGLdLADYPNLAAWLARLA 188
 
Name Accession Description Interval E-value
GST_C_8 cd03207
C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; ...
 11-75 5.20e-07

C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 8; composed of Agrobacterium tumefaciens GST and other 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 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 three-dimensional structure of Agrobacterium tumefaciens GST has been determined but there is no information on its functional characterization.


Pssm-ID: 198316 [Multi-domain]  Cd Length: 101  Bit Score: 43.82  E-value: 5.20e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225205307  11 EQQKSSGFGSFERAFHCLETGIAsANPYICGKNLTAVDVYVGYFLIFLCKYALIQPTPLINQYLD 75
Cdd:cd03207   31 EPAIAAAYGDLDERLAALEAALA-GRPYLVGERFSAADLLLASVLRWARAFGLLPEYPALRAYVA 94
GST_C_Omega_like cd03190
C-terminal, alpha helical domain of Class Omega-like Glutathione S-transferases; Glutathione ...
 34-84 6.74e-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: 33.32  E-value: 6.74e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 225205307  34 SANPYICGKNLTAVDVY---------VGYFLIFLCKYALIQPTPLINQYLDSLALNNEIK 84
Cdd:cd03190   54 SKQPYLLGDRLTEADIRlfttlirfdPVYHQHFKCNLKTIRDYPNLWRYLRRLYQNPGVF 113
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
21-78 9.90e-03

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 33.33  E-value: 9.90e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 225205307  21 FERAFHCLETGIAsANPYICGKNLTAVDVYVGYFLIFLCKYAL-IQPTPLINQYLDSLA 78
Cdd:COG0625  131 LARLLAVLEARLA-GGPYLAGDRFSIADIALAPVLRRLDRLGLdLADYPNLAAWLARLA 188
 
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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