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Conserved domains on  [gi|84375507|gb|EAP92410|]
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glutaredoxin 2 [Vibrio splendidus 12B01]

Protein Classification

glutaredoxin 2( domain architecture ID 11484691)

glutaredoxin 2 is an aytpical glutaredoxin that catalyzes the glutathione dependent protein disulfide reduction of certain substrates, primarily proteins involved in cellular redox regulation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10387 PRK10387
glutaredoxin 2; Provisional
 1-209 8.01e-95

glutaredoxin 2; Provisional


:

Pssm-ID: 236679 [Multi-domain]  Cd Length: 210  Bit Score: 275.22  E-value: 8.01e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375507    1 MKLYIYDHCPFCARVAYIAQSLGLNIELVSVDYDDAQTLIDLIGKKMVPVLQRNDGSIMAESLDIIVYFMDLKSSDEQR- 79
Cdd:PRK10387   1 MKLYIYDHCPFCVKARMIFGLKNIPVELIVLANDDEATPIRMIGQKQVPILQKDDGSYMPESLDIVHYIDELDGKPLLTg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375507   80 EPSEQAALFQSRAFPLTQQIGRPRWWNLDLAEYRSAGAKEAWRASKETEGFNFEELLEKTPQYVQLINPLLKDAELLLDL 159
Cdd:PRK10387  81 KRSPAIEEWLRKVFGYLNKLLYPRFAKADLPEFATPSARQYFIDKKEASIGDFDALLAHTPGLIKEINADLRALDPLIVK 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 84375507  160 ENGESSLPLVDQALYFSMLRGFCVEPSITWPPTLERWLEKQSQTLGIKLL 209
Cdd:PRK10387 161 PNAVNGELSTDDIHLFPILRNLTLVKGIEWPPRVADYRDNMSKKTQVPLL 210
 
Name Accession Description Interval E-value
PRK10387 PRK10387
glutaredoxin 2; Provisional
 1-209 8.01e-95

glutaredoxin 2; Provisional


Pssm-ID: 236679 [Multi-domain]  Cd Length: 210  Bit Score: 275.22  E-value: 8.01e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375507    1 MKLYIYDHCPFCARVAYIAQSLGLNIELVSVDYDDAQTLIDLIGKKMVPVLQRNDGSIMAESLDIIVYFMDLKSSDEQR- 79
Cdd:PRK10387   1 MKLYIYDHCPFCVKARMIFGLKNIPVELIVLANDDEATPIRMIGQKQVPILQKDDGSYMPESLDIVHYIDELDGKPLLTg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375507   80 EPSEQAALFQSRAFPLTQQIGRPRWWNLDLAEYRSAGAKEAWRASKETEGFNFEELLEKTPQYVQLINPLLKDAELLLDL 159
Cdd:PRK10387  81 KRSPAIEEWLRKVFGYLNKLLYPRFAKADLPEFATPSARQYFIDKKEASIGDFDALLAHTPGLIKEINADLRALDPLIVK 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 84375507  160 ENGESSLPLVDQALYFSMLRGFCVEPSITWPPTLERWLEKQSQTLGIKLL 209
Cdd:PRK10387 161 PNAVNGELSTDDIHLFPILRNLTLVKGIEWPPRVADYRDNMSKKTQVPLL 210
GrxB COG2999
Glutaredoxin 2 [Posttranslational modification, protein turnover, chaperones];
1-209 5.19e-63

Glutaredoxin 2 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442237 [Multi-domain]  Cd Length: 215  Bit Score: 194.68  E-value: 5.19e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375507   1 MKLYIYDHCPFCARVAYIAQSLGLNIELVSVDYDDAQTLIDLIGKKMVPVLQRNDGSIMAESLDIIVYFMDLKSSDE-QR 79
Cdd:COG2999   1 MKLYIYDHCPFCVRARMIFGLKNIPVELIVLLNDDEETPIRMIGKKMVPILEKDDGSYMPESLDIVHYIDELDGKPIlTG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375507  80 EPSEQAALFQSRAFPLTQQIGRPRWWNLDLAEYRSAGAKEAWRASKETEGFNFEELLEKTPQYVQLINPLLKDAELLLDL 159
Cdd:COG2999  81 PVRPEIAAWLKKVSSYVNRLLYPRWAKAPLPEFATPSARAYFINKKEASIGDFEELLANTPELIAELNQDLEELEPLIKS 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 84375507 160 ENGESSLPLVDQALYFSMLRGFCVEPSITWPPTLERWLEKQSQTLGIKLL 209
Cdd:COG2999 161 PSAVNGELSLDDIILFPLLRSLTIVKGIQFPPKVRAYRDRMSKKTGVPLL 210
GRXB TIGR02182
Glutaredoxin, GrxB family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 2-209 3.19e-61

Glutaredoxin, GrxB family; Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This model includes the highly abundant E. coli GrxB (Grx2) glutaredoxin which is notably longer than either GrxA or GrxC. Unlike the other two E. coli glutaredoxins, GrxB appears to be unable to reduce ribonucleotide reductase, and may have more to do with resistance to redox stress. [Energy metabolism, Electron transport]


Pssm-ID: 274018 [Multi-domain]  Cd Length: 209  Bit Score: 189.98  E-value: 3.19e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375507     2 KLYIYDHCPFCARVAYIAQSLGLNIELVSVDYDDAQTLIDLIGKKMVPVLQRNDGSIMAESLDIIVYFMDLKSSD-EQRE 80
Cdd:TIGR02182   1 KLYIYDHCPFCVRARMIFGLKNIPVEKHVLLNDDEETPIRMIGAKQVPILQKDDGRAMPESLDIVAYFDKLDGEPlLTGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375507    81 PSEQAALFQSRAFPLTQQIGRPRWWNLDLAEYRSAGAKEAWRASKETEGFNFEELLEKTPQYVQLINPLLKDAELLLDLE 160
Cdd:TIGR02182  81 VSPEIEAWLRKVTGYANKLLLPRFAKSDLPEFATQSARKYFTDKKEASAGNFSALLNHTPGLLEEINADLEELDKLIDGP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 84375507   161 NGESSLPLVDQALYFSMLRGFCVEPSITWPPTLERWLEKQSQTLGIKLL 209
Cdd:TIGR02182 161 NAVNGELSEDDILVFPLLRNLTLVAGINWPSRVADYLDNMSKKSKVPLL 209
Glutaredoxin2_C pfam04399
Glutaredoxin 2, C terminal domain; Glutaredoxins are a multifunctional family of ...
 89-209 2.59e-39

Glutaredoxin 2, C terminal domain; Glutaredoxins are a multifunctional family of glutathione-dependent disulphide oxidoreductases. Unlike other glutaredoxins, glutaredoxin 2 (Grx2) cannot reduce ribonucleotide reductase. Grx2 has significantly higher catalytic activity in the reduction of mixed disulphides with glutathione (GSH) compared with other glutaredoxins. The active site residues (Cys9-Pro10-Tyr11-Cys12, in Escherichia coli Grx2, Swiss:P39811), which are found at the interface between the N- and C-terminal domains are identical to other glutaredoxins, but there is no other similarity between glutaredoxin 2 and other glutaredoxins. Grx2 is structurally similar to glutathione-S-transferases (GST), but there is no obvious sequence similarity. The inter-domain contacts are mainly hydrophobic, suggesting that the two domains are unlikely to be stable on their own. Both domains are needed for correct folding and activity of Grx2. It is thought that the primary function of Grx2 is to catalyze reversible glutathionylation of proteins with GSH in cellular redox regulation including the response to oxidative stress.


Pssm-ID: 461291  Cd Length: 130  Bit Score: 131.55  E-value: 2.59e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375507    89 QSRAFPLTQQIGRPRWWNLDLAEYRSAGAKEAWRASKETEGFNFEELLEKTPQYVQLINPLLKDAELLLDLENGESSLPL 168
Cdd:pfam04399   6 LKRVFPYLNRLLLPRFAAAPLPEFATQSAREYFRNKKEASIGSFEELLAKSPELIAQLNADLEALEPLILSSHAVNGQLS 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 84375507   169 VDQALYFSMLRGFCVEPSITWPPTLERWLEKQSQTLGIKLL 209
Cdd:pfam04399  86 YDDILLFPILRSLTIVKGLQWPPEVRAYLDRMSAATGVPLL 126
GST_N_GRX2 cd03037
GST_N family, Glutaredoxin 2 (GRX2) subfamily; composed of bacterial proteins similar to E. ...
 1-69 1.46e-29

GST_N family, Glutaredoxin 2 (GRX2) subfamily; composed of bacterial proteins similar to E. coli GRX2, an atypical GRX with a molecular mass of about 24kD, compared with other GRXs which are 9-12kD in size. GRX2 adopts a GST fold containing an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. It contains a redox active CXXC motif located in the N-terminal domain but is not able to reduce ribonucleotide reductase like other GRXs. However, it catalyzes GSH-dependent protein disulfide reduction of other substrates efficiently. GRX2 is thought to function primarily in catalyzing the reversible glutathionylation of proteins in cellular redox regulation including stress responses.


Pssm-ID: 239335 [Multi-domain]  Cd Length: 71  Bit Score: 104.78  E-value: 1.46e-29
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 84375507   1 MKLYIYDHCPFCARVAYIAQSLGLNIELVSVDYDDAQTLIDLIGKKMVPVLQRNDGSIMAESLDIIVYF 69
Cdd:cd03037   1 MKLYIYEHCPFCVKARMIAGLKNIPVEQIILQNDDEATPIRMIGAKQVPILEKDDGSFMAESLDIVAFI 69
 
Name Accession Description Interval E-value
PRK10387 PRK10387
glutaredoxin 2; Provisional
 1-209 8.01e-95

glutaredoxin 2; Provisional


Pssm-ID: 236679 [Multi-domain]  Cd Length: 210  Bit Score: 275.22  E-value: 8.01e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375507    1 MKLYIYDHCPFCARVAYIAQSLGLNIELVSVDYDDAQTLIDLIGKKMVPVLQRNDGSIMAESLDIIVYFMDLKSSDEQR- 79
Cdd:PRK10387   1 MKLYIYDHCPFCVKARMIFGLKNIPVELIVLANDDEATPIRMIGQKQVPILQKDDGSYMPESLDIVHYIDELDGKPLLTg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375507   80 EPSEQAALFQSRAFPLTQQIGRPRWWNLDLAEYRSAGAKEAWRASKETEGFNFEELLEKTPQYVQLINPLLKDAELLLDL 159
Cdd:PRK10387  81 KRSPAIEEWLRKVFGYLNKLLYPRFAKADLPEFATPSARQYFIDKKEASIGDFDALLAHTPGLIKEINADLRALDPLIVK 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 84375507  160 ENGESSLPLVDQALYFSMLRGFCVEPSITWPPTLERWLEKQSQTLGIKLL 209
Cdd:PRK10387 161 PNAVNGELSTDDIHLFPILRNLTLVKGIEWPPRVADYRDNMSKKTQVPLL 210
GrxB COG2999
Glutaredoxin 2 [Posttranslational modification, protein turnover, chaperones];
1-209 5.19e-63

Glutaredoxin 2 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442237 [Multi-domain]  Cd Length: 215  Bit Score: 194.68  E-value: 5.19e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375507   1 MKLYIYDHCPFCARVAYIAQSLGLNIELVSVDYDDAQTLIDLIGKKMVPVLQRNDGSIMAESLDIIVYFMDLKSSDE-QR 79
Cdd:COG2999   1 MKLYIYDHCPFCVRARMIFGLKNIPVELIVLLNDDEETPIRMIGKKMVPILEKDDGSYMPESLDIVHYIDELDGKPIlTG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375507  80 EPSEQAALFQSRAFPLTQQIGRPRWWNLDLAEYRSAGAKEAWRASKETEGFNFEELLEKTPQYVQLINPLLKDAELLLDL 159
Cdd:COG2999  81 PVRPEIAAWLKKVSSYVNRLLYPRWAKAPLPEFATPSARAYFINKKEASIGDFEELLANTPELIAELNQDLEELEPLIKS 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 84375507 160 ENGESSLPLVDQALYFSMLRGFCVEPSITWPPTLERWLEKQSQTLGIKLL 209
Cdd:COG2999 161 PSAVNGELSLDDIILFPLLRSLTIVKGIQFPPKVRAYRDRMSKKTGVPLL 210
GRXB TIGR02182
Glutaredoxin, GrxB family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 2-209 3.19e-61

Glutaredoxin, GrxB family; Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This model includes the highly abundant E. coli GrxB (Grx2) glutaredoxin which is notably longer than either GrxA or GrxC. Unlike the other two E. coli glutaredoxins, GrxB appears to be unable to reduce ribonucleotide reductase, and may have more to do with resistance to redox stress. [Energy metabolism, Electron transport]


Pssm-ID: 274018 [Multi-domain]  Cd Length: 209  Bit Score: 189.98  E-value: 3.19e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375507     2 KLYIYDHCPFCARVAYIAQSLGLNIELVSVDYDDAQTLIDLIGKKMVPVLQRNDGSIMAESLDIIVYFMDLKSSD-EQRE 80
Cdd:TIGR02182   1 KLYIYDHCPFCVRARMIFGLKNIPVEKHVLLNDDEETPIRMIGAKQVPILQKDDGRAMPESLDIVAYFDKLDGEPlLTGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375507    81 PSEQAALFQSRAFPLTQQIGRPRWWNLDLAEYRSAGAKEAWRASKETEGFNFEELLEKTPQYVQLINPLLKDAELLLDLE 160
Cdd:TIGR02182  81 VSPEIEAWLRKVTGYANKLLLPRFAKSDLPEFATQSARKYFTDKKEASAGNFSALLNHTPGLLEEINADLEELDKLIDGP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 84375507   161 NGESSLPLVDQALYFSMLRGFCVEPSITWPPTLERWLEKQSQTLGIKLL 209
Cdd:TIGR02182 161 NAVNGELSEDDILVFPLLRNLTLVAGINWPSRVADYLDNMSKKSKVPLL 209
Glutaredoxin2_C pfam04399
Glutaredoxin 2, C terminal domain; Glutaredoxins are a multifunctional family of ...
 89-209 2.59e-39

Glutaredoxin 2, C terminal domain; Glutaredoxins are a multifunctional family of glutathione-dependent disulphide oxidoreductases. Unlike other glutaredoxins, glutaredoxin 2 (Grx2) cannot reduce ribonucleotide reductase. Grx2 has significantly higher catalytic activity in the reduction of mixed disulphides with glutathione (GSH) compared with other glutaredoxins. The active site residues (Cys9-Pro10-Tyr11-Cys12, in Escherichia coli Grx2, Swiss:P39811), which are found at the interface between the N- and C-terminal domains are identical to other glutaredoxins, but there is no other similarity between glutaredoxin 2 and other glutaredoxins. Grx2 is structurally similar to glutathione-S-transferases (GST), but there is no obvious sequence similarity. The inter-domain contacts are mainly hydrophobic, suggesting that the two domains are unlikely to be stable on their own. Both domains are needed for correct folding and activity of Grx2. It is thought that the primary function of Grx2 is to catalyze reversible glutathionylation of proteins with GSH in cellular redox regulation including the response to oxidative stress.


Pssm-ID: 461291  Cd Length: 130  Bit Score: 131.55  E-value: 2.59e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375507    89 QSRAFPLTQQIGRPRWWNLDLAEYRSAGAKEAWRASKETEGFNFEELLEKTPQYVQLINPLLKDAELLLDLENGESSLPL 168
Cdd:pfam04399   6 LKRVFPYLNRLLLPRFAAAPLPEFATQSAREYFRNKKEASIGSFEELLAKSPELIAQLNADLEALEPLILSSHAVNGQLS 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 84375507   169 VDQALYFSMLRGFCVEPSITWPPTLERWLEKQSQTLGIKLL 209
Cdd:pfam04399  86 YDDILLFPILRSLTIVKGLQWPPEVRAYLDRMSAATGVPLL 126
GST_N_GRX2 cd03037
GST_N family, Glutaredoxin 2 (GRX2) subfamily; composed of bacterial proteins similar to E. ...
 1-69 1.46e-29

GST_N family, Glutaredoxin 2 (GRX2) subfamily; composed of bacterial proteins similar to E. coli GRX2, an atypical GRX with a molecular mass of about 24kD, compared with other GRXs which are 9-12kD in size. GRX2 adopts a GST fold containing an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. It contains a redox active CXXC motif located in the N-terminal domain but is not able to reduce ribonucleotide reductase like other GRXs. However, it catalyzes GSH-dependent protein disulfide reduction of other substrates efficiently. GRX2 is thought to function primarily in catalyzing the reversible glutathionylation of proteins in cellular redox regulation including stress responses.


Pssm-ID: 239335 [Multi-domain]  Cd Length: 71  Bit Score: 104.78  E-value: 1.46e-29
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 84375507   1 MKLYIYDHCPFCARVAYIAQSLGLNIELVSVDYDDAQTLIDLIGKKMVPVLQRNDGSIMAESLDIIVYF 69
Cdd:cd03037   1 MKLYIYEHCPFCVKARMIAGLKNIPVEQIILQNDDEATPIRMIGAKQVPILEKDDGSFMAESLDIVAFI 69
GST_C_GRX2 cd03199
C-terminal, alpha helical domain of Glutaredoxin 2; Glutathione S-transferase (GST) C-terminal ...
 101-209 2.41e-14

C-terminal, alpha helical domain of Glutaredoxin 2; Glutathione S-transferase (GST) C-terminal domain family, Glutaredoxin 2 (GRX2) subfamily; composed of Escherichia coli GRX2 and similar proteins. Escherichia coli GRX2 is an atypical GRX with a molecular mass of about 24kD (most GRXs range from 9-12kD). It adopts a GST fold containing an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. It contains a redox active CXXC motif located in the N-terminal domain, but is not able to reduce ribonucleotide reductase like other GRXs. However, it catalyzes GSH-dependent protein disulfide reduction of other substrates efficiently. GRX2 is thought to function primarily in catalyzing the reversible glutathionylation of proteins in cellular redox regulation including stress responses.


Pssm-ID: 198308  Cd Length: 128  Bit Score: 66.80  E-value: 2.41e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375507 101 RPRWWNLDLAEYRSAGAKEAWRASKETEGFNFEELLEKTPQYVQLINPLLKDAE-LLLDLENGESSLPLvDQALYFSMLR 179
Cdd:cd03199  20 LPRFAKADLPEFATPSARAYFIRKKEASIGSFEELLAKTPELIAELNADLEALDpLILSSDAVNGELSY-DDIILFPLLR 98

                        90       100       110
                ....*....|....*....|....*....|
gi 84375507 180 GFCVEPSITWPPTLERWLEKQSQTLGIKLL 209
Cdd:cd03199  99 NLTIVKGLEFPPKVRAYIDNMSALSDVPLY 128
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 1-68 8.23e-10

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: 52.96  E-value: 8.23e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375507   1 MKLYIYDHCPFCARVAYIAQSLGLNIELVSVDYDDAQT--LIDLIGKKMVPVLQRnDGSIMAESLDIIVY 68
Cdd:cd00570   1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQeeFLALNPLGKVPVLED-GGLVLTESLAILEY 69
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
3-69 2.86e-09

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 51.84  E-value: 2.86e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 84375507     3 LYIYDHCPFCARVAYIAQSLGLNIELVSVDYDD-AQTLIDLIGKKMVPVLQRnDGSIMAESLDIIVYF 69
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPPGDhPPELLAKNPLGKVPVLED-DGGILCESLAIIDYL 67
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 8-69 7.67e-08

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 47.63  E-value: 7.67e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 84375507     8 HCPFCARVAYIAQSLGL--NIELVSVDYDDA-QTLIDLIGKKMVPVLQRNDGSIMAESLDIIVYF 69
Cdd:pfam13409   1 FSPFSHRVRLALEEKGLpyEIELVDLDPKDKpPELLALNPLGTVPVLVLPDGTVLTDSLVILEYL 65
GST_N_3 cd03049
GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with ...
 1-71 3.63e-07

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.


Pssm-ID: 239347 [Multi-domain]  Cd Length: 73  Bit Score: 46.10  E-value: 3.63e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 84375507   1 MKLYIYDHCPF--CARVAYIAQSLGLNIELVSVD-YDDAQTLIDL--IGKkmVPVLQRNDGSIMAESlDIIVYFMD 71
Cdd:cd03049   1 MKLLYSPTSPYvrKVRVAAHETGLGDDVELVLVNpWSDDESLLAVnpLGK--IPALVLDDGEALFDS-RVICEYLD 73
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
1-68 2.58e-06

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 46.43  E-value: 2.58e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 84375507   1 MKLYIYDHCPFCARVAYIAQSLGLNIELVSVDYDDAQT----LIDLIGKKMVPVLQrNDGSIMAESLDIIVY 68
Cdd:COG0625   2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQkspeFLALNPLGKVPVLV-DDGLVLTESLAILEY 72
GST_N_Beta cd03057
GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 1-72 7.34e-05

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: 39.83  E-value: 7.34e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84375507   1 MKLYIYDHCpfCARVAYIA-QSLGLNIELVSVDYDDAQT----LIDLIGKKMVPVLQRNDGSIMAESLDIIVYFMDL 72
Cdd:cd03057   1 MKLYYSPGA--CSLAPHIAlEELGLPFELVRVDLRTKTQkgadYLAINPKGQVPALVLDDGEVLTESAAILQYLADL 75
GST_N_Omega_like cd03060
GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to ...
 3-66 9.29e-05

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.


Pssm-ID: 239358 [Multi-domain]  Cd Length: 71  Bit Score: 39.26  E-value: 9.29e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 84375507   3 LYIYDHCPFCARVAYIAQSLGLNIELVSVDY-DDAQTLIDLIGKKMVPVLQRNDGSIMAESLDII 66
Cdd:cd03060   3 LYSFRRCPYAMRARMALLLAGITVELREVELkNKPAEMLAASPKGTVPVLVLGNGTVIEESLDIM 67
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
2-55 1.97e-04

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 38.64  E-value: 1.97e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 84375507   2 KLYIYDHCPFCARVAYIAQSLGLNIELVSVDYDDA--QTLIDLIGKKMVPVLQRND 55
Cdd:COG0695   3 TLYTTPGCPYCARAKRLLDEKGIPYEEIDVDEDPEarEELRERSGRRTVPVIFIGG 58
Glutaredoxin pfam00462
Glutaredoxin;
3-51 5.03e-04

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 37.10  E-value: 5.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 84375507     3 LYIYDHCPFCARVAYIAQSLGLNIELVSVDYDDA--QTLIDLIGKKMVPVL 51
Cdd:pfam00462   3 LYTKPTCPFCKRAKRLLKSLGVDFEEIDVDEDPEirEELKELSGWPTVPQV 53
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
 1-69 2.06e-03

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: 35.74  E-value: 2.06e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 84375507   1 MKLYIYDHCPFCARVA-YIAQSlGLNIELVSVDYDDAQTLIDLIGKK----MVPVLQRNDGSIMAESLDIIVYF 69
Cdd:cd03051   1 MKLYDSPTAPNPRRVRiFLAEK-GIDVPLVTVDLAAGEQRSPEFLAKnpagTVPVLELDDGTVITESVAICRYL 73
GST_N_2GST_N cd03041
GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed ...
 1-68 5.98e-03

GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed of uncharacterized proteins. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains.


Pssm-ID: 239339 [Multi-domain]  Cd Length: 77  Bit Score: 34.63  E-value: 5.98e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 84375507   1 MKLYIYDHCPFCARVAYIAQSLGLNIELVSVDYDDA--QTLIDLIGKKMVPVL-QRNDGSIMAESLDIIVY 68
Cdd:cd03041   2 LELYEFEGSPFCRLVREVLTELELDVILYPCPKGSPkrDKFLEKGGKVQVPYLvDPNTGVQMFESADIVKY 72
 
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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