C-terminal, alpha helical domain of Stringent starvation protein A; Glutathione S-transferase (GST) C-terminal domain 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 thioredoxin-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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491996086  92 PILRAQCRLNIHRIQNDWFSLIDFIERDPTTAEAQRALNQLREEVLALGPVFSDSDYFLSEDFSLVDCYVAPLLWRMNTL 171
Cdd:cd03186    1 PVSRARSRLMMHRIEQDWYPLLDTILNGRDEKEAEKARKELRESLTALAPVFAASPYFLSEEFSLVDCYLAPLLWRLPAL 80

                         90       100
                 ....*....|....*....|....*....
gi 491996086 172 GVEFNGaGSKAVKAYMNRVFKRDSFVQSI 200
Cdd:cd03186   81 GIELPK-QAKAIKDYMERVFARDSFQASL 108

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 491996086   11 TLFSTKTDIYSHQVRIVLAEKGVAYEIENILPGTI---SEDLIEVNPRGTVPVLVDRDLILSNARIIMEYLDE 80
Cdd:pfam02798   4 TLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGAGpekSPELLKLNPLGKVPALEDGGKKLTESRAILEYIAR 76

C-terminal, alpha helical domain of Stringent starvation protein A; Glutathione S-transferase (GST) C-terminal domain 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 thioredoxin-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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491996086  92 PILRAQCRLNIHRIQNDWFSLIDFIERDPTTAEAQRALNQLREEVLALGPVFSDSDYFLSEDFSLVDCYVAPLLWRMNTL 171
Cdd:cd03186    1 PVSRARSRLMMHRIEQDWYPLLDTILNGRDEKEAEKARKELRESLTALAPVFAASPYFLSEEFSLVDCYLAPLLWRLPAL 80

                         90       100
                 ....*....|....*....|....*....
gi 491996086 172 GVEFNGaGSKAVKAYMNRVFKRDSFVQSI 200
Cdd:cd03186   81 GIELPK-QAKAIKDYMERVFARDSFQASL 108

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 491996086  11 TLFSTKTDIYSHQVRIVLAEKGVAYEIENILPGTISEDLIEVNPRGTVPVLVDRDLILSNARIIMEYLDERF 82
Cdd:cd03059    2 TLYSGPDDVYSHRVRIVLAEKGVSVEIIDVDPDNPPEDLAELNPYGTVPTLVDRDLVLYESRIIMEYLDERF 73

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 491996086   11 TLFSTKTDIYSHQVRIVLAEKGVAYEIENILPGTI---SEDLIEVNPRGTVPVLVDRDLILSNARIIMEYLDE 80
Cdd:pfam02798   4 TLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGAGpekSPELLKLNPLGKVPALEDGGKKLTESRAILEYIAR 76

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491996086   20 YSHQVRIVLAEKGVAYEIENI--LPGTISEDLIEVNPRGTVPVLVDRD-LILSNARIIMEYLDER 81
Cdd:pfam13409   4 FSHRVRLALEEKGLPYEIELVdlDPKDKPPELLALNPLGTVPVLVLPDgTVLTDSLVILEYLEEL 68

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491996086  100 LNIHRIQNDWFSLIDFIERDPTTAEAqrALNQLREEVLALGPVFSDSDYFLSEDFSLVDCYVAPLLWRMNTLGVEFNGAG 179
Cdd:pfam00043   1 LMDLRMQIALLPYVPPEEKKEPEVDE--ALEKVARVLSALEEVLKGQTYLVGDKLTLADIALAPALLWLYELDPACLREK 78

                          90
                  ....*....|....*
gi 491996086  180 SKAVKAYMNRVFKRD 194
Cdd:pfam00043  79 FPNLKAWFERVAARP 93

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491996086  20 YSHQVRIVLAEKGVAYE-IENILpGTISEDLIEVNP-RGTVPVLVDRDLILSNARIIMEYLDERF 82
Cdd:cd03058   11 FVLRVRIALALKGVPYEyVEEDL-GNKSELLLASNPvHKKIPVLLHNGKPICESLIIVEYIDEAW 74

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491996086  24 VRIVLAEKGVAYEIENILPGTI---SEDLIEVNPRGTVPVLV-DRDLILSNARIIMEYLDERFP 83
Cdd:cd03057   14 PHIALEELGLPFELVRVDLRTKtqkGADYLAINPKGQVPALVlDDGEVLTESAAILQYLADLHP 77

glutathione transferase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491996086  20 YSHQVRIVLAEKGVAYEIENIlpgtiseDL----------IEVNPRGTVPVLVDRDLILSNARIIMEYLDERFPHPPLMP 89
Cdd:PRK15113  18 YVMSAFVALQEKGLPFELKTV-------DLdagehlqptyQGYSLTRRVPTLQHDDFELSESSAIAEYLEERFAPPAWER 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491996086  90 VYPILRaQCRLNIHRIQNdWF-SliDFI----ERD-----------PTTAEAQRALNQLreeVLALGPVFSDSDYFLSED 153
Cdd:PRK15113  91 IYPADL-QARARARQIQA-WLrS--DLMplreERPtdvvfagakkaPLSEAGKAAAEKL---FAVAERLLAPGQPNLFGE 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 491996086 154 FSLVDCYVAPLLWRMNTLGVEFngagSKAVKAYMNRVFKRDSfVQ 198
Cdd:PRK15113 164 WCIADTDLALMLNRLVLHGDEV----PERLADYATFQWQRAS-VQ 203

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 491996086  21 SHQVRIVLAEKGVAYEIENIL---PGTISEDLIEVNPRGTVPVLVDRDLIL--SNAriIMEYLDERFP 83
Cdd:cd03046   11 SFRILWLLEELGLPYELVLYDrgpGEQAPPEYLAINPLGKVPVLVDGDLVLteSAA--IILYLAEKYG 76

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 491996086  71 ARIIMEYLDERFPHPplmpvypilraqcrLNIHRIQNDWFSLIDFIERDPTTAEAQRALNQLrEEVLAlgpvfsDSDYFL 150
Cdd:cd00299    1 VRALEDWADATLAPP--------------LVRLLYLEKVPLPKDEAAVEAAREELPALLAAL-EQLLA------GRPYLA 59

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 491996086 151 SEDFSLVDCYVAPLLWRMNTLG-VEFNGAGSKAVKAYMNRV 190
Cdd:cd00299   60 GDQFSLADVALAPVLARLEALGpYYDLLDEYPRLKAWYDRL 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491996086  20 YSHQVRIVLAEKGVAYEIENILPGTISEDLIEVNPRGTVPVL-VDRDLILSNARIIMEYLD 79
Cdd:cd03055   29 YAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPQGKVPALeIDEGKVVYESLIICEYLD 89

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491996086  21 SHQVRIVLAEKGVAYEIE--NILPG-TISEDLIEVNPRGTVPVLVDRDLIL--SNAriIMEYL 78
Cdd:cd03056   12 CYKVRLLLALLGIPYEWVevDILKGeTRTPEFLALNPNGEVPVLELDGRVLaeSNA--ILVYL 72

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491996086  18 DIYSHQ------VRIVLAEKGVAYEIE--NILPGTI-SEDLIEVNPRGTVPVLVDR---DLIL--SNAriIMEYLDERFP 83
Cdd:cd03048    3 TLYTHGtpngfkVSIMLEELGLPYEIHpvDISKGEQkKPEFLKINPNGRIPAIVDHngtPLTVfeSGA--ILLYLAEKYD 80

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

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491996086  21 SHQVRIVLAEKGVAYEIENI-LPgtISED----LIEVNPRGTVPVLVDRDLILSNARIIMEYLD 79
Cdd:cd03052   12 SQKVRLVIAEKGLRCEEYDVsLP--LSEHnepwFMRLNPTGEVPVLIHGDNIICDPTQIIDYLE 73

glutathione S-transferase

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491996086  21 SHQVRIVLAEKGVAYEienilpgTISEDLIE----------VNPRGTVPVLVDRDLILSNARIIMEYLDERF 82
Cdd:PLN02395  13 PKRALVTLIEKGVEFE-------TVPVDLMKgehkqpeylaLQPFGVVPVIVDGDYKIFESRAIMRYYAEKY 77

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491996086  24 VRIVLAEKGVAY--------EIENILPGTISedlievNPRGTVPVLVDRD-LILSNARIIMEYLDERFP 83
Cdd:cd03038   22 TRLALNHKGLEYktvpvefpDIPPILGELTS------GGFYTVPVIVDGSgEVIGDSFAIAEYLEEAYP 84

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 491996086  11 TLFSTKTDIYSHQVRIVLAEKGVAYEIENIL--PGTISEdLIEVNPRGTVPVLVDRDLILSN 70
Cdd:cd02976    3 TVYTKPDCPYCKATKRFLDERGIPFEEVDVDedPEALEE-LKKLNGYRSVPVVVIGDEHLSG 63

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 491996086  10 PTLFSTKTDIYSHQVRIVLAEKGVAYEIENILPGTISEDLIEVNPRGTVPVLVdrdliLSNARIIMEYLD 79
Cdd:cd03060    1 PILYSFRRCPYAMRARMALLLAGITVELREVELKNKPAEMLAASPKGTVPVLV-----LGNGTVIEESLD 65