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Conserved domains on  [gi|489125516|ref|WP_003035313|]
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MULTISPECIES: glutathione S-transferase family protein [Citrobacter]

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];
1-206 6.89e-63

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


:

Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 193.96  E-value: 6.89e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516   1 MITLWGRNNSTNVKKVLWTLEELELPYNQILAGGQHGGNRDADYLALNPNGLVPLLRDDetDVVLWESNTIVRYLAAQYG 80
Cdd:COG0625    1 MMKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLALNPLGKVPVLVDD--GLVLTESLAILEYLAERYP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516  81 QKRLWIDAPAARAVGEKWMDWANQTLSPAHRVILFGLvrtpADQRDLAAIEASKQVCDNLFAILDNALADQSWFSGAEFG 160
Cdd:COG0625   79 EPPLLPADPAARARVRQWLAWADGDLHPALRNLLERL----APEKDPAAIARARAELARLLAVLEARLAGGPYLAGDRFS 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 489125516 161 TADIAVAPFIYNLFNVGLSWTSRPHLERWYQQLTERPAFQKIVMIP 206
Cdd:COG0625  155 IADIALAPVLRRLDRLGLDLADYPNLAAWLARLAARPAFQRALAAA 200
 
Name Accession Description Interval E-value
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
1-206 6.89e-63

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 193.96  E-value: 6.89e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516   1 MITLWGRNNSTNVKKVLWTLEELELPYNQILAGGQHGGNRDADYLALNPNGLVPLLRDDetDVVLWESNTIVRYLAAQYG 80
Cdd:COG0625    1 MMKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLALNPLGKVPVLVDD--GLVLTESLAILEYLAERYP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516  81 QKRLWIDAPAARAVGEKWMDWANQTLSPAHRVILFGLvrtpADQRDLAAIEASKQVCDNLFAILDNALADQSWFSGAEFG 160
Cdd:COG0625   79 EPPLLPADPAARARVRQWLAWADGDLHPALRNLLERL----APEKDPAAIARARAELARLLAVLEARLAGGPYLAGDRFS 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 489125516 161 TADIAVAPFIYNLFNVGLSWTSRPHLERWYQQLTERPAFQKIVMIP 206
Cdd:COG0625  155 IADIALAPVLRRLDRLGLDLADYPNLAAWLARLAARPAFQRALAAA 200
GST_C_2 cd03180
C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; ...
 90-199 5.19e-41

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: 135.10  E-value: 5.19e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516  90 AARAVGEKWMDWANQTLSPAHRVILFGLVRTPADQRDLAAIEASKQVCDNLFAILDNALADQSWFSGAEFGTADIAVAPF 169
Cdd:cd03180    1 AQRALADRWMDWQTSTLNPAFRYAFWGLVRTPPEQRDPAAIAASLAACNKLMAILDAQLARQAYLAGDRFTLADIALGCS 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 489125516 170 IYNLFNVGLSWTSRPHLERWYQQLTERPAF 199
Cdd:cd03180   81 VYRWLELPIERPALPHLERWYARLSQRPAF 110
PLN02395 PLN02395
glutathione S-transferase
 14-203 1.09e-16

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 75.29  E-value: 1.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516  14 KKVLWTLEELELPYNQILAGGQHGGNRDADYLALNPNGLVPLLRDDetDVVLWESNTIVRYLAAQYGQK--RLWIDAPAA 91
Cdd:PLN02395  14 KRALVTLIEKGVEFETVPVDLMKGEHKQPEYLALQPFGVVPVIVDG--DYKIFESRAIMRYYAEKYRSQgpDLLGKTIEE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516  92 RAVGEKWMDWANQTLSPA------HrvILFGLVRT-PADQRdlaAIEASKQVCDNLFAILDNALADQSWFSGAEFGTADI 164
Cdd:PLN02395  92 RGQVEQWLDVEATSYHPPllnltlH--ILFASKMGfPADEK---VIKESEEKLAKVLDVYEARLSKSKYLAGDFVSLADL 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 489125516 165 AVAPFI-YNLFNVGLSW--TSRPHLERWYQQLTERPAFQKIV 203
Cdd:PLN02395 167 AHLPFTeYLVGPIGKAYliKDRKHVSAWWDDISSRPAWKEVL 208
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 2-76 2.64e-12

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: 60.01  E-value: 2.64e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489125516    2 ITLWGRNNSTNVKKVLWTLEELELPYNQILAGGQHGGNRDADYLALNPNGLVPLLRDDetDVVLWESNTIVRYLA 76
Cdd:pfam02798   3 LTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGAGPEKSPELLKLNPLGKVPALEDG--GKKLTESRAILEYIA 75
 
Name Accession Description Interval E-value
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
1-206 6.89e-63

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 193.96  E-value: 6.89e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516   1 MITLWGRNNSTNVKKVLWTLEELELPYNQILAGGQHGGNRDADYLALNPNGLVPLLRDDetDVVLWESNTIVRYLAAQYG 80
Cdd:COG0625    1 MMKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLALNPLGKVPVLVDD--GLVLTESLAILEYLAERYP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516  81 QKRLWIDAPAARAVGEKWMDWANQTLSPAHRVILFGLvrtpADQRDLAAIEASKQVCDNLFAILDNALADQSWFSGAEFG 160
Cdd:COG0625   79 EPPLLPADPAARARVRQWLAWADGDLHPALRNLLERL----APEKDPAAIARARAELARLLAVLEARLAGGPYLAGDRFS 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 489125516 161 TADIAVAPFIYNLFNVGLSWTSRPHLERWYQQLTERPAFQKIVMIP 206
Cdd:COG0625  155 IADIALAPVLRRLDRLGLDLADYPNLAAWLARLAARPAFQRALAAA 200
GST_C_2 cd03180
C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; ...
 90-199 5.19e-41

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: 135.10  E-value: 5.19e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516  90 AARAVGEKWMDWANQTLSPAHRVILFGLVRTPADQRDLAAIEASKQVCDNLFAILDNALADQSWFSGAEFGTADIAVAPF 169
Cdd:cd03180    1 AQRALADRWMDWQTSTLNPAFRYAFWGLVRTPPEQRDPAAIAASLAACNKLMAILDAQLARQAYLAGDRFTLADIALGCS 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 489125516 170 IYNLFNVGLSWTSRPHLERWYQQLTERPAF 199
Cdd:cd03180   81 VYRWLELPIERPALPHLERWYARLSQRPAF 110
GST_N_2 cd03047
GST_N family, unknown subfamily 2; composed of uncharacterized bacterial proteins with ...
 2-76 2.33e-38

GST_N 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The sequence from Burkholderia cepacia was identified as part of a gene cluster involved in the degradation of 2,4,5-trichlorophenoxyacetic acid. Some GSTs (e.g. Class Zeta and Delta) are known to catalyze dechlorination reactions.


Pssm-ID: 239345 [Multi-domain]  Cd Length: 73  Bit Score: 127.05  E-value: 2.33e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489125516   2 ITLWGRNNSTNVKKVLWTLEELELPYNQILAGGQHGGNRDADYLALNPNGLVPLLRDDetDVVLWESNTIVRYLA 76
Cdd:cd03047    1 LTIWGRRSSINVQKVLWLLDELGLPYERIDAGGQFGGLDTPEFLAMNPNGRVPVLEDG--DFVLWESNAILRYLA 73
GST_N_Ure2p_like cd03048
GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related ...
 1-81 1.64e-20

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: 81.44  E-value: 1.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516   1 MITLWGrNNSTNVKKVLWTLEELELPYNQILAGGQHGGNRDADYLALNPNGLVPLLRD-DETDVVLWESNTIVRYLAAQY 79
Cdd:cd03048    1 MITLYT-HGTPNGFKVSIMLEELGLPYEIHPVDISKGEQKKPEFLKINPNGRIPAIVDhNGTPLTVFESGAILLYLAEKY 79


                 ..
gi 489125516  80 GQ 81
Cdd:cd03048   80 DK 81
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
 2-80 5.83e-19

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: 77.16  E-value: 5.83e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489125516   2 ITLWGRNNSTNVKkVLWTLEELELPYNQILAGGQHGGNRDADYLALNPNGLVPLLRDDetDVVLWESNTIVRYLAAQYG 80
Cdd:cd03046    1 ITLYHLPRSRSFR-ILWLLEELGLPYELVLYDRGPGEQAPPEYLAINPLGKVPVLVDG--DLVLTESAAIILYLAEKYG 76
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 2-76 4.14e-17

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: 72.22  E-value: 4.14e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489125516   2 ITLWGRNNSTNVKKVLWTLEELELPYNQILAGgqHGGNRDADYLALNPNGLVPLLRDDetDVVLWESNTIVRYLA 76
Cdd:cd00570    1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVD--LGEGEQEEFLALNPLGKVPVLEDG--GLVLTESLAILEYLA 71
PLN02395 PLN02395
glutathione S-transferase
 14-203 1.09e-16

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 75.29  E-value: 1.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516  14 KKVLWTLEELELPYNQILAGGQHGGNRDADYLALNPNGLVPLLRDDetDVVLWESNTIVRYLAAQYGQK--RLWIDAPAA 91
Cdd:PLN02395  14 KRALVTLIEKGVEFETVPVDLMKGEHKQPEYLALQPFGVVPVIVDG--DYKIFESRAIMRYYAEKYRSQgpDLLGKTIEE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516  92 RAVGEKWMDWANQTLSPA------HrvILFGLVRT-PADQRdlaAIEASKQVCDNLFAILDNALADQSWFSGAEFGTADI 164
Cdd:PLN02395  92 RGQVEQWLDVEATSYHPPllnltlH--ILFASKMGfPADEK---VIKESEEKLAKVLDVYEARLSKSKYLAGDFVSLADL 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 489125516 165 AVAPFI-YNLFNVGLSW--TSRPHLERWYQQLTERPAFQKIV 203
Cdd:PLN02395 167 AHLPFTeYLVGPIGKAYliKDRKHVSAWWDDISSRPAWKEVL 208
PLN02473 PLN02473
glutathione S-transferase
 1-205 2.97e-16

glutathione S-transferase


Pssm-ID: 166114 [Multi-domain]  Cd Length: 214  Bit Score: 73.87  E-value: 2.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516   1 MITLWGRNNSTNVKKVLWTLEELELPYNQILAGGQHGGNRDADYLALNPNGLVPLLRDDetDVVLWESNTIVRYLAAQYG 80
Cdd:PLN02473   2 VVKVYGQIKAANPQRVLLCFLEKGIEFEVIHVDLDKLEQKKPEHLLRQPFGQVPAIEDG--DLKLFESRAIARYYATKYA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516  81 QK--RLWIDAPAARAVGEKWMDWANQTLSPAHRVILFGLVRTP--ADQRDLAAIEASKQVCDNLFAILDNALADQSWFSG 156
Cdd:PLN02473  80 DQgtDLLGKTLEHRAIVDQWVEVENNYFYAVALPLVINLVFKPrlGEPCDVALVEELKVKFDKVLDVYENRLATNRYLGG 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489125516 157 AEFGTADIAVAP---FIYNLFNVGLSWTSRPHLERWYQQLTERPAFQKIVMI 205
Cdd:PLN02473 160 DEFTLADLTHMPgmrYIMNETSLSGLVTSRENLNRWWNEISARPAWKKLMEL 211
PRK10542 PRK10542
glutathionine S-transferase; Provisional
 42-198 2.07e-14

glutathionine S-transferase; Provisional


Pssm-ID: 182533 [Multi-domain]  Cd Length: 201  Bit Score: 68.56  E-value: 2.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516  42 ADYLALNPNGLVP-LLRDDETdvVLWESNTIVRYLAAQYGQKRLWidAPAARAVGEKWMDWANQTLSPAHRVI--LFgLV 118
Cdd:PRK10542  41 DDYLAINPKGQVPaLLLDDGT--LLTEGVAIMQYLADSVPDRQLL--APVGSLSRYHTIEWLNYIATELHKGFtpLF-RP 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516 119 RTPADQRDLAAIEASKQvcdnlFAILDNALADQSWFSGAEFGTADiavaPFIYNLFN----VGLSWTSRPHLERWYQQLT 194
Cdd:PRK10542 116 DTPEEYKPTVRAQLEKK-----FQYVDEALADEQWICGQRFTIAD----AYLFTVLRwayaVKLNLEGLEHIAAYMQRVA 186


                 ....
gi 489125516 195 ERPA 198
Cdd:PRK10542 187 ERPA 190
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
 2-78 1.04e-13

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: 63.44  E-value: 1.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516   2 ITLWGRNNSTNVKKVLWTLEELELPYNQI---LAGGQHggnRDADYLALNPNGLVPLLRDDetDVVLWESNTIVRYLAAQ 78
Cdd:cd03053    2 LKLYGAAMSTCVRRVLLCLEEKGVDYELVpvdLTKGEH---KSPEHLARNPFGQIPALEDG--DLKLFESRAITRYLAEK 76
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
 2-76 3.12e-13

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: 62.21  E-value: 3.12e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489125516   2 ITLWGRNNSTNVKKVLWTLEELELPYNQI---LAGGQHggnRDADYLALNPNGLVPLLRDDETdvVLWESNTIVRYLA 76
Cdd:cd03056    1 MKLYGFPLSGNCYKVRLLLALLGIPYEWVevdILKGET---RTPEFLALNPNGEVPVLELDGR--VLAESNAILVYLA 73
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 2-76 2.64e-12

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: 60.01  E-value: 2.64e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489125516    2 ITLWGRNNSTNVKKVLWTLEELELPYNQILAGGQHGGNRDADYLALNPNGLVPLLRDDetDVVLWESNTIVRYLA 76
Cdd:pfam02798   3 LTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGAGPEKSPELLKLNPLGKVPALEDG--GKKLTESRAILEYIA 75
GST_C_YfcG_like cd10291
C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and ...
 140-201 4.68e-12

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: 60.36  E-value: 4.68e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489125516 140 LFAILDNALADQSWFSGAEFGTADIAVAPFIYNLFNVGLSWTSRPHLERWYQQLTERPAFQK 201
Cdd:cd10291   48 LYGVLDRRLAKSKYLAGDEYSIADIAIWPWVARHEWQGIDLADFPNLKRWFERLAARPAVQK 109
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
4-83 6.60e-12

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 58.78  E-value: 6.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516    4 LWGRNNSTNVKKVLWTLEELELPYNQILAggqHGGNRDADYLALNPNGLVPLLRDDETdvVLWESNTIVRYLAAQYGQKR 83
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPI---PPGDHPPELLAKNPLGKVPVLEDDGG--ILCESLAIIDYLEELYPGPP 75
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 98-193 7.47e-12

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: 59.43  E-value: 7.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516  98 WMDWANQTLSPAHRVILFglVRTPADQRDLAAIEASKQVCDNLFAILDNALADQSWFSGAEFGTADIAVAPFIYNLFNVG 177
Cdd:cd00299    4 LEDWADATLAPPLVRLLY--LEKVPLPKDEAAVEAAREELPALLAALEQLLAGRPYLAGDQFSLADVALAPVLARLEALG 81

                         90
                 ....*....|....*....
gi 489125516 178 ---LSWTSRPHLERWYQQL 193
Cdd:cd00299   82 pyyDLLDEYPRLKAWYDRL 100
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 10-78 3.44e-11

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 56.87  E-value: 3.44e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489125516   10 STNVKKVLWTLEELELPYN--QILAggqHGGNRDADYLALNPNGLVPLLRDDETDvVLWESNTIVRYLAAQ 78
Cdd:pfam13409   2 SPFSHRVRLALEEKGLPYEieLVDL---DPKDKPPELLALNPLGTVPVLVLPDGT-VLTDSLVILEYLEEL 68
PRK11752 PRK11752
putative S-transferase; Provisional
 12-205 6.90e-11

putative S-transferase; Provisional


Pssm-ID: 183298 [Multi-domain]  Cd Length: 264  Bit Score: 59.94  E-value: 6.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516  12 NVKKVLWTLEELelpynqiLAGGQHGGNRDA-------------DYLALNPNGLVPLLRDDETD--VVLWESNTIVRYLA 76
Cdd:PRK11752  54 NGQKVTIMLEEL-------LALGVKGAEYDAwlirigegdqfssGFVEINPNSKIPALLDRSGNppIRVFESGAILLYLA 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516  77 AQYGQkrLWIDAPAARAVGEKWMDWanQTLSPAHRVILFGLVRTPADQR-----DLAAIEASKQvcdnlFAILDNALADQ 151
Cdd:PRK11752 127 EKFGA--FLPKDLAARTETLNWLFW--QQGSAPFLGGGFGHFYAYAPEKieyaiNRFTMEAKRQ-----LDVLDKQLAEH 197

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489125516 152 SWFSGAEFGTADIAVAPFiY------NLFNVG--LSWTSRPHLERWYQQLTERPAFQKIVMI 205
Cdd:PRK11752 198 EYIAGDEYTIADIAIWPW-YgnlvlgNLYDAAefLDVGSYKHVQRWAKEIAERPAVKRGRIV 258
GST_N_Beta cd03057
GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 18-79 9.79e-11

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: 55.62  E-value: 9.79e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489125516  18 WTLEELELPYNQILAGGQHGGNRDADYLALNPNGLVPLLRDDEtDVVLWESNTIVRYLAAQY 79
Cdd:cd03057   16 IALEELGLPFELVRVDLRTKTQKGADYLAINPKGQVPALVLDD-GEVLTESAAILQYLADLH 76
GST_C_Ure2p_like cd03178
C-terminal, alpha helical domain of Ure2p and related Glutathione S-transferase-like proteins; ...
 122-201 1.47e-10

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: 56.10  E-value: 1.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516 122 ADQRDLAAIEASKQVCDNLFAILDNALADQSWFSGAEFGTADIAVAPFIYNLFNVGLSWTSR-PHLERWYQQLTERPAFQ 200
Cdd:cd03178   30 APEKIPYAIERYTDEVKRLYGVLDKRLSDRPYLAGEEYSIADIALYPWTHYADLGGFADLSEyPNVKRWLERIAARPAVQ 109


                 .
gi 489125516 201 K 201
Cdd:cd03178  110 K 110
PRK13972 PRK13972
GSH-dependent disulfide bond oxidoreductase; Provisional
 10-198 1.64e-10

GSH-dependent disulfide bond oxidoreductase; Provisional


Pssm-ID: 172475 [Multi-domain]  Cd Length: 215  Bit Score: 58.16  E-value: 1.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516  10 STNVKKVLWTLEELELPYNQILAGGQHGGNRDADYLALNPNGLVPLLRDDE-----TDVVLWESNTIVRYLAAQYGqkrL 84
Cdd:PRK13972   9 TPNGHKITLFLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDHSpadggEPLSLFESGAILLYLAEKTG---L 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516  85 WIDAPA-ARAVGEKWMDWANQTLSPahrviLFGL---VRTPADQRDLAAIEASKQVCDNLFAILDNALADQSWFSGAEFG 160
Cdd:PRK13972  86 FLSHETrERAATLQWLFWQVGGLGP-----MLGQnhhFNHAAPQTIPYAIERYQVETQRLYHVLNKRLENSPWLGGENYS 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 489125516 161 TADIAVAPFIYNLFNVGLSWTSRPHLERWYQQLTERPA 198
Cdd:PRK13972 161 IADIACWPWVNAWTRQRIDLAMYPAVKNWHERIRSRPA 198
GST_C_EF1Bgamma_like cd03181
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ...
 97-203 3.13e-10

Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of Elongation Factor 1B and similar proteins; Glutathione S-transferase (GST) C-terminal domain family, Gamma subunit of Elongation Factor 1B (EF1Bgamma) 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 thioredoxin-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 to 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. Also included in this subfamily is the GST_C-like domain at the N-terminus of human valyl-tRNA synthetase (ValRS) and its homologs. Metazoan ValRS forms a stable complex with Elongation Factor-1H (EF-1H), and together, they catalyze consecutive steps in protein biosynthesis, tRNA aminoacylation and its transfer to EF.


Pssm-ID: 198290 [Multi-domain]  Cd Length: 123  Bit Score: 55.64  E-value: 3.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516  97 KWMDWANQTLSPAHRVILFGLV-RTPADQrdlAAIEASKQVCDNLFAILDNALADQSWFSGAEFGTADIAVAPFIYNLF- 174
Cdd:cd03181    7 QWISFANSELLPAAATWVLPLLgIAPYNK---KAVDKAKEDLKRALGVLEEHLLTRTYLVGERITLADIFVASALLRGFe 83

                         90       100       110
                 ....*....|....*....|....*....|.
gi 489125516 175 -NVGLSWTSR-PHLERWYQQLTERPAFQKIV 203
Cdd:cd03181   84 tVLDPEFRKKyPNVTRWFNTVVNQPKFKAVF 114
GST_C_Phi cd03187
C-terminal, alpha helical domain of Class Phi Glutathione S-transferases; Glutathione ...
 91-203 1.29e-09

C-terminal, alpha helical domain of Class Phi Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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 Phi GST subfamily has experience extensive gene duplication. The Arabidopsis and Oryza genomes contain 13 and 16 Tau 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: 198296 [Multi-domain]  Cd Length: 118  Bit Score: 53.77  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516  91 ARAVGEKWMDWANQTLSPAHRVILFGLVRTP--ADQRDLAAIEASKQVCDNLFAILDNALADQSWFSGAEFGTADIAVAP 168
Cdd:cd03187    2 ERALVEQWLEVEAHQFDPPASKLVFELVFKPmlGLKTDEAVVEENEAKLKKVLDVYEARLSKSKYLAGDSFTLADLSHLP 81

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489125516 169 FIYNLFNVGLS--WTSRPHLERWYQQLTERPAFQKIV 203
Cdd:cd03187   82 NLHYLMATPSKklFDSRPHVKAWWEDISARPAWKKVL 118
GST_C_Beta cd03188
C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ...
 97-201 4.39e-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: 4.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516  97 KWMDWANQTLSPAHRVILFglvrtPADQRDLAAIEASKQVC----DNLFAILDNALADQSWFSGAEFGTADIAVAPFIYN 172
Cdd:cd03188    8 EWLNFIASELHKAFGPLFY-----PARWADDALAEEVKAAArerlERRLAYLDAQLAGGPYLLGDQFSVADAYLFVVLRW 82

                         90       100
                 ....*....|....*....|....*....
gi 489125516 173 LFNVGLSWTSRPHLERWYQQLTERPAFQK 201
Cdd:cd03188   83 ARAVGLDLSDWPHLAAYLARVAARPAVQA 111
sspA PRK09481
stringent starvation protein A; Provisional
 38-200 1.96e-08

stringent starvation protein A; Provisional


Pssm-ID: 236537 [Multi-domain]  Cd Length: 211  Bit Score: 52.40  E-value: 1.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516  38 GNRDADYLALNPNGLVPLLRDDEtdVVLWESNTIVRYLAAQYGQKRLWIDAPAARAVGEKWM-----DWanqtLSPAHRV 112
Cdd:PRK09481  44 DNLPQDLIDLNPYQSVPTLVDRE--LTLYESRIIMEYLDERFPHPPLMPVYPVARGESRLMMhriekDW----YSLMNKI 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516 113 ilfglVRTPADQRDlaaiEASKQVCDNLFAILDnALADQSWFSGAEFGTADIAVAPFIYNLFNVGLSWTSR--PHLERWY 190
Cdd:PRK09481 118 -----VNGSASEAD----AARKQLREELLAIAP-VFGEKPYFMSEEFSLVDCYLAPLLWRLPVLGIELSGPgaKELKGYM 187

                        170
                 ....*....|
gi 489125516 191 QQLTERPAFQ 200
Cdd:PRK09481 188 TRVFERDSFL 197
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 113-197 2.53e-08

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: 49.59  E-value: 2.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516  113 ILFGLVRTPADQRDLAAIEASKQVcDNLFAILDNALADQSWFSGAEFGTADIAVAPFIYNLF--NVGLSWTSRPHLERWY 190
Cdd:pfam00043   8 IALLPYVPPEEKKEPEVDEALEKV-ARVLSALEEVLKGQTYLVGDKLTLADIALAPALLWLYelDPACLREKFPNLKAWF 86


                  ....*..
gi 489125516  191 QQLTERP 197
Cdd:pfam00043  87 ERVAARP 93
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
 14-206 1.03e-07

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 50.76  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516  14 KKVLWTLEELELPYNQILAggqHGGNRDADYLALNPNGLVPLLRDDETDVVlwESNTIVRYLAAQYGQKRLWIdAPAARA 93
Cdd:PLN02817  77 QRVLLTLEEKHLPYDMKLV---DLTNKPEWFLKISPEGKVPVVKLDEKWVA--DSDVITQALEEKYPDPPLAT-PPEKAS 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516  94 VGEKwmdwanqtLSPAhrVILFGLVRTPADqrdlaaieASKQVCDNLFAILDNALADQSWF-SGAEFGTADIAVAPFIYN 172
Cdd:PLN02817 151 VGSK--------IFST--FIGFLKSKDPGD--------GTEQALLDELTSFDDYIKENGPFiNGEKISAADLSLGPKLYH 212

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 489125516 173 LfNVGL----SWT---SRPHLERWYQQLTERPAFQKIVMIP 206
Cdd:PLN02817 213 L-EIALghykNWSvpdSLPFVKSYMKNIFSMESFVKTRALP 252
GST_N_2GST_N cd03041
GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed ...
 1-79 1.52e-07

GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed of uncharacterized 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 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: 239339 [Multi-domain]  Cd Length: 77  Bit Score: 47.34  E-value: 1.52e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489125516   1 MITLWGRNNSTNVKKVLWTLEELELPYnqILAGGQHGGNRDADYLALNPNGLVPLLRDDETDVVLWESNTIVRYLAAQY 79
Cdd:cd03041    1 PLELYEFEGSPFCRLVREVLTELELDV--ILYPCPKGSPKRDKFLEKGGKVQVPYLVDPNTGVQMFESADIVKYLFKTY 77
GST_N_Delta_Epsilon cd03045
GST_N family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved ...
 16-77 8.76e-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: 44.90  E-value: 8.76e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489125516  16 VLWTLEELELPYNQILAGGQHGGNRDADYLALNPNGLVPLLRDDetDVVLWESNTIVRYLAA 77
Cdd:cd03045   15 VLLTAKALGLELNLKEVNLMKGEHLKPEFLKLNPQHTVPTLVDN--GFVLWESHAILIYLVE 74
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 129-191 1.13e-06

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 44.62  E-value: 1.13e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489125516  129 AIEASKQVCDNLFAILDNALADQSWFSGAEFGTADIAVAPFIYNLFNVGLSWTSR---PHLERWYQ 191
Cdd:pfam13410   1 ALERAREQLRAALDALEARLADGPGLLGDRPTLADIALAPVLARLDAAYPGLDLRegyPRLRAWLE 66
GST_N_1 cd03043
GST_N family, unknown subfamily 1; composed of uncharacterized proteins, predominantly from ...
 20-76 8.15e-06

GST_N family, unknown subfamily 1; composed of uncharacterized proteins, predominantly from bacteria, 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: 239341 [Multi-domain]  Cd Length: 73  Bit Score: 42.20  E-value: 8.15e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489125516  20 LEELELPYNQILAGGQHGGNRdADYLALNPNGLVPLLRDDETDVvlWESNTIVRYLA 76
Cdd:cd03043   20 LKAAGIPFEEILVPLYTPDTR-ARILEFSPTGKVPVLVDGGIVV--WDSLAICEYLA 73
GST_C_YghU_like cd10292
C-terminal, alpha helical domain of Escherichia coli Yghu Glutathione S-transferases and ...
 129-201 9.18e-06

C-terminal, alpha helical domain of Escherichia coli Yghu Glutathione S-transferases and related uncharacterized proteins; Glutathione S-transferase (GST) C-terminal domain family, YghU-like subfamily; composed of the Escherichia coli YghU 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. YghU is one of nine GST homologs in the genome of Escherichia coli. It is similar to Escherichia coli YfcG in that it has poor GSH transferase activity towards typical substrates. It shows modest reductase activity towards some organic hydroperoxides. Like YfcG, YghU also shows good disulfide bond oxidoreductase activity comparable to the activities of glutaredoxins and thioredoxins. YghU 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 YghU reveals two GSH molecules bound in its active site.


Pssm-ID: 198325 [Multi-domain]  Cd Length: 118  Bit Score: 43.22  E-value: 9.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516 129 AIEASKQVcdnlfAILDNALADQSWFSGAEFGTADIAVAPFIYNLFNVG-------LSWTSRPHLERWYQQLTERPAFQK 201
Cdd:cd10292   42 TMEAKRQL-----DVLDRQLATHKYLAGDEYTIADMAIWPWYGGLALGSlydaaefLDVDEYKHVQRWAKDIAARPAVKR 116
GST_C_GTT2_like cd03182
C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione ...
 131-199 1.10e-05

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: 43.08  E-value: 1.10e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489125516 131 EASKQVCDNLFAILDNALADQSWFSGAEFGTADIAVapFIYNLFNVGLSWT---SRPHLERWYQQLTERPAF 199
Cdd:cd03182   47 ERNKKRVIDFLPVLDKRLAESPYVAGDRFSIADITA--FVALDFAKNLKLPvpeELTALRRWYERMAARPSA 116
GST_C_GDAP1_like cd03204
C-terminal, alpha helical domain of Ganglioside-induced differentiation-associated protein ...
 151-199 3.66e-05

C-terminal, alpha helical domain of Ganglioside-induced differentiation-associated protein 1-like proteins; Glutathione S-transferase (GST) C-terminal domain family, Ganglioside-induced differentiation-associated protein 1 (GDAP1)-like 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 thioredoxin-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: 198313  Cd Length: 111  Bit Score: 41.67  E-value: 3.66e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489125516 151 QSWFSGAEFGTADIAVAPFIYNLFNVGLS---WT--SRPHLERWYQQLTERPAF 199
Cdd:cd03204   58 QQWLCGESFTAADISLSVLLHRLKFLGLSrrfWGngKRPNIESYFERVRQRESF 111
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
 9-75 4.13e-05

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: 40.36  E-value: 4.13e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516   9 NSTNVKKVLWTLEE--LELPYNQI-LAGGQHGGNRdadYLALNPNGLVPLLRDDEtDVVLWESNTIVRYL 75
Cdd:cd03051    8 TAPNPRRVRIFLAEkgIDVPLVTVdLAAGEQRSPE---FLAKNPAGTVPVLELDD-GTVITESVAICRYL 73
GST_C_GDAP1 cd10303
C-terminal, alpha helical domain of Ganglioside-induced differentiation-associated protein 1; ...
 151-199 5.30e-05

C-terminal, alpha helical domain of Ganglioside-induced differentiation-associated protein 1; Glutathione S-transferase (GST) C-terminal domain 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 thioredoxin-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: 198336 [Multi-domain]  Cd Length: 111  Bit Score: 41.15  E-value: 5.30e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489125516 151 QSWFSGAEFGTADIAVAPFIYNLFNVGLS---WTS--RPHLERWYQQLTERPAF 199
Cdd:cd10303   58 QPWLCGEFFSLADVSLAVTLHRLKFLGLArrnWGNgkRPNLETYYERVLKRKTF 111
GST_N_Zeta cd03042
GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 25-75 6.21e-05

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: 39.86  E-value: 6.21e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489125516  25 LPYNQI---LAGGQHggnRDADYLALNPNGLVPLLRDDetDVVLWESNTIVRYL 75
Cdd:cd03042   24 LDYEYVpvnLLKGEQ---LSPAYRALNPQGLVPTLVID--GLVLTQSLAIIEYL 72
GST_N_EF1Bgamma cd03044
GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part ...
 3-78 6.91e-05

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: 39.93  E-value: 6.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516   3 TLWGRNNSTNVKKVLWTLE----ELELPYNQilaggQHGGNRDADYLALNPNGLVP-LLRDDETdvVLWESNTIVRYLAA 77
Cdd:cd03044    2 TLYTYPGNPRSLKILAAAKynglDVEIVDFQ-----PGKENKTPEFLKKFPLGKVPaFEGADGF--CLFESNAIAYYVAN 74


                 .
gi 489125516  78 Q 78
Cdd:cd03044   75 L 75
GST_N_Theta cd03050
GST_N family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial ...
 16-79 9.61e-05

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: 39.53  E-value: 9.61e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489125516  16 VLWTLEELELPYNQI---LAGGQHggnRDADYLALNPNGLVPLLRDDetDVVLWESNTIVRYLAAQY 79
Cdd:cd03050   15 VYIFLKLNKIPFEECpidLRKGEQ---LTPEFKKINPFGKVPAIVDG--DFTLAESVAILRYLARKF 76
GST_C_GTT1_like cd03189
C-terminal, alpha helical domain of GTT1-like Glutathione S-transferases; Glutathione ...
 138-197 1.27e-04

C-terminal, alpha helical domain of GTT1-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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. 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: 198298 [Multi-domain]  Cd Length: 123  Bit Score: 40.37  E-value: 1.27e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489125516 138 DNLFAILDNALADQSWFSGAEFGTADI--AVAPFIYNLFNVGLSwtSRPHLERWYQQLTERP 197
Cdd:cd03189   64 KRHLDFLEDHLAKHPYFAGDELTAADImmSFPLEAALARGPLLE--QYPNIAAYLERIEARP 123
GST_C_5 cd03196
C-terminal, alpha helical domain of an unknown subfamily 5 of Glutathione S-transferases; ...
 144-202 2.65e-04

C-terminal, alpha helical domain of an unknown subfamily 5 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 5; 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: 198305 [Multi-domain]  Cd Length: 115  Bit Score: 39.06  E-value: 2.65e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489125516 144 LDNALADQSWFSGAEFGTADIAVAPFIYNLFNVGLSW---TSRPHLERWYQQLTERPAFQKI 202
Cdd:cd03196   53 LEARLSQHAYLFGDRPSLADYAIFPFVRQFAHVDRDWfdaSPYPNLRRWLNRFLQSPLFSKI 114
PLN02378 PLN02378
glutathione S-transferase DHAR1
 14-201 5.61e-04

glutathione S-transferase DHAR1


Pssm-ID: 166019 [Multi-domain]  Cd Length: 213  Bit Score: 39.69  E-value: 5.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516  14 KKVLWTLEELELPYNQILAggqHGGNRDADYLALNPNGLVPLLRDDETDVVlwESNTIVRYLAAQYGQKRLWIDAPAArA 93
Cdd:PLN02378  24 QRALLTLEEKSLTYKIHLI---NLSDKPQWFLDISPQGKVPVLKIDDKWVT--DSDVIVGILEEKYPDPPLKTPAEFA-S 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516  94 VGEKwmdwanqtlspahrviLFGLVRTPADQRDlaAIEASKQVCDNLFAILDNALA--DQSWFSGAEFGTADIAVAPFIY 171
Cdd:PLN02378  98 VGSN----------------IFGTFGTFLKSKD--SNDGSEHALLVELEALENHLKshDGPFIAGERVSAVDLSLAPKLY 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 489125516 172 NLfNVGL----SWT---SRPHLERWYQQLTERPAFQK 201
Cdd:PLN02378 160 HL-QVALghfkSWSvpeSFPHVHNYMKTLFSLDSFEK 195
GST_N_SspA cd03059
GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ...
 38-79 1.02e-03

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: 36.54  E-value: 1.02e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 489125516  38 GNRDADYLALNPNGLVPLLRDdeTDVVLWESNTIVRYLAAQY 79
Cdd:cd03059   34 DNPPEDLAELNPYGTVPTLVD--RDLVLYESRIIMEYLDERF 73
GST_C_Delta_Epsilon cd03177
C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; ...
 113-202 1.03e-03

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: 37.51  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516 113 ILFGlvRTPADQRDLAAIEASkqvcdnlFAILDNALADQSWFSGAEFGTADIAVAPFIYNLFNVGLSWTSRPHLERWYQQ 192
Cdd:cd03177   28 ILFG--GAEPPEEKLDKLEEA-------LEFLETFLEGSDYVAGDQLTIADLSLVATVSTLEVVGFDLSKYPNVAAWYER 98

                         90
                 ....*....|
gi 489125516 193 LTERPAFQKI 202
Cdd:cd03177   99 LKALPPGEEE 108
GST_C_Lambda cd03203
C-terminal, alpha helical domain of Class Lambda Glutathione S-transferases; Glutathione ...
 141-206 2.07e-03

C-terminal, alpha helical domain of Class Lambda Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Lambda subfamily; composed of plant-specific class Lambda GSTs. GSTs are cytosolic, usually 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 class Lambda subfamily was recently discovered, together with dehydroascorbate reductases (DHARs), as two outlying groups of the GST superfamily in Arabidopsis thaliana, which contain conserved active site cysteines. Characterization of recombinant A. thaliana proteins show that Lambda class GSTs are monomeric, similar to DHARs. They do not exhibit GSH conjugating or DHAR activities, but are active as thiol transferases, similar to glutaredoxins. Members of this subfamily were originally identified as encoded proteins of the In2-1 gene, which can be induced by treatment with herbicide safeners.


Pssm-ID: 198312  Cd Length: 120  Bit Score: 36.57  E-value: 2.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489125516 141 FAILDNALA---DQSWFSGaEFGTADIAVAPFIY-------NLFNVGLSwTSRPHLERWYQQLTERPAFQKIVMIP 206
Cdd:cd03203   39 FDYLENALSkfdDGPFFLG-QFSLVDIAYAPFIErfqivlsELRNYDIT-AGRPNLAKWIEEMNKIEAYTQTKVDP 112
GST_C_7 cd03206
C-terminal, alpha helical domain of an unknown subfamily 7 of Glutathione S-transferases; ...
 130-199 3.31e-03

C-terminal, alpha helical domain of an unknown subfamily 7 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 7; composed of uncharacterized 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: 198315 [Multi-domain]  Cd Length: 100  Bit Score: 35.66  E-value: 3.31e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516 130 IEASKQVCDNLFAILDNALADQSWFSGAEFGTADIAVAPFIYNLFNVGLSWTSRPHLERWYQQLTERPAF 199
Cdd:cd03206   31 PERARAISHRLLRLLDQHLAGRDWLAGDRPTIADVACYPYIALAPEGGVSLEPYPAIRAWLARVEALPGF 100
GST_C_8 cd03207
C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; ...
 98-198 5.46e-03

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: 35.35  E-value: 5.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516  98 WMDWANQTLSPAhrVILFGLVRTPADQRDLAAIEASKQVCDNLFAILDNALADQSWFSGAEFGTADIAVApfiynlfnVG 177
Cdd:cd03207    4 WLFFAAGTVEPP--LLNKALGRFFEPPWGEPAIAAAYGDLDERLAALEAALAGRPYLVGERFSAADLLLA--------SV 73

                         90       100
                 ....*....|....*....|....*...
gi 489125516 178 LSWT-------SRPHLERWYQQLTERPA 198
Cdd:cd03207   74 LRWArafgllpEYPALRAYVARCTARPA 101
GST_C_6 cd03205
C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; ...
 121-200 7.78e-03

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: 34.87  E-value: 7.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125516 121 PADQRDLAAIEASKQVCDNLFAILDNALADqswFSGAEFGTADIAVApfiynlfnVGLSWT-----------SRPHLERW 189
Cdd:cd03205   26 PEEKQHQPWIERQWGKIERALDALEAELGD---LPGGRLTLGDIAVA--------CALGYLdfrfpeldwraGHPALAAW 94

                         90
                 ....*....|.
gi 489125516 190 YQQLTERPAFQ 200
Cdd:cd03205   95 FARFEARPSFQ 105
 
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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