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Conserved domains on  [gi|1308010330|gb|AUE22578|]
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thioredoxin [Aeromonas phage Ah1]

Protein Classification

glutaredoxin( domain architecture ID 10114533)

glutaredoxin is a glutathione dependent reductase that catalyzes the reduction of disulfides in target proteins

CATH:  3.40.30.10
Gene Ontology:  GO:0015038|GO:0043295
PubMed:  14713336|15706083|10049365|15558583|9099998
SCOP:  3000031

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 14-84 4.81e-08

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.


:

Pssm-ID: 239017 [Multi-domain]  Cd Length: 72  Bit Score: 45.54  E-value: 4.81e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1308010330 14 CKPCLNAKRLLDTRMVDYVFLPIAkiskteEHKTNKADLTRRAKEHGVvvtsmPQVFADGEYIGGFEELKA 84
Cdd:cd02066   10 CPYCKRAKRLLESLGIEFEEIDIL------EDGELREELKELSGWPTV-----PQIFINGEFIGGYDDLKA 69
 
Name Accession Description Interval E-value
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 14-84 4.81e-08

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.


Pssm-ID: 239017 [Multi-domain]  Cd Length: 72  Bit Score: 45.54  E-value: 4.81e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1308010330 14 CKPCLNAKRLLDTRMVDYVFLPIAkiskteEHKTNKADLTRRAKEHGVvvtsmPQVFADGEYIGGFEELKA 84
Cdd:cd02066   10 CPYCKRAKRLLESLGIEFEEIDIL------EDGELREELKELSGWPTV-----PQIFINGEFIGGYDDLKA 69
grxA PRK11200
glutaredoxin 1; Provisional
 14-89 9.60e-08

glutaredoxin 1; Provisional


Pssm-ID: 183036 [Multi-domain]  Cd Length: 85  Bit Score: 45.02  E-value: 9.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308010330 14 CKPCLNAKRLLDT-----RMVDYVFLPI--AKISKteehktnkADLTRRAkehGVVVTSMPQVFADGEYIGGFEELKAWV 86
Cdd:PRK11200  11 CPYCVRAKELAEKlseerDDFDYRYVDIhaEGISK--------ADLEKTV---GKPVETVPQIFVDQKHIGGCTDFEAYV 79


                 ...
gi 1308010330 87 NEN 89
Cdd:PRK11200  80 KEN 82
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
1-87 3.36e-07

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 43.26  E-value: 3.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308010330  1 MLEVYGFDplelECKPCLNAKRLLDTRMVDYVFLPIakisktEEHKTNKADLTRRAKEHGVvvtsmPQVFADGEYIGGF- 79
Cdd:COG0695    1 KVTLYTTP----GCPYCARAKRLLDEKGIPYEEIDV------DEDPEAREELRERSGRRTV-----PVIFIGGEHLGGFd 65


                 ....*....
gi 1308010330 80 -EELKAWVN 87
Cdd:COG0695   66 eGELDALLA 74
GlrX-dom TIGR02190
Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to ...
 14-85 1.65e-06

Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to an N-terminal peroxiredoxin-like domain.


Pssm-ID: 131245 [Multi-domain]  Cd Length: 79  Bit Score: 41.75  E-value: 1.65e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308010330 14 CKPCLNAKRLLDTRMVDYVFLPIAKiskteehktnkaDLTRRAKEHGVVVTSMPQVFADGEYIGGFEELKAW 85
Cdd:TIGR02190 18 CPFCAKAKATLKEKGYDFEEIPLGN------------DARGRSLRAVTGATTVPQVFIGGKLIGGSDELEAY 77
Glutaredoxin pfam00462
Glutaredoxin;
14-76 5.72e-04

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 34.79  E-value: 5.72e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308010330 14 CKPCLNAKRLLDTRMVDYVFLPIakisktEEHKTNKADLTRRAKehgvvVTSMPQVFADGEYI 76
Cdd:pfam00462  9 CPFCKRAKRLLKSLGVDFEEIDV------DEDPEIREELKELSG-----WPTVPQVFIDGEHI 60
 
Name Accession Description Interval E-value
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 14-84 4.81e-08

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.


Pssm-ID: 239017 [Multi-domain]  Cd Length: 72  Bit Score: 45.54  E-value: 4.81e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1308010330 14 CKPCLNAKRLLDTRMVDYVFLPIAkiskteEHKTNKADLTRRAKEHGVvvtsmPQVFADGEYIGGFEELKA 84
Cdd:cd02066   10 CPYCKRAKRLLESLGIEFEEIDIL------EDGELREELKELSGWPTV-----PQIFINGEFIGGYDDLKA 69
grxA PRK11200
glutaredoxin 1; Provisional
 14-89 9.60e-08

glutaredoxin 1; Provisional


Pssm-ID: 183036 [Multi-domain]  Cd Length: 85  Bit Score: 45.02  E-value: 9.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308010330 14 CKPCLNAKRLLDT-----RMVDYVFLPI--AKISKteehktnkADLTRRAkehGVVVTSMPQVFADGEYIGGFEELKAWV 86
Cdd:PRK11200  11 CPYCVRAKELAEKlseerDDFDYRYVDIhaEGISK--------ADLEKTV---GKPVETVPQIFVDQKHIGGCTDFEAYV 79


                 ...
gi 1308010330 87 NEN 89
Cdd:PRK11200  80 KEN 82
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
1-87 3.36e-07

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 43.26  E-value: 3.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308010330  1 MLEVYGFDplelECKPCLNAKRLLDTRMVDYVFLPIakisktEEHKTNKADLTRRAKEHGVvvtsmPQVFADGEYIGGF- 79
Cdd:COG0695    1 KVTLYTTP----GCPYCARAKRLLDEKGIPYEEIDV------DEDPEAREELRERSGRRTV-----PVIFIGGEHLGGFd 65


                 ....*....
gi 1308010330 80 -EELKAWVN 87
Cdd:COG0695   66 eGELDALLA 74
GlrX-dom TIGR02190
Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to ...
 14-85 1.65e-06

Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to an N-terminal peroxiredoxin-like domain.


Pssm-ID: 131245 [Multi-domain]  Cd Length: 79  Bit Score: 41.75  E-value: 1.65e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308010330 14 CKPCLNAKRLLDTRMVDYVFLPIAKiskteehktnkaDLTRRAKEHGVVVTSMPQVFADGEYIGGFEELKAW 85
Cdd:TIGR02190 18 CPFCAKAKATLKEKGYDFEEIPLGN------------DARGRSLRAVTGATTVPQVFIGGKLIGGSDELEAY 77
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 14-84 5.98e-06

Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of bacterial GRXs, 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 E. coli GRX1 and GRX3, which are members of this subfamily.


Pssm-ID: 239510 [Multi-domain]  Cd Length: 75  Bit Score: 40.26  E-value: 5.98e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1308010330 14 CKPCLNAKRLLDTRMVDYVFLPIakisktEEHKTNKADLTRRAkehGVVVTsMPQVFADGEYIGGFEELKA 84
Cdd:cd03418   10 CPYCVRAKALLDKKGVDYEEIDV------DGDPALREEMINRS---GGRRT-VPQIFIGDVHIGGCDDLYA 70
PRK10638 PRK10638
glutaredoxin 3; Provisional
 14-84 6.20e-06

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 40.57  E-value: 6.20e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308010330 14 CKPCLNAKRLLDTRMVDYVFLPI-AKISKTEEhktnkadLTRRAKEhgvvvTSMPQVFADGEYIGGFEELKA 84
Cdd:PRK10638  12 CPFCHRAKALLNSKGVSFQEIPIdGDAAKREE-------MIKRSGR-----TTVPQIFIDAQHIGGCDDLYA 71
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 14-85 6.89e-06

Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing peroxiredoxin (PRX) and GRX domains, which is found in some pathogenic bacteria and cyanobacteria. PRXs are thiol-specific antioxidant (TSA) proteins that confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins. PRX-GRX hybrid proteins from Haemophilus influenza and Neisseria meningitis exhibit GSH-dependent peroxidase activity. The flow of reducing equivalents in the catalytic cycle of the hybrid protein goes from NADPH -> GSH reductase -> GSH -> GRX domain of hybrid -> PRX domain of hybrid -> peroxide substrate.


Pssm-ID: 239327 [Multi-domain]  Cd Length: 72  Bit Score: 40.19  E-value: 6.89e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308010330 14 CKPCLNAKRLLDTRMVDYVFLPIAKiskteehktnkaDLTRRAKEHGVVVTSMPQVFADGEYIGGFEELKAW 85
Cdd:cd03029   11 CPFCARAKAALQENGISYEEIPLGK------------DITGRSLRAVTGAMTVPQVFIDGELIGGSDDLEKY 70
Glutaredoxin pfam00462
Glutaredoxin;
14-76 5.72e-04

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 34.79  E-value: 5.72e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308010330 14 CKPCLNAKRLLDTRMVDYVFLPIakisktEEHKTNKADLTRRAKehgvvVTSMPQVFADGEYI 76
Cdd:pfam00462  9 CPFCKRAKRLLKSLGVDFEEIDV------DEDPEIREELKELSG-----WPTVPQVFIDGEHI 60
GRX_DEP cd03027
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ...
 11-83 8.17e-04

Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of uncharacterized proteins containing a GRX domain and additional domains DEP and DUF547, both of which have unknown functions. GRX is a glutathione (GSH) dependent reductase containing a redox active CXXC motif in a TRX fold. It has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. By altering the redox state of target proteins, GRX is involved in many cellular functions.


Pssm-ID: 239325 [Multi-domain]  Cd Length: 73  Bit Score: 34.69  E-value: 8.17e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308010330 11 ELECKPCLNAKRLLDTRMVDYVFLPIAKiskteeHKTNKADLTRRAKeHGVVvtsmPQVFADGEYIGGFEELK 83
Cdd:cd03027    8 RLGCEDCTAVRLFLREKGLPYVEINIDI------FPERKAELEERTG-SSVV----PQIFFNEKLVGGLTDLK 69
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 14-84 3.77e-03

Glutaredoxin, GrxC 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 family of glutaredoxins includes the E. coli protein GrxC (Grx3) which appears to have a secondary role in reducing ribonucleotide reductase (in the absence of GrxA) possibly indicating a role in the reduction of other protein disulfides. [Energy metabolism, Electron transport]


Pssm-ID: 274017 [Multi-domain]  Cd Length: 79  Bit Score: 33.00  E-value: 3.77e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1308010330 14 CKPCLNAKRLLDTRMVDYvflPIAKISKTEEHKTNKADLTRRakehgvvvTSMPQVFADGEYIGGFEELKA 84
Cdd:TIGR02181  9 CPYCTRAKALLSSKGVTF---TEIRVDGDPALRDEMMQRSGR--------RTVPQIFIGDVHVGGCDDLYA 68
 
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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