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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356805    6 VLYSYFRSSCSWRVRIALALKGIDYEIVPINLIKDGgQQFSEEFQTLNPMKQVPALKIDGITIGQSLAILEYLEETRPIP 85
Cdd:TIGR01262   1 KLYSYWRSSCSYRVRIALALKGIDYEYVPVNLLRDG-EQRSPEFLALNPQGLVPTLDIDGEVLTQSLAIIEYLEETYPDP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356805   86 RLLPQDPQKRAIVRMISDLIASGIQPLQNLSVLKQVGQ------ENQMPWAQKAITSGFNALEKILQSTAGKYCVGDEVS 159
Cdd:TIGR01262  80 PLLPADPIKRARVRALALLIACDIHPLNNLRVLQYLREklgveeEARNRWYQHWISKGFAALEALLQPHAGRFCVGDTPT 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564356805  160 MADVCLAPQVANAERFKVDLSPYPTISHINKALLALEAFQVSHPCRQPDTP 210
Cdd:TIGR01262 160 LADLCLVPQVYNAERFGVDLTPYPTLRRIAAALAALPAFQRAHPENQPDTP 210

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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356805    6 VLYSYFRSSCSWRVRIALALKGIDYEIVPINLIKDGgQQFSEEFQTLNPMKQVPALKIDGITIGQSLAILEYLEETRPIP 85
Cdd:TIGR01262   1 KLYSYWRSSCSYRVRIALALKGIDYEYVPVNLLRDG-EQRSPEFLALNPQGLVPTLDIDGEVLTQSLAIIEYLEETYPDP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356805   86 RLLPQDPQKRAIVRMISDLIASGIQPLQNLSVLKQVGQ------ENQMPWAQKAITSGFNALEKILQSTAGKYCVGDEVS 159
Cdd:TIGR01262  80 PLLPADPIKRARVRALALLIACDIHPLNNLRVLQYLREklgveeEARNRWYQHWISKGFAALEALLQPHAGRFCVGDTPT 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564356805  160 MADVCLAPQVANAERFKVDLSPYPTISHINKALLALEAFQVSHPCRQPDTP 210
Cdd:TIGR01262 160 LADLCLVPQVYNAERFGVDLTPYPTLRRIAAALAALPAFQRAHPENQPDTP 210

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356805  92 PQKRAIVRMISDLIASGIQPLQNLSVLKQVG------QENQMPWAQKAITSGFNALEKILQSTAGKYCVGDEVSMADVCL 165
Cdd:cd03191    1 PKKRARVRAIALIIACDIHPLQNLRVLKYLTeklgvsEEEKLAWAQHWIERGFQALEKLLASTAGKYCVGDEPTLADICL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 564356805 166 APQVANAERFKVDLSPYPTISHINKALLALEAFQVSHPCRQ 206
Cdd:cd03191   81 VPQVYNARRFGVDLSPYPTIVRINEACLELPAFQAAHPENQ 121

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564356805    7 LYSYFRSSCSWRVRIALALKGIDYEIVPINLikDGGQQFSEEFQTLNPMKQVPALKIDGITIGQSLAILEYLEE 80
Cdd:pfam02798   5 LYGIRGSPRAHRIRWLLAEKGVEYEIVPLDF--GAGPEKSPELLKLNPLGKVPALEDGGKKLTESRAILEYIAR 76

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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356805    6 VLYSYFRSSCSWRVRIALALKGIDYEIVPINLIKDGgQQFSEEFQTLNPMKQVPALKIDGITIGQSLAILEYLEETRPIP 85
Cdd:TIGR01262   1 KLYSYWRSSCSYRVRIALALKGIDYEYVPVNLLRDG-EQRSPEFLALNPQGLVPTLDIDGEVLTQSLAIIEYLEETYPDP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356805   86 RLLPQDPQKRAIVRMISDLIASGIQPLQNLSVLKQVGQ------ENQMPWAQKAITSGFNALEKILQSTAGKYCVGDEVS 159
Cdd:TIGR01262  80 PLLPADPIKRARVRALALLIACDIHPLNNLRVLQYLREklgveeEARNRWYQHWISKGFAALEALLQPHAGRFCVGDTPT 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564356805  160 MADVCLAPQVANAERFKVDLSPYPTISHINKALLALEAFQVSHPCRQPDTP 210
Cdd:TIGR01262 160 LADLCLVPQVYNAERFGVDLTPYPTLRRIAAALAALPAFQRAHPENQPDTP 210

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356805  92 PQKRAIVRMISDLIASGIQPLQNLSVLKQVG------QENQMPWAQKAITSGFNALEKILQSTAGKYCVGDEVSMADVCL 165
Cdd:cd03191    1 PKKRARVRAIALIIACDIHPLQNLRVLKYLTeklgvsEEEKLAWAQHWIERGFQALEKLLASTAGKYCVGDEPTLADICL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 564356805 166 APQVANAERFKVDLSPYPTISHINKALLALEAFQVSHPCRQ 206
Cdd:cd03191   81 VPQVYNARRFGVDLSPYPTIVRINEACLELPAFQAAHPENQ 121

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564356805   5 PVLYSYFRSSCSWRVRIALALKGIDYEIVPINLikdgGQQFSEEFQTLNPMKQVPALKIDGITIGQSLAILEYLE 79
Cdd:cd00570    1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDL----GEGEQEEFLALNPLGKVPVLEDGGLVLTESLAILEYLA 71

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564356805    7 LYSYFRSSCSWRVRIALALKGIDYEIVPINLikDGGQQFSEEFQTLNPMKQVPALKIDGITIGQSLAILEYLEE 80
Cdd:pfam02798   5 LYGIRGSPRAHRIRWLLAEKGVEYEIVPLDF--GAGPEKSPELLKLNPLGKVPALEDGGKKLTESRAILEYIAR 76

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564356805   7 LYSYFRSSCSWRVRIALALKGIDYEIVPINLIKdgGQQFSEEFQTLNPMKQVPALKIDGITIGQSLAILEYLEE 80
Cdd:cd03053    4 LYGAAMSTCVRRVLLCLEEKGVDYELVPVDLTK--GEHKSPEHLARNPFGQIPALEDGDLKLFESRAITRYLAE 75

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356805   13 SSCSWRVRIALALKGIDYEIVPINLIkdgGQQFSEEFQTLNPMKQVPALK-IDGITIGQSLAILEYLEET 81
Cdd:pfam13409   2 SPFSHRVRLALEEKGLPYEIELVDLD---PKDKPPELLALNPLGTVPVLVlPDGTVLTDSLVILEYLEEL 68

Glutathione S-transferase, N-terminal domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356805    7 LYSYFRSSCSWRVRIALALKGIDYEIVPINLikdggQQFSEEFQTLNPMKQVPALKIDGITIGQSLAILEYLEETRPIPR 86
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPP-----GDHPPELLAKNPLGKVPVLEDDGGILCESLAIIDYLEELYPGPP 75

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564356805   7 LYsYFRSSCSWRVRIALALKGIDYEIVPINLikDGGQQFSEEFQTLNPMKQVPALKI-DGITIGQSLAILEYLEETRP 83
Cdd:cd03057    3 LY-YSPGACSLAPHIALEELGLPFELVRVDL--RTKTQKGADYLAINPKGQVPALVLdDGEVLTESAAILQYLADLHP 77

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564356805   6 VLYSYFRSSCSWRVRIALALKGIDYEIVPINLIKDggqqfSEEFQTLNPM-KQVPALKIDGITIGQSLAILEYLEET 81
Cdd:cd03058    2 KLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNK-----SELLLASNPVhKKIPVLLHNGKPICESLIIVEYIDEA 73

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564356805   5 PVLYSYFRSSCSWRVRIALALKGIDYEIVPINLIKdgGQQFSEEFQTLNPMKQVPALKIDGITIGQSLAILEYLEE 80
Cdd:cd03045    1 IDLYYLPGSPPCRAVLLTAKALGLELNLKEVNLMK--GEHLKPEFLKLNPQHTVPTLVDNGFVLWESHAILIYLVE 74

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356805  95 RAIVRMISDLIASGIQPLQNLSVLKQVGQENQMPWAQKAITSGFNALEKILQSTagKYCVGDEVSMADVCLAPQVANAER 174
Cdd:cd00299    2 RALEDWADATLAPPLVRLLYLEKVPLPKDEAAVEAAREELPALLAALEQLLAGR--PYLAGDQFSLADVALAPVLARLEA 79

                         90
                 ....*....|..
gi 564356805 175 FKV---DLSPYP 183
Cdd:cd00299   80 LGPyydLLDEYP 91

stringent starvation protein A; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356805  16 SWRVRIALALKGIDYEIV---PINLikdggqqfSEEFQTLNPMKQVPALKIDGITIGQSLAILEYLEETRPIPRLLPQDP 92
Cdd:PRK09481  22 SHQVRIVLAEKGVSVEIEqveKDNL--------PQDLIDLNPYQSVPTLVDRELTLYESRIIMEYLDERFPHPPLMPVYP 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564356805  93 QKRAIVRMISDLIASGIQPLQNLsVLKQVGQENQMpwAQKAITSGFNALEKILQSTAgkYCVGDEVSMADVCLAP 167
Cdd:PRK09481  94 VARGESRLMMHRIEKDWYSLMNK-IVNGSASEADA--ARKQLREELLAIAPVFGEKP--YFMSEEFSLVDCYLAP 163

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564356805   6 VLYSYFRSSCSWRVRIALALKGIDYEIVPINLikdggQQFSEEFQTLNPMKQVPALKIDGITIGQSLAILEYLEE 80
Cdd:cd03059    2 TLYSGPDDVYSHRVRIVLAEKGVSVEIIDVDP-----DNPPEDLAELNPYGTVPTLVDRDLVLYESRIIMEYLDE 71

glutathione S-transferase DHAR1

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356805  16 SWRVRIALALKGIDYEIVPINLiKDGGQQFSEefqtLNPMKQVPALKIDGITIGQSLAILEYLEETRPIPRLlpQDPQKR 95
Cdd:PLN02378  23 SQRALLTLEEKSLTYKIHLINL-SDKPQWFLD----ISPQGKVPVLKIDDKWVTDSDVIVGILEEKYPDPPL--KTPAEF 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356805  96 AIVrmisdliasGIQPLQNLSVLKQVGQENQmpWAQKAITSGFNALEKILQSTAGKYCVGDEVSMADVCLAPQVANAE-- 173
Cdd:PLN02378  96 ASV---------GSNIFGTFGTFLKSKDSND--GSEHALLVELEALENHLKSHDGPFIAGERVSAVDLSLAPKLYHLQva 164

                        170       180       190
                 ....*....|....*....|....*....|
gi 564356805 174 --RFKVDLSP--YPTISHINKALLALEAFQ 199
Cdd:PLN02378 165 lgHFKSWSVPesFPHVHNYMKTLFSLDSFE 194

GSH-dependent disulfide bond oxidoreductase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356805  18 RVRIALALKGIDYEIVPINLIKDGgqQFSEEFQTLNPMKQVPAL----KIDG---ITIGQSLAILEYLEETRPIprLLPQ 90
Cdd:PRK13972  14 KITLFLEEAELDYRLIKVDLGKGG--QFRPEFLRISPNNKIPAIvdhsPADGgepLSLFESGAILLYLAEKTGL--FLSH 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356805  91 DPQKRAIVRMISDLIASGIQPLQNLSVLKQVGQENQMPWA----QKAITSGFNALEKILQSTAgkYCVGDEVSMADVCLA 166
Cdd:PRK13972  90 ETRERAATLQWLFWQVGGLGPMLGQNHHFNHAAPQTIPYAieryQVETQRLYHVLNKRLENSP--WLGGENYSIADIACW 167

                        170       180
                 ....*....|....*....|.
gi 564356805 167 PQVANAERFKVDLSPYPTISH 187
Cdd:PRK13972 168 PWVNAWTRQRIDLAMYPAVKN 188

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564356805   7 LYSYFRSSCSWRVRIALALKGIDYEIVPInliKDGGQQFSEEFQTLNPMKQVPALKI-DGITIGQSLAILEYL 78
Cdd:cd03044    3 LYTYPGNPRSLKILAAAKYNGLDVEIVDF---QPGKENKTPEFLKKFPLGKVPAFEGaDGFCLFESNAIAYYV 72

glutathionine S-transferase; Provisional

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564356805  14 SCSWRVRIALALKGIDYEIVPINLIKDGGQQfSEEFQTLNPMKQVPALKID-GITIGQSLAILEYLEETRPIPRLLP 89
Cdd:PRK10542   9 ACSLASHITLRESGLDFTLVSVDLAKKRLEN-GDDYLAINPKGQVPALLLDdGTLLTEGVAIMQYLADSVPDRQLLA 84

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564356805 141 LEKILQSTagKYCVGDEVSMADVCLAPQVANAERFKVDLSPYPTISHINKALLALEAFQ 199
Cdd:cd10291   52 LDRRLAKS--KYLAGDEYSIADIAIWPWVARHEWQGIDLADFPNLKRWFERLAARPAVQ 108

glutathione S-transferase

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356805   7 LYSYFRSSCSWRVRIALALKGIDYEIVPINLikDGGQQFSEEFQTLNPMKQVPALKIDGITIGQSLAILEYLeETRPIPR 86
Cdd:PLN02473   5 VYGQIKAANPQRVLLCFLEKGIEFEVIHVDL--DKLEQKKPEHLLRQPFGQVPAIEDGDLKLFESRAIARYY-ATKYADQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356805  87 ---LLPQDPQKRAIVRMISDL----IASGIQPL-QNLSVLKQVGQENQMPWAQKaITSGFNALEKILQS--TAGKYCVGD 156
Cdd:PLN02473  82 gtdLLGKTLEHRAIVDQWVEVennyFYAVALPLvINLVFKPRLGEPCDVALVEE-LKVKFDKVLDVYENrlATNRYLGGD 160

                        170
                 ....*....|.
gi 564356805 157 EVSMADVCLAP 167
Cdd:PLN02473 161 EFTLADLTHMP 171

NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active CXXC motif within a TRX fold, characterized by a glutaredoxin (GRX)-like sequence and TRX-like activity profile. In vitro, it displays protein disulfide reductase activity that is dependent on TRX reductase, not glutathione (GSH). It is part of the NrdHIEF operon, where NrdEF codes for class Ib ribonucleotide reductase (RNR-Ib), an efficient enzyme at low oxygen levels. Under these conditions when GSH is mostly conjugated to spermidine, NrdH can still function and act as a hydrogen donor for RNR-Ib. It has been suggested that the NrdHEF system may be the oldest RNR reducing system, capable of functioning in a microaerophilic environment, where GSH was not yet available. NrdH from Corynebacterium ammoniagenes can form domain-swapped dimers, although it is unknown if this happens in vivo. Domain-swapped dimerization, which results in the blocking of the TRX reductase binding site, could be a mechanism for regulating the oxidation state of the protein.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564356805   6 VLYSyfRSSCSW--RVRIALALKGIDYEIVPInlikDGGQQFSEEFQTLNPMKQVPALKIDG 65
Cdd:cd02976    3 TVYT--KPDCPYckATKRFLDERGIPFEEVDV----DEDPEALEELKKLNGYRSVPVVVIGD 58

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 564356805 141 LEKILQSTAgkYCVGDEVSMADVCLAP---QVANAERFKVDLSPYPTI 185
Cdd:cd03196   53 LEARLSQHA--YLFGDRPSLADYAIFPfvrQFAHVDRDWFDASPYPNL 98

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

                          10        20
                  ....*....|....*....|....*...
gi 564356805  138 FNALEKILQSTAGKYCVGDEVSMADVCL 165
Cdd:pfam14497  35 LGYFEKVLNKNGGGYLVGDKLTYADLAL 62

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564356805  27 GIDYEIVPInlikdgGQQF----SEEFQTLNPMKQVPALKIDGITIGQSLAILEYL 78
Cdd:cd03047   23 GLPYERIDA------GGQFggldTPEFLAMNPNGRVPVLEDGDFVLWESNAILRYL 72

GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to class Omega GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Class Omega GSTs show little or no GSH-conjugating activity towards standard GST substrates. Instead, they catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins. Like Omega enzymes, proteins in this subfamily contain a conserved cysteine equivalent to the first cysteine in the CXXC motif of glutaredoxins, which is a redox active residue capable of reducing GSH mixed disulfides in a monothiol mechanism.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564356805   5 PVLYSYFRSSCSWRVRIALALKGIDYEIVPINLiKDGgqqfSEEFQTLNPMKQVPAL-KIDGITIGQSLAIL 75
Cdd:cd03060    1 PILYSFRRCPYAMRARMALLLAGITVELREVEL-KNK----PAEMLAASPKGTVPVLvLGNGTVIEESLDIM 67

C-terminal, alpha helical domain of Class Alpha Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Alpha subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The class Alpha subfamily is composed of vertebrate GSTs which can form homodimer and heterodimers. There are at least six types of class Alpha GST subunits in rats, four of which have human counterparts, resulting in many possible isoenzymes with different activities, tissue distribution and substrate specificities. Human GSTA1-1 and GSTA2-2 show high GSH peroxidase activity. GSTA3-3 catalyzes the isomerization of intermediates in steroid hormone biosynthesis. GSTA4-4 preferentially catalyzes the GSH conjugation of alkenals.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564356805 130 AQKAITSGFNALEKILQSTAGKYCVGDEVSMADVCLAPQVANAERFKVD-LSPYP 183
Cdd:cd03208   40 KEKAKNRYFPVFEKVLKDHGQDFLVGNKLSRADVQLLEAILMVEELDPSiLSDFP 94

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564356805 119 KQVGQENQMPWAQKAITSGF-------NALEKILQstAGKYCVGDEVSMADVCLAPQVANAERFKvDLSPYPTI 185
Cdd:cd03207   19 KALGRFFEPPWGEPAIAAAYgdlderlAALEAALA--GRPYLVGERFSAADLLLASVLRWARAFG-LLPEYPAL 89