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Conserved domains on  [gi|976677613|gb|KVF73115|]
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glutathione S-transferase [Burkholderia vietnamiensis]

Protein Classification

glutathione S-transferase( domain architecture ID 10122718)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GST_C_GTT2_like cd03182
C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione ...
 104-220 5.25e-56

C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly uncharacterized proteins with similarity to the Saccharomyces cerevisiae GST protein, GTT2. 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. GTT2, a homodimer, exhibits GST activity with standard substrates. Strains with deleted GTT2 genes are viable but exhibit increased sensitivity to heat shock.


:

Pssm-ID: 198291 [Multi-domain]  Cd Length: 116  Bit Score: 174.05  E-value: 5.25e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613 104 TPLEKGVIHMMSKRAELELLDAISVYFHHATPGLGPnVELYQNAEWGLRQRDKALRGMHYFNDVLKRQPFVAGDAFSMAD 183
Cdd:cd03182    1 TPLEKALIEMWQRRAELQGLAPVFQAFRHATPGLKP-DREVQVPEWGERNKKRVIDFLPVLDKRLAESPYVAGDRFSIAD 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 976677613 184 ITVIGGLVFASIVKLPVPTECEALVDWYVRMRQRPSV 220
Cdd:cd03182   80 ITAFVALDFAKNLKLPVPEELTALRRWYERMAARPSA 116
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
 16-92 5.05e-34

GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly uncharacterized proteins with similarity to the S. cerevisiae GST protein, GTT2. 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. GTT2, a homodimer, exhibits GST activity with standard substrates. Strains with deleted GTT2 genes are viable but exhibit increased sensitivity to heat shock.


:

Pssm-ID: 239349 [Multi-domain]  Cd Length: 74  Bit Score: 116.63  E-value: 5.05e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 976677613  16 MTIYDFPKGPYPTRVRIALAEKGLRsrVEFVMVDLYKGEHKRPEFISeKNYSGTLPVLELEDGTCIAECTAITEYLD 92
Cdd:cd03051    1 MKLYDSPTAPNPRRVRIFLAEKGID--VPLVTVDLAAGEQRSPEFLA-KNPAGTVPVLELDDGTVITESVAICRYLE 74
 
Name Accession Description Interval E-value
GST_C_GTT2_like cd03182
C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione ...
 104-220 5.25e-56

C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly uncharacterized proteins with similarity to the Saccharomyces cerevisiae GST protein, GTT2. 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. GTT2, a homodimer, exhibits GST activity with standard substrates. Strains with deleted GTT2 genes are viable but exhibit increased sensitivity to heat shock.


Pssm-ID: 198291 [Multi-domain]  Cd Length: 116  Bit Score: 174.05  E-value: 5.25e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613 104 TPLEKGVIHMMSKRAELELLDAISVYFHHATPGLGPnVELYQNAEWGLRQRDKALRGMHYFNDVLKRQPFVAGDAFSMAD 183
Cdd:cd03182    1 TPLEKALIEMWQRRAELQGLAPVFQAFRHATPGLKP-DREVQVPEWGERNKKRVIDFLPVLDKRLAESPYVAGDRFSIAD 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 976677613 184 ITVIGGLVFASIVKLPVPTECEALVDWYVRMRQRPSV 220
Cdd:cd03182   80 ITAFVALDFAKNLKLPVPEELTALRRWYERMAARPSA 116
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
16-221 2.93e-46

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 152.36  E-value: 2.93e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613  16 MTIYDFPKGPYPTRVRIALAEKGLRsrVEFVMVDLYKGEHKRPEFIsEKNYSGTLPVLElEDGTCIAECTAITEYLDTLD 95
Cdd:COG0625    2 MKLYGSPPSPNSRRVRIALEEKGLP--YELVPVDLAKGEQKSPEFL-ALNPLGKVPVLV-DDGLVLTESLAILEYLAERY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613  96 GAPTLTGRTPLEKGVIHMMSKRAELELLDAISVYFHHATPGlgpnvelyQNAEWGLRQRDKALRGMHYFNDVLKRQPFVA 175
Cdd:COG0625   78 PEPPLLPADPAARARVRQWLAWADGDLHPALRNLLERLAPE--------KDPAAIARARAELARLLAVLEARLAGGPYLA 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 976677613 176 GDAFSMADITVIGGLVFASIVKLPVPtECEALVDWYVRMRQRPSVK 221
Cdd:COG0625  150 GDRFSIADIALAPVLRRLDRLGLDLA-DYPNLAAWLARLAARPAFQ 194
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
 16-92 5.05e-34

GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly uncharacterized proteins with similarity to the S. cerevisiae GST protein, GTT2. 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. GTT2, a homodimer, exhibits GST activity with standard substrates. Strains with deleted GTT2 genes are viable but exhibit increased sensitivity to heat shock.


Pssm-ID: 239349 [Multi-domain]  Cd Length: 74  Bit Score: 116.63  E-value: 5.05e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 976677613  16 MTIYDFPKGPYPTRVRIALAEKGLRsrVEFVMVDLYKGEHKRPEFISeKNYSGTLPVLELEDGTCIAECTAITEYLD 92
Cdd:cd03051    1 MKLYDSPTAPNPRRVRIFLAEKGID--VPLVTVDLAAGEQRSPEFLA-KNPAGTVPVLELDDGTVITESVAICRYLE 74
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 16-92 1.66e-14

Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to a variety of targets. Also included in the alignment, but not GSTs: S-crystallins from squid (similarity to GST previously noted); eukaryotic elongation factors 1-gamma (not known to have GST activity and similarity not previously recognized); HSP26 family of stress-related proteins including auxin-regulated proteins in plants and stringent starvation proteins in E. coli (not known to have GST activity and similarity not previously recognized). The glutathione molecule binds in a cleft between the N- and C-terminal domains - the catalytically important residues are proposed to reside in the N-terminal domain.


Pssm-ID: 460698 [Multi-domain]  Cd Length: 76  Bit Score: 66.17  E-value: 1.66e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 976677613   16 MTIYDFPKGPYPTRVRIALAEKGLrsRVEFVMVDLYKGEHKRPEFISEKNYsGTLPVLElEDGTCIAECTAITEYLD 92
Cdd:pfam02798   3 LTLYGIRGSPRAHRIRWLLAEKGV--EYEIVPLDFGAGPEKSPELLKLNPL-GKVPALE-DGGKKLTESRAILEYIA 75
PRK10542 PRK10542
glutathionine S-transferase; Provisional
 32-221 1.35e-13

glutathionine S-transferase; Provisional


Pssm-ID: 182533 [Multi-domain]  Cd Length: 201  Bit Score: 67.01  E-value: 1.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613  32 IALAEKGLrsrvEF--VMVDLYKgehKRPEfiSEKNY-----SGTLPVLELEDGTCIAECTAITEYL-----DTLDGAPT 99
Cdd:PRK10542  16 ITLRESGL----DFtlVSVDLAK---KRLE--NGDDYlainpKGQVPALLLDDGTLLTEGVAIMQYLadsvpDRQLLAPV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613 100 LTgrtplekgvihmMSKRAELELLDAISVYFHHA-TPGLGPNvelyQNAEWGLRQRDKALRGMHYFNDVLKRQPFVAGDA 178
Cdd:PRK10542  87 GS------------LSRYHTIEWLNYIATELHKGfTPLFRPD----TPEEYKPTVRAQLEKKFQYVDEALADEQWICGQR 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 976677613 179 FSMADITVIGGLVFASIVKLPVpTECEALVDWYVRMRQRPSVK 221
Cdd:PRK10542 151 FTIADAYLFTVLRWAYAVKLNL-EGLEHIAAYMQRVAERPAVA 192
maiA TIGR01262
maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and ...
 29-92 1.80e-09

maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and phenylalanine catabolism. It requires glutathione and belongs by homology to the zeta family of glutathione S-transferases. The enzyme (EC 5.2.1.2) is described as active also on maleylpyruvate, and the example from a Ralstonia sp. catabolic plasmid is described as a maleylpyruvate isomerase involved in gentisate catabolism. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273527 [Multi-domain]  Cd Length: 210  Bit Score: 55.80  E-value: 1.80e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 976677613   29 RVRIALAEKGLrsRVEFVMVDLYK-GEHKRPEFiSEKNYSGTLPVLELeDGTCIAECTAITEYLD 92
Cdd:TIGR01262  13 RVRIALALKGI--DYEYVPVNLLRdGEQRSPEF-LALNPQGLVPTLDI-DGEVLTQSLAIIEYLE 73
PRK15113 PRK15113
glutathione transferase;
25-99 7.55e-09

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 53.81  E-value: 7.55e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 976677613  25 PYPTRVRIALAEKGLRsrVEFVMVDLYKGEHKRPEFISeknYSGT--LPVLELEDGTcIAECTAITEYLDTLDGAPT 99
Cdd:PRK15113  17 PYVMSAFVALQEKGLP--FELKTVDLDAGEHLQPTYQG---YSLTrrVPTLQHDDFE-LSESSAIAEYLEERFAPPA 87
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 152-213 6.10e-05

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 40.00  E-value: 6.10e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 976677613  152 RQRDKALRGMHYFNDVLKRQPFVAGDAFSMADITVIGGLVFASIVKLPVP--TECEALVDWYVR 213
Cdd:pfam13410   4 RAREQLRAALDALEARLADGPGLLGDRPTLADIALAPVLARLDAAYPGLDlrEGYPRLRAWLER 67
 
Name Accession Description Interval E-value
GST_C_GTT2_like cd03182
C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione ...
 104-220 5.25e-56

C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly uncharacterized proteins with similarity to the Saccharomyces cerevisiae GST protein, GTT2. 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. GTT2, a homodimer, exhibits GST activity with standard substrates. Strains with deleted GTT2 genes are viable but exhibit increased sensitivity to heat shock.


Pssm-ID: 198291 [Multi-domain]  Cd Length: 116  Bit Score: 174.05  E-value: 5.25e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613 104 TPLEKGVIHMMSKRAELELLDAISVYFHHATPGLGPnVELYQNAEWGLRQRDKALRGMHYFNDVLKRQPFVAGDAFSMAD 183
Cdd:cd03182    1 TPLEKALIEMWQRRAELQGLAPVFQAFRHATPGLKP-DREVQVPEWGERNKKRVIDFLPVLDKRLAESPYVAGDRFSIAD 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 976677613 184 ITVIGGLVFASIVKLPVPTECEALVDWYVRMRQRPSV 220
Cdd:cd03182   80 ITAFVALDFAKNLKLPVPEELTALRRWYERMAARPSA 116
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
16-221 2.93e-46

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 152.36  E-value: 2.93e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613  16 MTIYDFPKGPYPTRVRIALAEKGLRsrVEFVMVDLYKGEHKRPEFIsEKNYSGTLPVLElEDGTCIAECTAITEYLDTLD 95
Cdd:COG0625    2 MKLYGSPPSPNSRRVRIALEEKGLP--YELVPVDLAKGEQKSPEFL-ALNPLGKVPVLV-DDGLVLTESLAILEYLAERY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613  96 GAPTLTGRTPLEKGVIHMMSKRAELELLDAISVYFHHATPGlgpnvelyQNAEWGLRQRDKALRGMHYFNDVLKRQPFVA 175
Cdd:COG0625   78 PEPPLLPADPAARARVRQWLAWADGDLHPALRNLLERLAPE--------KDPAAIARARAELARLLAVLEARLAGGPYLA 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 976677613 176 GDAFSMADITVIGGLVFASIVKLPVPtECEALVDWYVRMRQRPSVK 221
Cdd:COG0625  150 GDRFSIADIALAPVLRRLDRLGLDLA-DYPNLAAWLARLAARPAFQ 194
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
 16-92 5.05e-34

GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly uncharacterized proteins with similarity to the S. cerevisiae GST protein, GTT2. 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. GTT2, a homodimer, exhibits GST activity with standard substrates. Strains with deleted GTT2 genes are viable but exhibit increased sensitivity to heat shock.


Pssm-ID: 239349 [Multi-domain]  Cd Length: 74  Bit Score: 116.63  E-value: 5.05e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 976677613  16 MTIYDFPKGPYPTRVRIALAEKGLRsrVEFVMVDLYKGEHKRPEFISeKNYSGTLPVLELEDGTCIAECTAITEYLD 92
Cdd:cd03051    1 MKLYDSPTAPNPRRVRIFLAEKGID--VPLVTVDLAAGEQRSPEFLA-KNPAGTVPVLELDDGTVITESVAICRYLE 74
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 16-92 2.18e-16

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: 71.06  E-value: 2.18e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 976677613  16 MTIYDFPKGPYPTRVRIALAEKGLrsRVEFVMVDLYKGEHKrpEFIsEKNYSGTLPVLELeDGTCIAECTAITEYLD 92
Cdd:cd00570    1 LKLYYFPGSPRSLRVRLALEEKGL--PYELVPVDLGEGEQE--EFL-ALNPLGKVPVLED-GGLVLTESLAILEYLA 71
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
 16-92 1.30e-14

GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related fungal and bacterial 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. 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. The class Phi GST subfamily has experience extensive gene duplication. The Arabidopsis and Oryza genomes contain 13 and 16 Phi GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Tau GSTs, showing class specificity in substrate preference. Phi enzymes are highly reactive toward chloroacetanilide and thiocarbamate herbicides. Some Phi GSTs have other functions including transport of flavonoid pigments to the vacuole, shoot regeneration and GSH peroxidase activity.


Pssm-ID: 239351 [Multi-domain]  Cd Length: 76  Bit Score: 66.52  E-value: 1.30e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 976677613  16 MTIYDFPKGPYPTRVRIALAEKGLrsRVEFVMVDLYKGEHKRPEFiSEKNYSGTLPVLElEDGTCIAECTAITEYLD 92
Cdd:cd03053    2 LKLYGAAMSTCVRRVLLCLEEKGV--DYELVPVDLTKGEHKSPEH-LARNPFGQIPALE-DGDLKLFESRAITRYLA 74
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 16-92 1.66e-14

Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to a variety of targets. Also included in the alignment, but not GSTs: S-crystallins from squid (similarity to GST previously noted); eukaryotic elongation factors 1-gamma (not known to have GST activity and similarity not previously recognized); HSP26 family of stress-related proteins including auxin-regulated proteins in plants and stringent starvation proteins in E. coli (not known to have GST activity and similarity not previously recognized). The glutathione molecule binds in a cleft between the N- and C-terminal domains - the catalytically important residues are proposed to reside in the N-terminal domain.


Pssm-ID: 460698 [Multi-domain]  Cd Length: 76  Bit Score: 66.17  E-value: 1.66e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 976677613   16 MTIYDFPKGPYPTRVRIALAEKGLrsRVEFVMVDLYKGEHKRPEFISEKNYsGTLPVLElEDGTCIAECTAITEYLD 92
Cdd:pfam02798   3 LTLYGIRGSPRAHRIRWLLAEKGV--EYEIVPLDFGAGPEKSPELLKLNPL-GKVPALE-DGGKKLTESRAILEYIA 75
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 25-94 1.13e-13

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 63.80  E-value: 1.13e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613   25 PYPTRVRIALAEKGLRSRVEFVMVDlykGEHKRPEFiSEKNYSGTLPVLELEDGTCIAECTAITEYLDTL 94
Cdd:pfam13409   3 PFSHRVRLALEEKGLPYEIELVDLD---PKDKPPEL-LALNPLGTVPVLVLPDGTVLTDSLVILEYLEEL 68
PRK10542 PRK10542
glutathionine S-transferase; Provisional
 32-221 1.35e-13

glutathionine S-transferase; Provisional


Pssm-ID: 182533 [Multi-domain]  Cd Length: 201  Bit Score: 67.01  E-value: 1.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613  32 IALAEKGLrsrvEF--VMVDLYKgehKRPEfiSEKNY-----SGTLPVLELEDGTCIAECTAITEYL-----DTLDGAPT 99
Cdd:PRK10542  16 ITLRESGL----DFtlVSVDLAK---KRLE--NGDDYlainpKGQVPALLLDDGTLLTEGVAIMQYLadsvpDRQLLAPV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613 100 LTgrtplekgvihmMSKRAELELLDAISVYFHHA-TPGLGPNvelyQNAEWGLRQRDKALRGMHYFNDVLKRQPFVAGDA 178
Cdd:PRK10542  87 GS------------LSRYHTIEWLNYIATELHKGfTPLFRPD----TPEEYKPTVRAQLEKKFQYVDEALADEQWICGQR 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 976677613 179 FSMADITVIGGLVFASIVKLPVpTECEALVDWYVRMRQRPSVK 221
Cdd:PRK10542 151 FTIADAYLFTVLRWAYAVKLNL-EGLEHIAAYMQRVAERPAVA 192
GST_N_Zeta cd03042
GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 16-92 7.38e-13

GST_N family, Class Zeta subfamily; 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. 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. Class Zeta GSTs, also known as maleylacetoacetate (MAA) isomerases, catalyze the isomerization of MAA to fumarylacetoacetate, the penultimate step in tyrosine/phenylalanine catabolism, using GSH as a cofactor. They show little GSH-conjugating activity towards traditional GST substrates but display modest GSH peroxidase activity. They are also implicated in the detoxification of the carcinogen dichloroacetic acid by catalyzing its dechlorination to glyoxylic acid.


Pssm-ID: 239340 [Multi-domain]  Cd Length: 73  Bit Score: 61.82  E-value: 7.38e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 976677613  16 MTIYDFPKGPYPTRVRIALAEKGLrsRVEFVMVDLYKGEHKRPEFiSEKNYSGTLPVLELeDGTCIAECTAITEYLD 92
Cdd:cd03042    1 MILYSYFRSSASYRVRIALNLKGL--DYEYVPVNLLKGEQLSPAY-RALNPQGLVPTLVI-DGLVLTQSLAIIEYLD 73
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
 16-91 1.71e-12

GST_N family, unknown subfamily 4; composed of 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains.


Pssm-ID: 239354 [Multi-domain]  Cd Length: 73  Bit Score: 60.67  E-value: 1.71e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 976677613  16 MTIYDFPKGPYPTRVRIALAEKGLRsrVEFVMVDLYKGEHKRPEFiSEKNYSGTLPVLELeDGTCIAECTAITEYL 91
Cdd:cd03056    1 MKLYGFPLSGNCYKVRLLLALLGIP--YEWVEVDILKGETRTPEF-LALNPNGEVPVLEL-DGRVLAESNAILVYL 72
GST_N_3 cd03049
GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with ...
 16-92 1.48e-11

GST_N family, unknown subfamily 3; composed of 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains.


Pssm-ID: 239347 [Multi-domain]  Cd Length: 73  Bit Score: 58.04  E-value: 1.48e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 976677613  16 MTIYDFPKGPYPTRVRIALAEKGLRSRVEFVMVDLYKgehkRPEFISEKNYSGTLPVLELEDGTCIAECTAITEYLD 92
Cdd:cd03049    1 MKLLYSPTSPYVRKVRVAAHETGLGDDVELVLVNPWS----DDESLLAVNPLGKIPALVLDDGEALFDSRVICEYLD 73
PRK10357 PRK10357
putative glutathione S-transferase; Provisional
 25-219 5.56e-10

putative glutathione S-transferase; Provisional


Pssm-ID: 182405 [Multi-domain]  Cd Length: 202  Bit Score: 57.04  E-value: 5.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613  25 PYPTRVRIALAEKGLRsrVEFVMVDLYKGEHKRPEFisekNYSGTLPVLELEDGTCIAECTAITEYLDTLDGAPTLTGRT 104
Cdd:PRK10357  10 PFVRKISILLLEKGIT--FEFVNELPYNADNGVAQY----NPLGKVPALVTEEGECWFDSPIIAEYIELLNVAPAMLPRD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613 105 PLEKGVIHMMSKRAELELLDAISVYFHHATPGlgpnveLYQNAEWGLRQRDKALRGMhyfnDVLKR---QPFVAGDAFSM 181
Cdd:PRK10357  84 PLAALRVRQLEALADGIMDAALVSVREQARPA------AQQSEDELLRQREKINRSL----DALEGylvDGTLKTDTVNL 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 976677613 182 ADITV---IGGLVFASIvklpVPTEC---EALVDWYVRMRQRPS 219
Cdd:PRK10357 154 ATIAIacaVGYLNFRRV----APGWCvdrPHLVKLVENLFQRES 193
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 25-92 1.47e-09

GST_N family, Class Omega subfamily; 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. 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. Class Omega GSTs show little or no GSH-conjugating activity towards standard GST substrates. Instead, they catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins. They contain a conserved cysteine equivalent to the first cysteine in the CXXC motif of glutaredoxins, which is a redox active residue capable of reducing GSH mixed disulfides in a monothiol mechanism. Polymorphisms of the class Omega GST genes may be associated with the development of some types of cancer and the age-at-onset of both Alzheimer's and Parkinson's diseases.


Pssm-ID: 239353 [Multi-domain]  Cd Length: 89  Bit Score: 53.13  E-value: 1.47e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 976677613  25 PYPTRVRIALAEKGLRSRVefVMVDLykgEHKrPEFISEKNYSGTLPVLELEDGTCIAECTAITEYLD 92
Cdd:cd03055   28 PYAQRARLVLAAKNIPHEV--ININL---KDK-PDWFLEKNPQGKVPALEIDEGKVVYESLIICEYLD 89
maiA TIGR01262
maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and ...
 29-92 1.80e-09

maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and phenylalanine catabolism. It requires glutathione and belongs by homology to the zeta family of glutathione S-transferases. The enzyme (EC 5.2.1.2) is described as active also on maleylpyruvate, and the example from a Ralstonia sp. catabolic plasmid is described as a maleylpyruvate isomerase involved in gentisate catabolism. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273527 [Multi-domain]  Cd Length: 210  Bit Score: 55.80  E-value: 1.80e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 976677613   29 RVRIALAEKGLrsRVEFVMVDLYK-GEHKRPEFiSEKNYSGTLPVLELeDGTCIAECTAITEYLD 92
Cdd:TIGR01262  13 RVRIALALKGI--DYEYVPVNLLRdGEQRSPEF-LALNPQGLVPTLDI-DGEVLTQSLAIIEYLE 73
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
19-98 1.84e-09

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 52.61  E-value: 1.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613   19 YDFPKGPYPTRVRIALAEKGLrsRVEFVMVDLYkgeHKRPEFiSEKNYSGTLPVLELeDGTCIAECTAITEYLDTLDGAP 98
Cdd:pfam13417   2 YGFPGSPYARRVRIALNEKGL--PYEFVPIPPG---DHPPEL-LAKNPLGKVPVLED-DGGILCESLAIIDYLEELYPGP 74
PLN02395 PLN02395
glutathione S-transferase
 15-221 3.61e-09

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 54.87  E-value: 3.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613  15 IMTIYDfPKGPYPTRVRIALAEKGLRsrVEFVMVDLYKGEHKRPEFISEKNYsGTLPVLELEDGTcIAECTAITEYL--D 92
Cdd:PLN02395   2 VLKVYG-PAFASPKRALVTLIEKGVE--FETVPVDLMKGEHKQPEYLALQPF-GVVPVIVDGDYK-IFESRAIMRYYaeK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613  93 TLDGAPTLTGRTPLEKGVIHmmsKRAELEL------LDAISVYFHHATP-GLGPNVELYQNAEwglrqrDKALRGMHYFN 165
Cdd:PLN02395  77 YRSQGPDLLGKTIEERGQVE---QWLDVEAtsyhppLLNLTLHILFASKmGFPADEKVIKESE------EKLAKVLDVYE 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 976677613 166 DVLKRQPFVAGDAFSMADITvigGLVFASIVKLPVPTEC-----EALVDWYVRMRQRPSVK 221
Cdd:PLN02395 148 ARLSKSKYLAGDFVSLADLA---HLPFTEYLVGPIGKAYlikdrKHVSAWWDDISSRPAWK 205
GST_C_2 cd03180
C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; ...
 153-218 5.10e-09

C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 2; composed of 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.


Pssm-ID: 198289 [Multi-domain]  Cd Length: 110  Bit Score: 52.28  E-value: 5.10e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 976677613 153 QRDKAL---------RGMHYFNDVLKRQPFVAGDAFSMADItVIGGLVFASivkLPVPTE---CEALVDWYVRMRQRP 218
Cdd:cd03180   35 QRDPAAiaaslaacnKLMAILDAQLARQAYLAGDRFTLADI-ALGCSVYRW---LELPIErpaLPHLERWYARLSQRP 108
GST_C_Beta cd03188
C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ...
 121-222 6.42e-09

C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Beta subfamily; 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. 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. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they are involved in the protection against oxidative stress and are able to bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs, contributing to antibiotic resistance. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH. One member of this subfamily is a GST from Burkholderia xenovorans LB400 that is encoded by the bphK gene and is part of the biphenyl catabolic pathway.


Pssm-ID: 198297 [Multi-domain]  Cd Length: 113  Bit Score: 52.25  E-value: 6.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613 121 ELLDAISVYFHHATPGLGPNVELYQNAewglrQRDKALRGMHYFNDVLKRQPFVAGDAFSMADI---TVIGGLVFasiVK 197
Cdd:cd03188   16 ELHKAFGPLFYPARWADDALAEEVKAA-----ARERLERRLAYLDAQLAGGPYLLGDQFSVADAylfVVLRWARA---VG 87

                         90       100
                 ....*....|....*....|....*
gi 976677613 198 LPvPTECEALVDWYVRMRQRPSVKN 222
Cdd:cd03188   88 LD-LSDWPHLAAYLARVAARPAVQA 111
PRK15113 PRK15113
glutathione transferase;
25-99 7.55e-09

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 53.81  E-value: 7.55e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 976677613  25 PYPTRVRIALAEKGLRsrVEFVMVDLYKGEHKRPEFISeknYSGT--LPVLELEDGTcIAECTAITEYLDTLDGAPT 99
Cdd:PRK15113  17 PYVMSAFVALQEKGLP--FELKTVDLDAGEHLQPTYQG---YSLTrrVPTLQHDDFE-LSESSAIAEYLEERFAPPA 87
GST_N_SspA cd03059
GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ...
 16-92 3.84e-08

GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP)-associated protein required for the lytic development of phage P1 and for stationary phase-induced acid tolerance of E. coli. It is implicated in survival during nutrient starvation. SspA adopts the GST fold with an N-terminal TRX-fold domain and a C-terminal alpha helical domain, but it does not bind glutathione (GSH) and lacks GST activity. SspA is highly conserved among gram-negative bacteria. Related proteins found in Neisseria (called RegF), Francisella and Vibrio regulate the expression of virulence factors necessary for pathogenesis.


Pssm-ID: 239357 [Multi-domain]  Cd Length: 73  Bit Score: 48.86  E-value: 3.84e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 976677613  16 MTIYDFPKGPYPTRVRIALAEKGLrsRVEFVMVDLYkgeHKrPEFISEKNYSGTLPVLeLEDGTCIAECTAITEYLD 92
Cdd:cd03059    1 MTLYSGPDDVYSHRVRIVLAEKGV--SVEIIDVDPD---NP-PEDLAELNPYGTVPTL-VDRDLVLYESRIIMEYLD 70
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 111-214 6.95e-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: 49.03  E-value: 6.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613 111 IHMMSKRAELELLDAISVYFHHATPGLGPNVELYQNAewglrqRDKALRGMHYFNDVLKRQPFVAGDAFSMADITVIGGL 190
Cdd:cd00299    1 VRALEDWADATLAPPLVRLLYLEKVPLPKDEAAVEAA------REELPALLAALEQLLAGRPYLAGDQFSLADVALAPVL 74

                         90       100
                 ....*....|....*....|....*.
gi 976677613 191 VFASIVK--LPVPTECEALVDWYVRM 214
Cdd:cd00299   75 ARLEALGpyYDLLDEYPRLKAWYDRL 100
GST_N_Delta_Epsilon cd03045
GST_N family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved ...
 16-91 1.41e-07

GST_N family, Class Delta and Epsilon subfamily; 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. The class Delta and Epsilon subfamily is made up primarily of insect GSTs, which play major roles in insecticide resistance by facilitating reductive dehydrochlorination of insecticides or conjugating them with GSH to produce water-soluble metabolites that are easily excreted. They are also implicated in protection against cellular damage by oxidative stress.


Pssm-ID: 239343 [Multi-domain]  Cd Length: 74  Bit Score: 47.22  E-value: 1.41e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 976677613  16 MTIYDFPKGPyPTRVrIALAEKGLRSRVEFVMVDLYKGEHKRPEFIsEKNYSGTLPVLElEDGTCIAECTAITEYL 91
Cdd:cd03045    1 IDLYYLPGSP-PCRA-VLLTAKALGLELNLKEVNLMKGEHLKPEFL-KLNPQHTVPTLV-DNGFVLWESHAILIYL 72
PLN02473 PLN02473
glutathione S-transferase
 15-221 5.80e-07

glutathione S-transferase


Pssm-ID: 166114 [Multi-domain]  Cd Length: 214  Bit Score: 48.45  E-value: 5.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613  15 IMTIYDFPKGPYPTRVRIALAEKGLRsrVEFVMVDLYKGEHKRPEFISEKNYsGTLPVLEleDGTC-IAECTAITEYLDT 93
Cdd:PLN02473   2 VVKVYGQIKAANPQRVLLCFLEKGIE--FEVIHVDLDKLEQKKPEHLLRQPF-GQVPAIE--DGDLkLFESRAIARYYAT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613  94 --LDGAPTLTGRTpLEKGVIhmMSKRAELElldaiSVYFHHATPGLGPNV----ELYQNAEWGLRQRDKALRG--MHYFN 165
Cdd:PLN02473  77 kyADQGTDLLGKT-LEHRAI--VDQWVEVE-----NNYFYAVALPLVINLvfkpRLGEPCDVALVEELKVKFDkvLDVYE 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 976677613 166 DVLKRQPFVAGDAFSMADITVIGGLVF-ASIVKLP-VPTECEALVDWYVRMRQRPSVK 221
Cdd:PLN02473 149 NRLATNRYLGGDEFTLADLTHMPGMRYiMNETSLSgLVTSRENLNRWWNEISARPAWK 206
GST_N_EF1Bgamma cd03044
GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part ...
 17-91 6.10e-07

GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. The EF1B gamma subunit contains a GST fold consisting of an N-terminal TRX-fold domain and a C-terminal alpha helical domain. The GST-like domain of EF1Bgamma is believed to mediate the dimerization of the EF1 complex, which in yeast is a dimer of the heterotrimer EF1A:EF1Balpha:EF1Bgamma. In addition to its role in protein biosynthesis, EF1Bgamma may also display other functions. The recombinant rice protein has been shown to possess GSH conjugating activity. The yeast EF1Bgamma binds membranes in a calcium dependent manner and is also part of a complex that binds to the msrA (methionine sulfoxide reductase) promoter suggesting a function in the regulation of its gene expression.


Pssm-ID: 239342 [Multi-domain]  Cd Length: 75  Bit Score: 45.71  E-value: 6.10e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 976677613  17 TIYDFPKGPYPTRVRIALAEKGLrsrvEFVMVDLYKG-EHKRPEFISeKNYSGTLPVLELEDGTCIAECTAITEYL 91
Cdd:cd03044    2 TLYTYPGNPRSLKILAAAKYNGL----DVEIVDFQPGkENKTPEFLK-KFPLGKVPAFEGADGFCLFESNAIAYYV 72
GST_N_Beta cd03057
GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 30-91 1.20e-06

GST_N family, Class Beta subfamily; 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. 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. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit limited GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they also bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH.


Pssm-ID: 239355 [Multi-domain]  Cd Length: 77  Bit Score: 44.84  E-value: 1.20e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 976677613  30 VRIALAEKGLRsrVEFVMVDLYKGEHKRPEF--ISEKnysGTLPVLELEDGTCIAECTAITEYL 91
Cdd:cd03057   14 PHIALEELGLP--FELVRVDLRTKTQKGADYlaINPK---GQVPALVLDDGEVLTESAAILQYL 72
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
 28-91 1.27e-06

GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly uncharacterized proteins with similarity to the S. cerevisiae GST protein, GTT1, and the Schizosaccharomyces pombe GST-III. 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. GTT1, a homodimer, exhibits GST activity with standard substrates and associates with the endoplasmic reticulum. Its expression is induced after diauxic shift and remains high throughout the stationary phase. S. pombe GST-III is implicated in the detoxification of various metals.


Pssm-ID: 239344 [Multi-domain]  Cd Length: 76  Bit Score: 44.80  E-value: 1.27e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 976677613  28 TRVRIALAEKGLRsrVEFVMVDLYKGEHKRPEFIsEKNYSGTLPVLElEDGTCIAECTAITEYL 91
Cdd:cd03046   12 FRILWLLEELGLP--YELVLYDRGPGEQAPPEYL-AINPLGKVPVLV-DGDLVLTESAAIILYL 71
GST_N_Ure2p_like cd03048
GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related ...
 17-91 1.90e-05

GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related GSTs. Ure2p is a regulator for nitrogen catabolism in yeast. It represses the expression of several gene products involved in the use of poor nitrogen sources when rich sources are available. A transmissible conformational change of Ure2p results in a prion called [Ure3], an inactive, self-propagating and infectious amyloid. Ure2p displays a GST fold containing 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. The N-terminal TRX-fold domain is sufficient to induce the [Ure3] phenotype and is also called the prion domain of Ure2p. In addition to its role in nitrogen regulation, Ure2p confers protection to cells against heavy metal ion and oxidant toxicity, and shows glutathione (GSH) peroxidase activity. Characterized GSTs in this subfamily include Aspergillus fumigatus GSTs 1 and 2, and Schizosaccharomyces pombe GST-I. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of 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.


Pssm-ID: 239346 [Multi-domain]  Cd Length: 81  Bit Score: 41.76  E-value: 1.90e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 976677613  17 TIYDFPkGPYPTRVRIALAEKGLRsrVEFVMVDLYKGEHKRPEFIsEKNYSGTLPVLE--LEDGTCIAECTAITEYL 91
Cdd:cd03048    3 TLYTHG-TPNGFKVSIMLEELGLP--YEIHPVDISKGEQKKPEFL-KINPNGRIPAIVdhNGTPLTVFESGAILLYL 75
GST_N_Omega_like cd03060
GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to ...
 18-83 2.28e-05

GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to class Omega 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. 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. Class Omega GSTs show little or no GSH-conjugating activity towards standard GST substrates. Instead, they catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins. Like Omega enzymes, proteins in this subfamily contain a conserved cysteine equivalent to the first cysteine in the CXXC motif of glutaredoxins, which is a redox active residue capable of reducing GSH mixed disulfides in a monothiol mechanism.


Pssm-ID: 239358 [Multi-domain]  Cd Length: 71  Bit Score: 41.19  E-value: 2.28e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 976677613  18 IYDFPKGPYPTRVRIALAEKGLRsrVEFVMVDLykgEHKRPEFIsEKNYSGTLPVLELEDGTCIAE 83
Cdd:cd03060    3 LYSFRRCPYAMRARMALLLAGIT--VELREVEL---KNKPAEML-AASPKGTVPVLVLGNGTVIEE 62
sspA PRK09481
stringent starvation protein A; Provisional
 12-119 2.50e-05

stringent starvation protein A; Provisional


Pssm-ID: 236537 [Multi-domain]  Cd Length: 211  Bit Score: 43.54  E-value: 2.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613  12 KLPIMTIYDFPKGPYPTRVRIALAEKGLRSRVEFVMVDlykgehKRPEFISEKNYSGTLPVL---ELedgtCIAECTAIT 88
Cdd:PRK09481   7 KRSVMTLFSGPTDIYSHQVRIVLAEKGVSVEIEQVEKD------NLPQDLIDLNPYQSVPTLvdrEL----TLYESRIIM 76

                         90       100       110
                 ....*....|....*....|....*....|.
gi 976677613  89 EYLDTLDGAPTLTGRTPLEKGVIHMMSKRAE 119
Cdd:PRK09481  77 EYLDERFPHPPLMPVYPVARGESRLMMHRIE 107
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 16-92 2.66e-05

GST_N family, Class Tau subfamily; 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. 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. The plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones.


Pssm-ID: 239356 [Multi-domain]  Cd Length: 74  Bit Score: 41.11  E-value: 2.66e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 976677613  16 MTIYDFPKGPYPTRVRIALAEKGLrsRVEFVMVDLYKgehKRPEFISEKNYSGTLPVLeLEDGTCIAECTAITEYLD 92
Cdd:cd03058    1 VKLLGAWASPFVLRVRIALALKGV--PYEYVEEDLGN---KSELLLASNPVHKKIPVL-LHNGKPICESLIIVEYID 71
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 152-213 6.10e-05

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 40.00  E-value: 6.10e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 976677613  152 RQRDKALRGMHYFNDVLKRQPFVAGDAFSMADITVIGGLVFASIVKLPVP--TECEALVDWYVR 213
Cdd:pfam13410   4 RAREQLRAALDALEARLADGPGLLGDRPTLADIALAPVLARLDAAYPGLDlrEGYPRLRAWLER 67
PRK13972 PRK13972
GSH-dependent disulfide bond oxidoreductase; Provisional
 21-219 7.66e-05

GSH-dependent disulfide bond oxidoreductase; Provisional


Pssm-ID: 172475 [Multi-domain]  Cd Length: 215  Bit Score: 42.37  E-value: 7.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613  21 FPKGPYPTRVRIALAEKGLRSRVefVMVDLYKGEHKRPEF--ISEKN----------YSGTLPVLELEDGTC---IAECT 85
Cdd:PRK13972   6 FAPTPNGHKITLFLEEAELDYRL--IKVDLGKGGQFRPEFlrISPNNkipaivdhspADGGEPLSLFESGAIllyLAEKT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613  86 AITEYLDTLDGAPTLTGRTPLEKGVIHMMSKRAelelldaisvYFHHATPGLGP-NVELYQNaewglrqrdKALRGMHYF 164
Cdd:PRK13972  84 GLFLSHETRERAATLQWLFWQVGGLGPMLGQNH----------HFNHAAPQTIPyAIERYQV---------ETQRLYHVL 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 976677613 165 NDVLKRQPFVAGDAFSMADITV---IGGLVFASIVKLPVPteceALVDWYVRMRQRPS 219
Cdd:PRK13972 145 NKRLENSPWLGGENYSIADIACwpwVNAWTRQRIDLAMYP----AVKNWHERIRSRPA 198
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 154-218 1.38e-04

Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety of targets including S-crystallin from squid, the eukaryotic elongation factor 1-gamma, the HSP26 family of stress-related proteins and auxin-regulated proteins in plants. Stringent starvation proteins in E. coli are also included in the alignment but are not known to have GST activity. The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed to reside in the N-terminal domain. In plants, GSTs are encoded by a large gene family (48 GST genes in Arabidopsis) and can be divided into the phi, tau, theta, zeta, and lambda classes.


Pssm-ID: 459647 [Multi-domain]  Cd Length: 93  Bit Score: 39.58  E-value: 1.38e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613  154 RDKALRGMH----YFNDVLKRQPFVAGDAFSMADITVIGGLVFASIVKLPVPTE-CEALVDWYVRMRQRP 218
Cdd:pfam00043  24 VDEALEKVArvlsALEEVLKGQTYLVGDKLTLADIALAPALLWLYELDPACLREkFPNLKAWFERVAARP 93
GST_N_GDAP1 cd03052
GST_N family, Ganglioside-induced differentiation-associated protein 1 (GDAP1) subfamily; ...
 16-92 1.50e-04

GST_N family, Ganglioside-induced differentiation-associated protein 1 (GDAP1) subfamily; GDAP1 was originally identified as a highly expressed gene at the differentiated stage of GD3 synthase-transfected cells. More recently, mutations in GDAP1 have been reported to cause both axonal and demyelinating autosomal-recessive Charcot-Marie-Tooth (CMT) type 4A neuropathy. CMT is characterized by slow and progressive weakness and atrophy of muscles. Sequence analysis of GDAP1 shows similarities and differences with GSTs; it appears to contain both N-terminal TRX-fold and C-terminal alpha helical domains of GSTs, however, it also contains additional C-terminal transmembrane domains unlike GSTs. GDAP1 is mainly expressed in neuronal cells and is localized in the mitochondria through its transmembrane domains. It does not exhibit GST activity using standard substrates.


Pssm-ID: 239350 [Multi-domain]  Cd Length: 73  Bit Score: 39.07  E-value: 1.50e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 976677613  16 MTIYDFPKGPYPTRVRIALAEKGLrsRVEFVMVDLYKGEHKRPEFIsEKNYSGTLPVLeLEDGTCIAECTAITEYLD 92
Cdd:cd03052    1 LVLYHWTQSFSSQKVRLVIAEKGL--RCEEYDVSLPLSEHNEPWFM-RLNPTGEVPVL-IHGDNIICDPTQIIDYLE 73
GST_C_MetRS_N cd10307
Glutathione S-transferase C-terminal-like, alpha helical domain of Methionyl-tRNA synthetase ...
 162-216 2.67e-04

Glutathione S-transferase C-terminal-like, alpha helical domain of Methionyl-tRNA synthetase from higher eukaryotes; Glutathione S-transferase (GST) C-terminal domain family, Methionyl-tRNA synthetase (MetRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of MetRS from higher eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. MetRS is a class I aaRS, containing a Rossman fold catalytic core. It recognizes the initiator tRNA as well as the Met-tRNA for protein chain elongation. The GST_C-like domain of MetRS from higher eukaryotes is likely involved in protein-protein interactions, to mediate the formation of the multi-aaRS complex that acts as a molecular hub to coordinate protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.


Pssm-ID: 198340 [Multi-domain]  Cd Length: 102  Bit Score: 39.02  E-value: 2.67e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 976677613 162 HYFNDVLKRQPFVAGDAFSMADItVIGGLVFASIV-KLPVPTECEALVDWYVRMRQ 216
Cdd:cd10307   47 HLDQSLLKKSTPLLGDKLSSADV-VVWSALYPLGTdKSALPENLDNLRRWFQNVST 101
GST_C_6 cd03205
C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; ...
 145-221 2.92e-04

C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 6; composed of uncharacterized bacterial proteins with similarity to GSTs, including Pseudomonas fluorescens GST with a known three-dimensional structure. 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. Though the three-dimensional structure of Pseudomonas fluorescens GST has been determined, there is no information on its functional characterization.


Pssm-ID: 198314 [Multi-domain]  Cd Length: 109  Bit Score: 39.11  E-value: 2.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613 145 QNAEWGLRQRDKALRGMhyfnDVLKRQPF-VAGDAFSMADITV---IGGLVFAsIVKLPVPTECEALVDWYVRMRQRPSV 220
Cdd:cd03205   30 QHQPWIERQWGKIERAL----DALEAELGdLPGGRLTLGDIAVacaLGYLDFR-FPELDWRAGHPALAAWFARFEARPSF 104


                 .
gi 976677613 221 K 221
Cdd:cd03205  105 Q 105
GrxB COG2999
Glutaredoxin 2 [Posttranslational modification, protein turnover, chaperones];
70-132 3.72e-04

Glutaredoxin 2 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442237 [Multi-domain]  Cd Length: 215  Bit Score: 40.21  E-value: 3.72e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 976677613  70 LPVLELEDGTCIAECTAITEYLDTLDGAPTLTGRTplekgvihmmskRAELE-LLDAISVYFHH 132
Cdd:COG2999   48 VPILEKDDGSYMPESLDIVHYIDELDGKPILTGPV------------RPEIAaWLKKVSSYVNR 99
GST_N_etherase_LigE cd03038
GST_N family, Beta etherase LigE subfamily; composed of proteins similar to Sphingomonas ...
 25-93 4.84e-04

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: 37.71  E-value: 4.84e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 976677613  25 PYPTRVRIALAEKGLrsrvEFVMVDLYKGEHKRPEFISEKNYSGTLPVLELEDGTCIAECTAITEYLDT 93
Cdd:cd03038   17 PNVWKTRLALNHKGL----EYKTVPVEFPDIPPILGELTSGGFYTVPVIVDGSGEVIGDSFAIAEYLEE 81
GST_C_Delta_Epsilon cd03177
C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; ...
 143-218 7.83e-04

C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Delta and Epsilon subfamily; 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 class Delta and Epsilon subfamily is made up primarily of insect GSTs, which play major roles in insecticide resistance by facilitating reductive dehydrochlorination of insecticides or conjugating them with GSH to produce water-soluble metabolites that are easily excreted. They are also implicated in protection against cellular damage by oxidative stress.


Pssm-ID: 198287 [Multi-domain]  Cd Length: 117  Bit Score: 37.90  E-value: 7.83e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 976677613 143 LYQNAEWGLRQRDKALRGMHYFNDVLKRQPFVAGDAFSMADITVIGGLvfASIVKLPV-PTECEALVDWYVRMRQRP 218
Cdd:cd03177   29 LFGGAEPPEEKLDKLEEALEFLETFLEGSDYVAGDQLTIADLSLVATV--STLEVVGFdLSKYPNVAAWYERLKALP 103
GST_C_etherase_LigE cd03202
C-terminal, alpha helical domain of Beta etherase LigE; Glutathione S-transferase (GST) ...
 154-214 8.33e-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: 38.01  E-value: 8.33e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 976677613 154 RDKAL----RGMHYFNDVLKRQPFVAGDAFSMADITVIGGLVFASIVK-LPVPTECEALVDWYVRM 214
Cdd:cd03202   56 REERLaafrAALEPLRLTLAGQPFLGGAAPNYADYIVFGAFQWARSVSpLPLLEADDPVAAWRERM 121
PRK10387 PRK10387
glutaredoxin 2; Provisional
 16-104 8.97e-04

glutaredoxin 2; Provisional


Pssm-ID: 236679 [Multi-domain]  Cd Length: 210  Bit Score: 39.09  E-value: 8.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613  16 MTIYDFPKGPYPTRVRIALAEKGLRsrVEFVmVDLYKGEHKRPEFISEKnysgTLPVLELEDGTCIAECTAITEYLDTLD 95
Cdd:PRK10387   1 MKLYIYDHCPFCVKARMIFGLKNIP--VELI-VLANDDEATPIRMIGQK----QVPILQKDDGSYMPESLDIVHYIDELD 73


                 ....*....
gi 976677613  96 GAPTLTGRT 104
Cdd:PRK10387  74 GKPLLTGKR 82
GST_C_Ure2p_like cd03178
C-terminal, alpha helical domain of Ure2p and related Glutathione S-transferase-like proteins; ...
 165-221 1.17e-03

C-terminal, alpha helical domain of Ure2p and related Glutathione S-transferase-like proteins; Glutathione S-transferase (GST) C-terminal domain family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p, YfcG and YghU from Escherichia coli, and related GST-like proteins. Ure2p is a regulator for nitrogen catabolism in yeast. It represses the expression of several gene products involved in the use of poor nitrogen sources when rich sources are available. A transmissible conformational change of Ure2p results in a prion called [Ure3], an inactive, self-propagating and infectious amyloid. Ure2p displays a GST fold containing an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The N-terminal thioredoxin-fold domain is sufficient to induce the [Ure3] phenotype and is also called the prion domain of Ure2p. In addition to its role in nitrogen regulation, Ure2p confers protection to cells against heavy metal ion and oxidant toxicity, and shows glutathione (GSH) peroxidase activity. YfcG and YghU are two of the nine GST homologs in the genome of Escherichia coli. They display very low or no GSH transferase, but show very good disulfide bond oxidoreductase activity. YghU also shows modest organic hydroperoxide reductase activity. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of 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 active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain.


Pssm-ID: 198288 [Multi-domain]  Cd Length: 110  Bit Score: 37.23  E-value: 1.17e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 976677613 165 NDVLKRQPFVAGDAFSMADITVIGGLVFASIVKLPVPTECEALVDWYVRMRQRPSVK 221
Cdd:cd03178   53 DKRLSDRPYLAGEEYSIADIALYPWTHYADLGGFADLSEYPNVKRWLERIAARPAVQ 109
GST_C_YfcG_like cd10291
C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and ...
 165-221 3.08e-03

C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and related uncharacterized proteins; Glutathione S-transferase (GST) C-terminal domain family, YfcG-like subfamily; composed of the Escherichia coli YfcG and related 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 active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. YfcG is one of nine GST homologs in Escherichia coli. It is expressed predominantly during the late stationary phase where the predominant form of GSH is glutathionylspermidine (GspSH), suggesting that YfcG might interact with GspSH. It has very low or no GSH transferase or peroxidase activity, but displays a unique disulfide bond reductase activity that is comparable to thioredoxins (TRXs) and glutaredoxins (GRXs). However, unlike TRXs and GRXs, YfcG does not contain a redox active cysteine residue and may use a bound thiol disulfide couple such as 2GSH/GSSG for activity. The crystal structure of YcfG reveals a bound GSSG molecule in its active site. The actual physiological substrates for YfcG are yet to be identified.


Pssm-ID: 198324 [Multi-domain]  Cd Length: 110  Bit Score: 36.09  E-value: 3.08e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613 165 NDVLKRQPFVAGDAFSMADITVIGGLV---FASIVKLPVPteceALVDWYVRMRQRPSVK 221
Cdd:cd10291   53 DRRLAKSKYLAGDEYSIADIAIWPWVArheWQGIDLADFP----NLKRWFERLAARPAVQ 108
GST_N_Theta cd03050
GST_N family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial ...
 44-91 4.30e-03

GST_N family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial dichloromethane (DCM) dehalogenase. 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. 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. Mammalian class Theta GSTs show poor GSH conjugating activity towards the standard substrates, CDNB and ethacrynic acid, differentiating them from other mammalian GSTs. GSTT1-1 shows similar cataytic activity as bacterial DCM dehalogenase, catalyzing the GSH-dependent hydrolytic dehalogenation of dihalomethanes. This is an essential process in methylotrophic bacteria to enable them to use chloromethane and DCM as sole carbon and energy sources. The presence of polymorphisms in human GSTT1-1 and its relationship to the onset of diseases including cancer is subject of many studies. Human GSTT2-2 exhibits a highly specific sulfatase activity, catalyzing the cleavage of sulfate ions from aralkyl sufate esters, but not from aryl or alkyl sulfate esters.


Pssm-ID: 239348 [Multi-domain]  Cd Length: 76  Bit Score: 34.91  E-value: 4.30e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 976677613  44 EFVMVDLYKGEHKRPEFiSEKNYSGTLPVleLEDGT-CIAECTAITEYL 91
Cdd:cd03050   27 EECPIDLRKGEQLTPEF-KKINPFGKVPA--IVDGDfTLAESVAILRYL 72
GST_C_Tau cd03185
C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione ...
 169-221 7.68e-03

C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Tau subfamily; 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. 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 plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones.


Pssm-ID: 198294 [Multi-domain]  Cd Length: 127  Bit Score: 35.23  E-value: 7.68e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 976677613 169 KRQPFVAGDAFSMADItVIGGLVF-------ASIVKLPVPTECEALVDWYVRMRQRPSVK 221
Cdd:cd03185   53 GGKPFFGGDTIGYLDI-ALGSFLGwfkaieeVGGVKLLDEEKFPLLAAWAERFLEREAVK 111
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 163-221 8.38e-03

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


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 34.84  E-value: 8.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 976677613  163 YFNDVLKRQ--PFVAGDAFSMADITV---IGGLVFasIVKLPVPTECEALVDWYVRMRQRPSVK 221
Cdd:pfam14497  37 YFEKVLNKNggGYLVGDKLTYADLALfqvLDGLLY--PKAPDALDKYPKLKALHERVAARPNIK 98
 
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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