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Conserved domains on  [gi|21355857|ref|NP_649894|]
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glutathione S transferase Z1 [Drosophila melanogaster]

Protein Classification

maleylacetoacetate isomerase( domain architecture ID 11492162)

maleylacetoacetate isomerase is a bifunctional enzyme that shows maleylacetoacetate isomerase activity using glutathione as a cofactor and minimal glutathione-conjugating activity

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
maiA TIGR01262
maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and ...
35-240 3.81e-100

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: 290.38  E-value: 3.81e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857    35 ILYSYWPSSCSWRVRVALAIKKIDYDIKPTSLLKtvSGHAYTDEYREVNPMQKVPSLKIDGHTLCDSVAIIHYLEETRPQ 114
Cdd:TIGR01262   1 KLYSYWRSSCSYRVRIALALKGIDYEYVPVNLLR--DGEQRSPEFLALNPQGLVPTLDIDGEVLTQSLAIIEYLEETYPD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857   115 PALLPQDPVKRAKIREIVELICSGIQPLQNVSVLDHIGK------DQSLQWAQHWISRGFQGLEKVLSHSAGKFCVGDEL 188
Cdd:TIGR01262  79 PPLLPADPIKRARVRALALLIACDIHPLNNLRVLQYLREklgveeEARNRWYQHWISKGFAALEALLQPHAGRFCVGDTP 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 21355857   189 SMADICLVPQVRNARRYKADLTPYPTIVRLNQELQELDVFKATHPSTQPDCP 240
Cdd:TIGR01262 159 TLADLCLVPQVYNAERFGVDLTPYPTLRRIAAALAALPAFQRAHPENQPDTP 210
 
Name Accession Description Interval E-value
maiA TIGR01262
maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and ...
35-240 3.81e-100

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: 290.38  E-value: 3.81e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857    35 ILYSYWPSSCSWRVRVALAIKKIDYDIKPTSLLKtvSGHAYTDEYREVNPMQKVPSLKIDGHTLCDSVAIIHYLEETRPQ 114
Cdd:TIGR01262   1 KLYSYWRSSCSYRVRIALALKGIDYEYVPVNLLR--DGEQRSPEFLALNPQGLVPTLDIDGEVLTQSLAIIEYLEETYPD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857   115 PALLPQDPVKRAKIREIVELICSGIQPLQNVSVLDHIGK------DQSLQWAQHWISRGFQGLEKVLSHSAGKFCVGDEL 188
Cdd:TIGR01262  79 PPLLPADPIKRARVRALALLIACDIHPLNNLRVLQYLREklgveeEARNRWYQHWISKGFAALEALLQPHAGRFCVGDTP 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 21355857   189 SMADICLVPQVRNARRYKADLTPYPTIVRLNQELQELDVFKATHPSTQPDCP 240
Cdd:TIGR01262 159 TLADLCLVPQVYNAERFGVDLTPYPTLRRIAAALAALPAFQRAHPENQPDTP 210
GST_C_Zeta cd03191
C-terminal, alpha helical domain of Class Zeta Glutathione S-transferases; Glutathione ...
122-236 1.72e-64

C-terminal, alpha helical domain of Class Zeta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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. 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: 198300 [Multi-domain]  Cd Length: 121  Bit Score: 196.65  E-value: 1.72e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857 122 PVKRAKIREIVELICSGIQPLQNVSVLDHIGK------DQSLQWAQHWISRGFQGLEKVLSHSAGKFCVGDELSMADICL 195
Cdd:cd03191   1 PKKRARVRAIALIIACDIHPLQNLRVLKYLTEklgvseEEKLAWAQHWIERGFQALEKLLASTAGKYCVGDEPTLADICL 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 21355857 196 VPQVRNARRYKADLTPYPTIVRLNQELQELDVFKATHPSTQ 236
Cdd:cd03191  81 VPQVYNARRFGVDLSPYPTIVRINEACLELPAFQAAHPENQ 121
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
35-238 5.10e-61

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 190.49  E-value: 5.10e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857  35 ILYSYWPSSCSWRVRVALAIKKIDYDIKPTSLLKtvsGHAYTDEYREVNPMQKVPSLKIDGHTLCDSVAIIHYLEETRPQ 114
Cdd:COG0625   3 KLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAK---GEQKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857 115 PALLPQDPVKRAKIREIVELICSGIQP--LQNVSVLDHIGKDQSLQWAQHWISRGFQGLEKVLshSAGKFCVGDELSMAD 192
Cdd:COG0625  80 PPLLPADPAARARVRQWLAWADGDLHPalRNLLERLAPEKDPAAIARARAELARLLAVLEARL--AGGPYLAGDRFSIAD 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 21355857 193 ICLVPQVRNARRYKADLTPYPTIVRLNQELQELDVFKATHPSTQPD 238
Cdd:COG0625 158 IALAPVLRRLDRLGLDLADYPNLAAWLARLAARPAFQRALAAAEPD 203
PRK15113 PRK15113
glutathione transferase;
48-131 1.89e-14

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 69.99  E-value: 1.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857   48 VRVALAIKKIDYDIKPTSLlktVSGHAYTDEYREVNPMQKVPSLKIDGHTLCDSVAIIHYLEETRPQP---ALLPQDPVK 124
Cdd:PRK15113  22 AFVALQEKGLPFELKTVDL---DAGEHLQPTYQGYSLTRRVPTLQHDDFELSESSAIAEYLEERFAPPaweRIYPADLQA 98

                 ....*..
gi 21355857  125 RAKIREI 131
Cdd:PRK15113  99 RARARQI 105
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
42-111 4.82e-13

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 62.26  E-value: 4.82e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21355857    42 SSCSWRVRVALAIKKIDYDIKPTSLLktvsGHAYTDEYREVNPMQKVPSLK-IDGHTLCDSVAIIHYLEET 111
Cdd:pfam13409   2 SPFSHRVRLALEEKGLPYEIELVDLD----PKDKPPELLALNPLGTVPVLVlPDGTVLTDSLVILEYLEEL 68
 
Name Accession Description Interval E-value
maiA TIGR01262
maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and ...
35-240 3.81e-100

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: 290.38  E-value: 3.81e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857    35 ILYSYWPSSCSWRVRVALAIKKIDYDIKPTSLLKtvSGHAYTDEYREVNPMQKVPSLKIDGHTLCDSVAIIHYLEETRPQ 114
Cdd:TIGR01262   1 KLYSYWRSSCSYRVRIALALKGIDYEYVPVNLLR--DGEQRSPEFLALNPQGLVPTLDIDGEVLTQSLAIIEYLEETYPD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857   115 PALLPQDPVKRAKIREIVELICSGIQPLQNVSVLDHIGK------DQSLQWAQHWISRGFQGLEKVLSHSAGKFCVGDEL 188
Cdd:TIGR01262  79 PPLLPADPIKRARVRALALLIACDIHPLNNLRVLQYLREklgveeEARNRWYQHWISKGFAALEALLQPHAGRFCVGDTP 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 21355857   189 SMADICLVPQVRNARRYKADLTPYPTIVRLNQELQELDVFKATHPSTQPDCP 240
Cdd:TIGR01262 159 TLADLCLVPQVYNAERFGVDLTPYPTLRRIAAALAALPAFQRAHPENQPDTP 210
GST_C_Zeta cd03191
C-terminal, alpha helical domain of Class Zeta Glutathione S-transferases; Glutathione ...
122-236 1.72e-64

C-terminal, alpha helical domain of Class Zeta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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. 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: 198300 [Multi-domain]  Cd Length: 121  Bit Score: 196.65  E-value: 1.72e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857 122 PVKRAKIREIVELICSGIQPLQNVSVLDHIGK------DQSLQWAQHWISRGFQGLEKVLSHSAGKFCVGDELSMADICL 195
Cdd:cd03191   1 PKKRARVRAIALIIACDIHPLQNLRVLKYLTEklgvseEEKLAWAQHWIERGFQALEKLLASTAGKYCVGDEPTLADICL 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 21355857 196 VPQVRNARRYKADLTPYPTIVRLNQELQELDVFKATHPSTQ 236
Cdd:cd03191  81 VPQVYNARRFGVDLSPYPTIVRINEACLELPAFQAAHPENQ 121
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
35-238 5.10e-61

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 190.49  E-value: 5.10e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857  35 ILYSYWPSSCSWRVRVALAIKKIDYDIKPTSLLKtvsGHAYTDEYREVNPMQKVPSLKIDGHTLCDSVAIIHYLEETRPQ 114
Cdd:COG0625   3 KLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAK---GEQKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857 115 PALLPQDPVKRAKIREIVELICSGIQP--LQNVSVLDHIGKDQSLQWAQHWISRGFQGLEKVLshSAGKFCVGDELSMAD 192
Cdd:COG0625  80 PPLLPADPAARARVRQWLAWADGDLHPalRNLLERLAPEKDPAAIARARAELARLLAVLEARL--AGGPYLAGDRFSIAD 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 21355857 193 ICLVPQVRNARRYKADLTPYPTIVRLNQELQELDVFKATHPSTQPD 238
Cdd:COG0625 158 IALAPVLRRLDRLGLDLADYPNLAAWLARLAARPAFQRALAAAEPD 203
GST_N_Zeta cd03042
GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
34-109 6.23e-38

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: 127.30  E-value: 6.23e-38
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21355857  34 PILYSYWPSSCSWRVRVALAIKKIDYDIKPTSLLKtvsGHAYTDEYREVNPMQKVPSLKIDGHTLCDSVAIIHYLE 109
Cdd:cd03042   1 MILYSYFRSSASYRVRIALNLKGLDYEYVPVNLLK---GEQLSPAYRALNPQGLVPTLVIDGLVLTQSLAIIEYLD 73
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
34-109 5.91e-20

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: 80.69  E-value: 5.91e-20
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21355857  34 PILYSYWPSSCSWRVRVALAIKKIDYDIKPTSLLKtvsghAYTDEYREVNPMQKVPSLKIDGHTLCDSVAIIHYLE 109
Cdd:cd00570   1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGE-----GEQEEFLALNPLGKVPVLEDGGLVLTESLAILEYLA 71
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
35-108 7.86e-15

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: 67.21  E-value: 7.86e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21355857  35 ILYSYWPSSCSWRVRVALAIKKIDYDIKPTSLLKtvsGHAYTDEYREVNPMQKVPSLKIDGHTLCDSVAIIHYL 108
Cdd:cd03056   2 KLYGFPLSGNCYKVRLLLALLGIPYEWVEVDILK---GETRTPEFLALNPNGEVPVLELDGRVLAESNAILVYL 72
PRK15113 PRK15113
glutathione transferase;
48-131 1.89e-14

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 69.99  E-value: 1.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857   48 VRVALAIKKIDYDIKPTSLlktVSGHAYTDEYREVNPMQKVPSLKIDGHTLCDSVAIIHYLEETRPQP---ALLPQDPVK 124
Cdd:PRK15113  22 AFVALQEKGLPFELKTVDL---DAGEHLQPTYQGYSLTRRVPTLQHDDFELSESSAIAEYLEERFAPPaweRIYPADLQA 98

                 ....*..
gi 21355857  125 RAKIREI 131
Cdd:PRK15113  99 RARARQI 105
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
42-111 4.82e-13

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 62.26  E-value: 4.82e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21355857    42 SSCSWRVRVALAIKKIDYDIKPTSLLktvsGHAYTDEYREVNPMQKVPSLK-IDGHTLCDSVAIIHYLEET 111
Cdd:pfam13409   2 SPFSHRVRLALEEKGLPYEIELVDLD----PKDKPPELLALNPLGTVPVLVlPDGTVLTDSLVILEYLEEL 68
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
34-113 5.03e-13

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: 62.52  E-value: 5.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857  34 PILYsYWPSSCSWRVRVALAIKKIDYDIKPTSLLKTVSGHAytdEYREVNPMQKVPSLKIDGHTLCDSVAIIHYLEETRP 113
Cdd:cd03046   1 ITLY-HLPRSRSFRILWLLEELGLPYELVLYDRGPGEQAPP---EYLAINPLGKVPVLVDGDLVLTESAAIILYLAEKYG 76
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
36-115 7.37e-13

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 61.86  E-value: 7.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857    36 LYSYWPSSCSWRVRVALAIKKIDYDIKPTSLLKTVsghaytDEYREVNPMQKVPSLKIDGHTLCDSVAIIHYLEETRPQP 115
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHP------PELLAKNPLGKVPVLEDDGGILCESLAIIDYLEELYPGP 74
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
35-110 1.09e-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: 61.55  E-value: 1.09e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21355857    35 ILYSYWPSSCSWRVRVALAIKKIDYDIKPtslLKTVSGHAYTDEYREVNPMQKVPSLKIDGHTLCDSVAIIHYLEE 110
Cdd:pfam02798   4 TLYGIRGSPRAHRIRWLLAEKGVEYEIVP---LDFGAGPEKSPELLKLNPLGKVPALEDGGKKLTESRAILEYIAR 76
PRK10357 PRK10357
putative glutathione S-transferase; Provisional
75-233 1.42e-11

putative glutathione S-transferase; Provisional


Pssm-ID: 182405 [Multi-domain]  Cd Length: 202  Bit Score: 61.66  E-value: 1.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857   75 YTDEYR--EVNPMQKVPSLKID-GHTLCDSVAIIHYLEETRPQPALLPQDPVKRAKIREIvELICSGIQPLQNVSVLDHI 151
Cdd:PRK10357  34 YNADNGvaQYNPLGKVPALVTEeGECWFDSPIIAEYIELLNVAPAMLPRDPLAALRVRQL-EALADGIMDAALVSVREQA 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857  152 --GKDQSLQWAQHW---ISRGFQGLEKVLSHSAGKfcvGDELSMADI---CLVPQVrNARRykadLTP-----YPTIVRL 218
Cdd:PRK10357 113 rpAAQQSEDELLRQrekINRSLDALEGYLVDGTLK---TDTVNLATIaiaCAVGYL-NFRR----VAPgwcvdRPHLVKL 184
                        170
                 ....*....|....*
gi 21355857  219 NQELQELDVFKATHP 233
Cdd:PRK10357 185 VENLFQRESFARTEP 199
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
36-109 1.54e-10

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: 55.77  E-value: 1.54e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21355857  36 LYSYWPSSCSWRVRVALAIKKIDYDIKPTSLlktVSGHAYTDEYREVNPMQKVPSLKI-DGHTLCDSVAIIHYLE 109
Cdd:cd03051   3 LYDSPTAPNPRRVRIFLAEKGIDVPLVTVDL---AAGEQRSPEFLAKNPAGTVPVLELdDGTVITESVAICRYLE 74
GST_N_Theta cd03050
GST_N family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial ...
56-108 4.70e-10

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: 54.56  E-value: 4.70e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 21355857  56 KIDYDIKPTSLLKtvsGHAYTDEYREVNPMQKVPSLKIDGHTLCDSVAIIHYL 108
Cdd:cd03050  23 KIPFEECPIDLRK---GEQLTPEFKKINPFGKVPAIVDGDFTLAESVAILRYL 72
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
33-110 1.56e-09

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: 53.04  E-value: 1.56e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21355857  33 KPILYSYWPSSCSWRVRVALAIKKIDYDIKPTSLLKtvsGHAYTDEYREVNPMQKVPSLKIDGHTLCDSVAIIHYLEE 110
Cdd:cd03053   1 VLKLYGAAMSTCVRRVLLCLEEKGVDYELVPVDLTK---GEHKSPEHLARNPFGQIPALEDGDLKLFESRAITRYLAE 75
GST_N_Delta_Epsilon cd03045
GST_N family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved ...
34-110 1.92e-09

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: 52.61  E-value: 1.92e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21355857  34 PILYsYWPSSCSWRVrVALAIKK--IDYDIKPTSLLKtvsGHAYTDEYREVNPMQKVPSLKIDGHTLCDSVAIIHYLEE 110
Cdd:cd03045   1 IDLY-YLPGSPPCRA-VLLTAKAlgLELNLKEVNLMK---GEHLKPEFLKLNPQHTVPTLVDNGFVLWESHAILIYLVE 74
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
35-111 3.67e-09

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: 51.89  E-value: 3.67e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21355857  35 ILYSYWPSSCSWRVRVALAIKKIDYDIKPTSLLKTvsghayTDEYREVNPM-QKVPSLKIDGHTLCDSVAIIHYLEET 111
Cdd:cd03058   2 KLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNK------SELLLASNPVhKKIPVLLHNGKPICESLIIVEYIDEA 73
GST_N_Ure2p_like cd03048
GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related ...
35-111 1.94e-08

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: 50.24  E-value: 1.94e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857  35 ILYSyWPSSCSWRVRVALAIKKIDYDIKPTSLLKtvsGHAYTDEYREVNPMQKVPSLkID----GHTLCDSVAIIHYLEE 110
Cdd:cd03048   3 TLYT-HGTPNGFKVSIMLEELGLPYEIHPVDISK---GEQKKPEFLKINPNGRIPAI-VDhngtPLTVFESGAILLYLAE 77

                .
gi 21355857 111 T 111
Cdd:cd03048  78 K 78
GST_N_Beta cd03057
GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
36-113 7.01e-08

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: 48.69  E-value: 7.01e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21355857  36 LYsYWPSSCSWRVRVALAIKKIDYDIKPTSLLKTVSGhayTDEYREVNPMQKVPSLKI-DGHTLCDSVAIIHYLEETRP 113
Cdd:cd03057   3 LY-YSPGACSLAPHIALEELGLPFELVRVDLRTKTQK---GADYLAINPKGQVPALVLdDGEVLTESAAILQYLADLHP 77
GST_N_etherase_LigE cd03038
GST_N family, Beta etherase LigE subfamily; composed of proteins similar to Sphingomonas ...
46-113 2.95e-06

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: 44.26  E-value: 2.95e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21355857  46 WRVRVALAIKKIDYDIKPTSL---LKTVSGHAYTDEYRevnpmqkVPSLK-IDGHTLCDSVAIIHYLEETRP 113
Cdd:cd03038  20 WKTRLALNHKGLEYKTVPVEFpdiPPILGELTSGGFYT-------VPVIVdGSGEVIGDSFAIAEYLEEAYP 84
sspA PRK09481
stringent starvation protein A; Provisional
45-129 3.43e-06

stringent starvation protein A; Provisional


Pssm-ID: 236537 [Multi-domain]  Cd Length: 211  Bit Score: 46.63  E-value: 3.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857   45 SWRVRVALAIKKIDYDI---KPTSLlktvsghayTDEYREVNPMQKVPSLkIDGH-TLCDSVAIIHYLEETRPQPALLPQ 120
Cdd:PRK09481  22 SHQVRIVLAEKGVSVEIeqvEKDNL---------PQDLIDLNPYQSVPTL-VDRElTLYESRIIMEYLDERFPHPPLMPV 91

                 ....*....
gi 21355857  121 DPVKRAKIR 129
Cdd:PRK09481  92 YPVARGESR 100
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
128-213 2.29e-05

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: 42.10  E-value: 2.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857 128 IREIVELICSGIQPLQNVSVLDHIGKD----QSLQWAQHWISRGFQGLEKVLSHsaGKFCVGDELSMADICLVPQVRNAR 203
Cdd:cd00299   1 VRALEDWADATLAPPLVRLLYLEKVPLpkdeAAVEAAREELPALLAALEQLLAG--RPYLAGDQFSLADVALAPVLARLE 78
                        90
                ....*....|...
gi 21355857 204 R---YKADLTPYP 213
Cdd:cd00299  79 AlgpYYDLLDEYP 91
PLN02378 PLN02378
glutathione S-transferase DHAR1
78-231 3.65e-05

glutathione S-transferase DHAR1


Pssm-ID: 166019 [Multi-domain]  Cd Length: 213  Bit Score: 43.55  E-value: 3.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857   78 EYREVNPMQKVPSLKIDGHTLCDSVAIIHYLEETRPQPALlpQDPVKRAKIreivelicsGIQPLQNVSVLdhIGKDQSL 157
Cdd:PLN02378  50 WFLDISPQGKVPVLKIDDKWVTDSDVIVGILEEKYPDPPL--KTPAEFASV---------GSNIFGTFGTF--LKSKDSN 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857  158 QWAQHWISRGFQGLEKVLSHSAGKFCVGDELSMADICLVPQVRNAR----RYKADLTP--YPTIVRLNQELQELDVFKAT 231
Cdd:PLN02378 117 DGSEHALLVELEALENHLKSHDGPFIAGERVSAVDLSLAPKLYHLQvalgHFKSWSVPesFPHVHNYMKTLFSLDSFEKT 196
PRK10542 PRK10542
glutathionine S-transferase; Provisional
39-215 5.79e-05

glutathionine S-transferase; Provisional


Pssm-ID: 182533 [Multi-domain]  Cd Length: 201  Bit Score: 42.75  E-value: 5.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857   39 YWPSSCSWRVRVALAIKKIDYDIKPTSLL--KTVSGhaytDEYREVNPMQKVPSLKID-GHTLCDSVAIIHYLEETRPQP 115
Cdd:PRK10542   5 YKPGACSLASHITLRESGLDFTLVSVDLAkkRLENG----DDYLAINPKGQVPALLLDdGTLLTEGVAIMQYLADSVPDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857  116 ALL-PQDPVKRAKIREIVELICS----GIQPLQNVSVldhigKDQSLQWAQHWISRGFQGLEKVLSHSagKFCVGDELSM 190
Cdd:PRK10542  81 QLLaPVGSLSRYHTIEWLNYIATelhkGFTPLFRPDT-----PEEYKPTVRAQLEKKFQYVDEALADE--QWICGQRFTI 153
                        170       180
                 ....*....|....*....|....*
gi 21355857  191 ADICLVPQVRNARRYKADLTPYPTI 215
Cdd:PRK10542 154 ADAYLFTVLRWAYAVKLNLEGLEHI 178
GST_C_Sigma_like cd03192
C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione ...
164-220 1.20e-04

C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, including GSTs from class Mu, Pi, and Alpha. 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. Vertebrate class Sigma GSTs are characterized as GSH-dependent hematopoietic prostaglandin (PG) D synthases and are responsible for the production of PGD2 by catalyzing the isomerization of PGH2. The functions of PGD2 include the maintenance of body temperature, inhibition of platelet aggregation, bronchoconstriction, vasodilation, and mediation of allergy and inflammation. Other class Sigma-like members include the class II insect GSTs, S-crystallins from cephalopods, nematode-specific GSTs, and 28-kDa GSTs from parasitic flatworms. Drosophila GST2 is associated with indirect flight muscle and exhibits preference for catalyzing GSH conjugation to lipid peroxidation products, indicating an anti-oxidant role. S-crystallin constitutes the major lens protein in cephalopod eyes and is responsible for lens transparency and proper refractive index. The 28-kDa GST from Schistosoma is a multifunctional enzyme, exhibiting GSH transferase, GSH peroxidase, and PGD2 synthase activities, and may play an important role in host-parasite interactions. Members also include novel GSTs from the fungus Cunninghamella elegans, designated as class Gamma, and from the protozoan Blepharisma japonicum, described as a light-inducible GST.


Pssm-ID: 198301 [Multi-domain]  Cd Length: 104  Bit Score: 40.30  E-value: 1.20e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857 164 ISRGFQGLEKVLSHSAGKFCVGDELSMADICL---VPQVRNARRyKADLTPYPTIVRLNQ 220
Cdd:cd03192  44 LPKFLGKFEKILKKSGGGYFVGDKLTWADLALfdvLDYLLYLLP-KDLLEKYPKLKALRE 102
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
171-218 1.47e-04

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


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 39.85  E-value: 1.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 21355857   171 LEKVLSHSAGKFCVGDELSMADICL---VPQVRNARRYKAdLTPYPTIVRL 218
Cdd:pfam14497  38 FEKVLNKNGGGYLVGDKLTYADLALfqvLDGLLYPKAPDA-LDKYPKLKAL 87
GST_C_Delta_Epsilon cd03177
C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; ...
171-217 2.56e-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: 39.44  E-value: 2.56e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 21355857 171 LEKVLSHSagKFCVGDELSMADICLVPQVRNARRYKADLTPYPTIVR 217
Cdd:cd03177  50 LETFLEGS--DYVAGDQLTIADLSLVATVSTLEVVGFDLSKYPNVAA 94
PLN02395 PLN02395
glutathione S-transferase
35-197 3.29e-04

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 40.62  E-value: 3.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857   35 ILYSYWPS-SCSWRVRVALAIKKIDYDIKPTSLLKtvsGHAYTDEYREVNPMQKVPSLKIDGHTLCDSVAIIHYL-EETR 112
Cdd:PLN02395   2 VLKVYGPAfASPKRALVTLIEKGVEFETVPVDLMK---GEHKQPEYLALQPFGVVPVIVDGDYKIFESRAIMRYYaEKYR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857  113 PQ-PALLPQDPVKRAKIREIVELICSGIQP-LQNVSVLDHIGKDQSLQWAQHWISRGFQGLEKVLS-----HSAGKFCVG 185
Cdd:PLN02395  79 SQgPDLLGKTIEERGQVEQWLDVEATSYHPpLLNLTLHILFASKMGFPADEKVIKESEEKLAKVLDvyearLSKSKYLAG 158
                        170
                 ....*....|..
gi 21355857  186 DELSMADICLVP 197
Cdd:PLN02395 159 DFVSLADLAHLP 170
GST_N_EF1Bgamma cd03044
GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part ...
36-108 7.51e-04

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: 37.23  E-value: 7.51e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21355857  36 LYSYwPSSC-SWRVRVALAIKKIDYDIKPTSLLKTVSghayTDEYREVNPMQKVPSLKI-DGHTLCDSVAIIHYL 108
Cdd:cd03044   3 LYTY-PGNPrSLKILAAAKYNGLDVEIVDFQPGKENK----TPEFLKKFPLGKVPAFEGaDGFCLFESNAIAYYV 72
GST_N_1 cd03043
GST_N family, unknown subfamily 1; composed of uncharacterized proteins, predominantly from ...
45-108 1.08e-03

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: 36.81  E-value: 1.08e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21355857  45 SWRVRVALAIKKidYDIKPTSLLKTVSGHAYTDEYREVNPMQKVPSLKIDGHTLCDSVAIIHYL 108
Cdd:cd03043  11 SWSLRPWLLLKA--AGIPFEEILVPLYTPDTRARILEFSPTGKVPVLVDGGIVVWDSLAICEYL 72
GST_C_YfcG_like cd10291
C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and ...
171-224 1.49e-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: 37.25  E-value: 1.49e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 21355857 171 LEKVLSHSagKFCVGDELSMADICLVPQVRNARRYKADLTPYPTIVRLNQELQE 224
Cdd:cd10291  52 LDRRLAKS--KYLAGDEYSIADIAIWPWVARHEWQGIDLADFPNLKRWFERLAA 103
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
44-117 2.71e-03

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 38.05  E-value: 2.71e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21355857   44 CSWRVRVALAI--KKIDYDIKPTSLLKTvsghayTDEYREVNPMQKVPSLKIDGHTLCDSVAIIHYLEETRPQPAL 117
Cdd:PLN02817  73 CPFCQRVLLTLeeKHLPYDMKLVDLTNK------PEWFLKISPEGKVPVVKLDEKWVADSDVITQALEEKYPDPPL 142
GST_C_5 cd03196
C-terminal, alpha helical domain of an unknown subfamily 5 of Glutathione S-transferases; ...
160-223 3.00e-03

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: 36.36  E-value: 3.00e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355857 160 AQHWISRgfqgLEKVLSHSAgkFCVGDELSMADICLVPQVR-----NARRYKADltPYPTIVR-LNQELQ 223
Cdd:cd03196  46 AEEFLAE----LEARLSQHA--YLFGDRPSLADYAIFPFVRqfahvDRDWFDAS--PYPNLRRwLNRFLQ 107
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
159-213 5.47e-03

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 34.60  E-value: 5.47e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 21355857   159 WAQHWISRGFQGLEKVLSHSAGK-FCVGDELSMADICLVP---QVRNARRYKADLTPYP 213
Cdd:pfam13410   1 ALERAREQLRAALDALEARLADGpGLLGDRPTLADIALAPvlaRLDAAYPGLDLREGYP 59
 
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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