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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641620   5 SARSLGKGSAPPGPVPeGQIRVYSMRFCPFAQRTLMVLKAKGIRHEIININLKNKPEWFFEKNPFGLVPVLENTQGHLIT 84
Cdd:cd03055     1 SSKHLAKGSAEPPPVP-GIIRLYSMRFCPYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPQGKVPALEIDEGKVVY 79

                          90
                  ....*....|
gi 1958641620  85 ESVITCEYLD 94
Cdd:cd03055    80 ESLIICEYLD 89

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641620   5 SARSLGKGSAPPGPVPeGQIRVYSMRFCPFAQRTLMVLKAKGIRHEIININLKNKPEWFFEKNPFGLVPVLENTQGHLIT 84
Cdd:cd03055     1 SSKHLAKGSAEPPPVP-GIIRLYSMRFCPYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPQGKVPALEIDEGKVVY 79

                          90
                  ....*....|
gi 1958641620  85 ESVITCEYLD 94
Cdd:cd03055    80 ESLIICEYLD 89

C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal 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 Omega GSTs show little or no GSH-conjugating activity towards standard GST substrates. Instead, they catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins. They contain a conserved cysteine equivalent to the first cysteine in the CXXC motif of glutaredoxins, which is a redox active residue capable of reducing GSH mixed disulfides in a monothiol mechanism. Polymorphisms of the class Omega GST genes may be associated with the development of some types of cancer and the age-at-onset of both Alzheimer's and Parkinson's diseases.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641620 108 YEKACQKMTFELFSKVPSLVTSFIRAKRKEdhPGIKEELKKEFSKLEEAMAKKRTAFFGGNSLSMIDYLIWPWFQRLEAL 187
Cdd:cd03184     1 YEKAQQKMLIERFSKVPSAFYKFLRSGEDR--KGLKEELRSALENLEEELAKRGTPFFGGNSPGMVDYMIWPWFERLEAL 78

                          90
                  ....*....|...
gi 1958641620 188 ELN-EFFLSELGT 199
Cdd:cd03184    79 KLLdGYELCLDRF 91

glutathione dehydrogenase (ascorbate)

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641620  32 CPFAQRTLMVLKAKGIRHEIININLKNKPEWFFEKNPFGLVPVLENTQGHLITESVITcEYLDEAYPEKKLfpDDPYEKA 111
Cdd:PLN02817   73 CPFCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISPEGKVPVVKLDEKWVADSDVIT-QALEEKYPDPPL--ATPPEKA 149

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958641620 112 cqkmtfELFSKVPSLVTSFIRAKRKEDhpGIKEELKKEFSKLEEAMaKKRTAFFGGNSLSMIDYLIWPWFQRLE 185
Cdd:PLN02817  150 ------SVGSKIFSTFIGFLKSKDPGD--GTEQALLDELTSFDDYI-KENGPFINGEKISAADLSLGPKLYHLE 214

glutathione transferase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641620  31 FCPFAQRTLMVLKAKGIRHEIININLKNK----PEWFfEKNPFGLVPVLENTQGHLiTESVITCEYLDEAYPE---KKLF 103
Cdd:PRK15113   15 FSPYVMSAFVALQEKGLPFELKTVDLDAGehlqPTYQ-GYSLTRRVPTLQHDDFEL-SESSAIAEYLEERFAPpawERIY 92

                  ....*...
gi 1958641620 104 PDDPYEKA 111
Cdd:PRK15113   93 PADLQARA 100

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641620   5 SARSLGKGSAPPGPVPeGQIRVYSMRFCPFAQRTLMVLKAKGIRHEIININLKNKPEWFFEKNPFGLVPVLENTQGHLIT 84
Cdd:cd03055     1 SSKHLAKGSAEPPPVP-GIIRLYSMRFCPYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPQGKVPALEIDEGKVVY 79

                          90
                  ....*....|
gi 1958641620  85 ESVITCEYLD 94
Cdd:cd03055    80 ESLIICEYLD 89

C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal 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 Omega GSTs show little or no GSH-conjugating activity towards standard GST substrates. Instead, they catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins. They contain a conserved cysteine equivalent to the first cysteine in the CXXC motif of glutaredoxins, which is a redox active residue capable of reducing GSH mixed disulfides in a monothiol mechanism. Polymorphisms of the class Omega GST genes may be associated with the development of some types of cancer and the age-at-onset of both Alzheimer's and Parkinson's diseases.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641620 108 YEKACQKMTFELFSKVPSLVTSFIRAKRKEdhPGIKEELKKEFSKLEEAMAKKRTAFFGGNSLSMIDYLIWPWFQRLEAL 187
Cdd:cd03184     1 YEKAQQKMLIERFSKVPSAFYKFLRSGEDR--KGLKEELRSALENLEEELAKRGTPFFGGNSPGMVDYMIWPWFERLEAL 78

                          90
                  ....*....|...
gi 1958641620 188 ELN-EFFLSELGT 199
Cdd:cd03184    79 KLLdGYELCLDRF 91

Glutathione S-transferase, N-terminal domain;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958641620  27 YSMRFCPFAQRTLMVLKAKGIRHEIININLKNKPEWFFEKNPFGLVPVLEnTQGHLITESVITCEYLDEAYPEKK 101
Cdd:pfam13417   2 YGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNPLGKVPVLE-DDGGILCESLAIIDYLEELYPGPP 75

glutathione dehydrogenase (ascorbate)

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641620  32 CPFAQRTLMVLKAKGIRHEIININLKNKPEWFFEKNPFGLVPVLENTQGHLITESVITcEYLDEAYPEKKLfpDDPYEKA 111
Cdd:PLN02817   73 CPFCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISPEGKVPVVKLDEKWVADSDVIT-QALEEKYPDPPL--ATPPEKA 149

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958641620 112 cqkmtfELFSKVPSLVTSFIRAKRKEDhpGIKEELKKEFSKLEEAMaKKRTAFFGGNSLSMIDYLIWPWFQRLE 185
Cdd:PLN02817  150 ------SVGSKIFSTFIGFLKSKDPGD--GTEQALLDELTSFDDYI-KENGPFINGEKISAADLSLGPKLYHLE 214

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 1958641620  23 QIRVYSMRFCPFAQRTLMVLKAKGIRHEIININLK---NKPEWFFEKNPFGLVPVLEnTQGHLITESVITCEYLDE 95
Cdd:pfam02798   2 VLTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGagpEKSPELLKLNPLGKVPALE-DGGKKLTESRAILEYIAR 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 1958641620  24 IRVYSMRFCPFAQRTLMVLKAKGIRHEIININLK---NKPEWFFEKNPFGLVPVLENtQGHLITESVITCEYLDE 95
Cdd:cd03053     2 LKLYGAAMSTCVRRVLLCLEEKGVDYELVPVDLTkgeHKSPEHLARNPFGQIPALED-GDLKLFESRAITRYLAE 75

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958641620  27 YSMRFCPFAQRTLMVLKAKGIRHEIININLKNKPEWFFEKNPFGLVPVLENTQGHLITESV 87
Cdd:cd03060     4 YSFRRCPYAMRARMALLLAGITVELREVELKNKPAEMLAASPKGTVPVLVLGNGTVIEESL 64

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958641620  35 AQRTLMVLKAKGIRHEIININLKN---KPEWFFEKNPFGLVPVLENtQGHLITESVITCEYLDEAYP 98
Cdd:cd03046    11 SFRILWLLEELGLPYELVLYDRGPgeqAPPEYLAINPLGKVPVLVD-GDLVLTESAAIILYLAEKYG 76

stringent starvation protein A; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641620  34 FAQRTLMVLKAKGIRHEIININLKNKPEWFFEKNPFGLVPVLENTQGHLItESVITCEYLDEAYPEKKLFPDDPYEKACQ 113
Cdd:PRK09481   21 YSHQVRIVLAEKGVSVEIEQVEKDNLPQDLIDLNPYQSVPTLVDRELTLY-ESRIIMEYLDERFPHPPLMPVYPVARGES 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641620 114 KMT--------FELFSKVPSLVTSFIRAKRKEdhpgIKEELkkefskLEEAMAKKRTAFFGGNSLSMIDYLIWPWFQRLE 185
Cdd:PRK09481  100 RLMmhriekdwYSLMNKIVNGSASEADAARKQ----LREEL------LAIAPVFGEKPYFMSEEFSLVDCYLAPLLWRLP 169

                  ..
gi 1958641620 186 AL 187
Cdd:PRK09481  170 VL 171

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 1958641620 116 TFELFSKVPSLVTSFIRAKRKEDHPGIKEELKKEFSKLEEAMAKKRtaFFGGNSLSMIDYLIWPWFQRLEALELNEFFLS 195
Cdd:cd00299    11 TLAPPLVRLLYLEKVPLPKDEAAVEAAREELPALLAALEQLLAGRP--YLAGDQFSLADVALAPVLARLEALGPYYDLLD 88

                  .
gi 1958641620 196 E 196
Cdd:cd00299    89 E 89

GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958641620  33 PFAQRTLMVL--KAKGIRHEIININLKNKPEWFFEKNPFGLVPVLENTQGHLITESVITCEYLD 94
Cdd:cd03049    10 PYVRKVRVAAheTGLGDDVELVLVNPWSDDESLLAVNPLGKIPALVLDDGEALFDSRVICEYLD 73

glutathione transferase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641620  31 FCPFAQRTLMVLKAKGIRHEIININLKNK----PEWFfEKNPFGLVPVLENTQGHLiTESVITCEYLDEAYPE---KKLF 103
Cdd:PRK15113   15 FSPYVMSAFVALQEKGLPFELKTVDLDAGehlqPTYQ-GYSLTRRVPTLQHDDFEL-SESSAIAEYLEERFAPpawERIY 92

                  ....*...
gi 1958641620 104 PDDPYEKA 111
Cdd:PRK15113   93 PADLQARA 100

putative glutathione S-transferase; Provisional

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958641620  33 PFAQRTLMVLKAKGIRHEIININLKNKPEWFFEKNPFGLVPVLENTQGHLITESVITCEYLDEAYPEKKLFPDDP 107
Cdd:PRK10357   10 PFVRKISILLLEKGITFEFVNELPYNADNGVAQYNPLGKVPALVTEEGECWFDSPIIAEYIELLNVAPAMLPRDP 84

GST_N family, Chloride Intracellular Channel (CLIC) subfamily; composed of CLIC1-5, p64, parchorin and similar proteins. They are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division and apoptosis. They can exist in both water-soluble and membrane-bound states, and are found in various vesicles and membranes. Biochemical studies of the C. elegans homolog, EXC-4, show that the membrane localization domain is present in the N-terminal part of the protein. The structure of soluble human CLIC1 reveals that it is monomeric and it adopts a fold similar to GSTs, containing an N-terminal domain with a TRX fold and a C-terminal alpha helical domain. Upon oxidation, the N-terminal domain of CLIC1 undergoes a structural change to form a non-covalent dimer stabilized by the formation of an intramolecular disulfide bond between two cysteines that are far apart in the reduced form. The CLIC1 dimer bears no similarity to GST dimers. The redox-controlled structural rearrangement exposes a large hydrophobic surface, which is masked by dimerization in vitro. In vivo, this surface may represent the docking interface of CLIC1 in its membrane-bound state. The two cysteines in CLIC1 that form the disulfide bond in oxidizing conditions are essential for dimerization and chloride channel activity, however, in other subfamily members, the second cysteine is not conserved.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958641620  32 CPFAQRTLMVLKAKGIRHEIININLKNKPEwFFEKNPFGLVP 73
Cdd:cd03061    22 CPFCQRLFMVLWLKGVVFNVTTVDMKRKPE-DLKDLAPGTQP 62

glutathione S-transferase

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641620  22 GQIRVYsmrfCPfaQRTLMVLKAKGIRHEIININL----KNKPEWFFeKNPFGLVPVLEN 77
Cdd:PLN02473    7 GQIKAA----NP--QRVLLCFLEKGIEFEVIHVDLdkleQKKPEHLL-RQPFGQVPAIED 59

Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, as well as E. coli GRX1 and GRX3, which are members of this family. E. coli GRX2, however, is a 24-kDa protein that belongs to the GSH S-transferase (GST) family.

                          10        20        30
                  ....*....|....*....|....*....|..
gi 1958641620  24 IRVYSMRFCPFAQRTLMVLKAKGIRHEIININ 55
Cdd:cd02066     2 VVVFSKSTCPYCKRAKRLLESLGIEFEEIDIL 33

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 1958641620  26 VYSMRFCPFAQRTLMVLKAKGIRHEIINI--NLKNKPEWFFEKNPFGLVPVLENTQGHLITESVITCEYL 93
Cdd:cd03044     3 LYTYPGNPRSLKILAAAKYNGLDVEIVDFqpGKENKTPEFLKKFPLGKVPAFEGADGFCLFESNAIAYYV 72