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Conserved domains on  [gi|446792482|ref|WP_000869738|]
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MULTISPECIES: glutaredoxin family protein [Bacillus]

Protein Classification

glutaredoxin family protein( domain architecture ID 10530477)

glutaredoxin/thioredoxin family protein functions as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein thiol or disulfide bonds using an active site disulfide or dithiol, present in a CXXC motif

CATH:  3.40.30.10
PubMed:  11441809|11012661|14713336
SCOP:  4000237

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glrx-like pfam05768
Glutaredoxin-like domain (DUF836); These proteins are related to the pfam00462 family. This ...
 3-76 9.98e-21

Glutaredoxin-like domain (DUF836); These proteins are related to the pfam00462 family. This entry includes several viral glutaredoxins and many related bacterial and eukaryotic proteins of unknown function. The best characterized member is G4L from Vaccinia virus (strain Western Reserve/WR) (VACV), which is necessary for virion morphogenesis and replication. This is a cytoplasmic protein which functions as a shuttle in a redox pathway between membrane-associated E10R and L1R or F9L.


:

Pssm-ID: 399055  Cd Length: 80  Bit Score: 77.72  E-value: 9.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446792482   3 VVLYTKNDCGLCVKAKQVLQEVQCEYSFQIEEIDIYEDNDLLEKYHLMIPVVEIDG------KQVEYGNIHKGVIINYIK 76
Cdd:pfam05768  1 LTLYGKPGCGLCEGAEEVLEPLALELGFELEVIDIDGDPELLAKYGLEIPVLAFVGiskffnLEILSWRLDEEQLAAELE 80
 
Name Accession Description Interval E-value
Glrx-like pfam05768
Glutaredoxin-like domain (DUF836); These proteins are related to the pfam00462 family. This ...
 3-76 9.98e-21

Glutaredoxin-like domain (DUF836); These proteins are related to the pfam00462 family. This entry includes several viral glutaredoxins and many related bacterial and eukaryotic proteins of unknown function. The best characterized member is G4L from Vaccinia virus (strain Western Reserve/WR) (VACV), which is necessary for virion morphogenesis and replication. This is a cytoplasmic protein which functions as a shuttle in a redox pathway between membrane-associated E10R and L1R or F9L.


Pssm-ID: 399055  Cd Length: 80  Bit Score: 77.72  E-value: 9.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446792482   3 VVLYTKNDCGLCVKAKQVLQEVQCEYSFQIEEIDIYEDNDLLEKYHLMIPVVEIDG------KQVEYGNIHKGVIINYIK 76
Cdd:pfam05768  1 LTLYGKPGCGLCEGAEEVLEPLALELGFELEVIDIDGDPELLAKYGLEIPVLAFVGiskffnLEILSWRLDEEQLAAELE 80
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
2-61 2.75e-11

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 53.28  E-value: 2.75e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446792482  2 KVVLYTKNDCGLCVKAKQVLQevqcEYSFQIEEIDIYED----NDLLEKYHLM-IPVVEIDGKQV 61
Cdd:COG0695   1 KVTLYTTPGCPYCARAKRLLD----EKGIPYEEIDVDEDpearEELRERSGRRtVPVIFIGGEHL 61
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 2-61 3.37e-08

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.


Pssm-ID: 239274 [Multi-domain]  Cd Length: 73  Bit Score: 45.68  E-value: 3.37e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446792482  2 KVVLYTKNDCGLCVKAKQVLQEVQCEYsfqiEEIDIYEDNDLLEKYH-----LMIPVVEIDGKQV 61
Cdd:cd02976   1 EVTVYTKPDCPYCKATKRFLDERGIPF----EEVDVDEDPEALEELKklngyRSVPVVVIGDEHL 61
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
 2-61 7.21e-07

Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the conserved CxxC motif and includes the Clostridium pasteurianum protein YruB which has been cloned from a rubredoxin operon. Somewhat related to NrdH, it is unknown whether this protein actually interacts with glutathione/glutathione reducatase, or, like NrdH, some other reductant system.


Pssm-ID: 274027 [Multi-domain]  Cd Length: 74  Bit Score: 42.37  E-value: 7.21e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446792482   2 KVVLYTKNDCGLCVKAKQVLQEVQCEYsfqiEEIDIYED----NDLLEKYHLM-IPVVEIDGKQV 61
Cdd:TIGR02196  1 KVKVYTTPWCPPCVKAKEYLTSKGVAF----EEIDVEKDaaarEELLKVYGQRgVPVIVIGHKIV 61
 
Name Accession Description Interval E-value
Glrx-like pfam05768
Glutaredoxin-like domain (DUF836); These proteins are related to the pfam00462 family. This ...
 3-76 9.98e-21

Glutaredoxin-like domain (DUF836); These proteins are related to the pfam00462 family. This entry includes several viral glutaredoxins and many related bacterial and eukaryotic proteins of unknown function. The best characterized member is G4L from Vaccinia virus (strain Western Reserve/WR) (VACV), which is necessary for virion morphogenesis and replication. This is a cytoplasmic protein which functions as a shuttle in a redox pathway between membrane-associated E10R and L1R or F9L.


Pssm-ID: 399055  Cd Length: 80  Bit Score: 77.72  E-value: 9.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446792482   3 VVLYTKNDCGLCVKAKQVLQEVQCEYSFQIEEIDIYEDNDLLEKYHLMIPVVEIDG------KQVEYGNIHKGVIINYIK 76
Cdd:pfam05768  1 LTLYGKPGCGLCEGAEEVLEPLALELGFELEVIDIDGDPELLAKYGLEIPVLAFVGiskffnLEILSWRLDEEQLAAELE 80
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
2-61 2.75e-11

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 53.28  E-value: 2.75e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446792482  2 KVVLYTKNDCGLCVKAKQVLQevqcEYSFQIEEIDIYED----NDLLEKYHLM-IPVVEIDGKQV 61
Cdd:COG0695   1 KVTLYTTPGCPYCARAKRLLD----EKGIPYEEIDVDEDpearEELRERSGRRtVPVIFIGGEHL 61
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 2-61 3.37e-08

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.


Pssm-ID: 239274 [Multi-domain]  Cd Length: 73  Bit Score: 45.68  E-value: 3.37e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446792482  2 KVVLYTKNDCGLCVKAKQVLQEVQCEYsfqiEEIDIYEDNDLLEKYH-----LMIPVVEIDGKQV 61
Cdd:cd02976   1 EVTVYTKPDCPYCKATKRFLDERGIPF----EEVDVDEDPEALEELKklngyRSVPVVVIGDEHL 61
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
 2-61 7.21e-07

Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the conserved CxxC motif and includes the Clostridium pasteurianum protein YruB which has been cloned from a rubredoxin operon. Somewhat related to NrdH, it is unknown whether this protein actually interacts with glutathione/glutathione reducatase, or, like NrdH, some other reductant system.


Pssm-ID: 274027 [Multi-domain]  Cd Length: 74  Bit Score: 42.37  E-value: 7.21e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446792482   2 KVVLYTKNDCGLCVKAKQVLQEVQCEYsfqiEEIDIYED----NDLLEKYHLM-IPVVEIDGKQV 61
Cdd:TIGR02196  1 KVKVYTTPWCPPCVKAKEYLTSKGVAF----EEIDVEKDaaarEELLKVYGQRgVPVIVIGHKIV 61
Glutaredoxin pfam00462
Glutaredoxin;
3-61 2.76e-06

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 40.57  E-value: 2.76e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446792482   3 VVLYTKNDCGLCVKAKQVLQevqcEYSFQIEEIDIYEDND----LLEKYHLM-IPVVEIDGKQV 61
Cdd:pfam00462  1 VVLYTKPTCPFCKRAKRLLK----SLGVDFEEIDVDEDPEireeLKELSGWPtVPQVFIDGEHI 60
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 2-45 1.51e-05

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: 38.60  E-value: 1.51e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 446792482  2 KVVLYTKNDCGLCVKAKQVLQevqcEYSFQIEEIDIYEDNDLLE 45
Cdd:cd02066   1 KVVVFSKSTCPYCKRAKRLLE----SLGIEFEEIDILEDGELRE 40
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 2-46 2.02e-05

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: 38.72  E-value: 2.02e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 446792482  2 KVVLYTKNDCGLCVKAKQVLQevqcEYSFQIEEIDIYEDNDLLEK 46
Cdd:cd03418   1 KVEIYTKPNCPYCVRAKALLD----KKGVDYEEIDVDGDPALREE 41
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 3-61 7.84e-04

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: 34.41  E-value: 7.84e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446792482  3 VVLYTKNDCGLCVKAKQVLQEVQCEYsfqiEEIDIyeDNDLLEKY------HLMIPVVEIDGKQV 61
Cdd:cd03029   3 VSLFTKPGCPFCARAKAALQENGISY----EEIPL--GKDITGRSlravtgAMTVPQVFIDGELI 61
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 2-47 9.27e-04

Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of proteins similar to human 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 human GRX1 and GRX2, which are members of this subfamily. Also included in this subfamily are the N-terminal GRX domains of proteins similar to human thioredoxin reductase 1 and 3.


Pssm-ID: 239511 [Multi-domain]  Cd Length: 82  Bit Score: 34.44  E-value: 9.27e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 446792482  2 KVVLYTKNDCGLCVKAKQVLQEVQCEYsfQIEEIDIYEDNDLLEKY 47
Cdd:cd03419   1 PVVVFSKSYCPYCKRAKSLLKELGVKP--AVVELDQHEDGSEIQDY 44
GlrX_NrdH TIGR02194
Glutaredoxin-like protein NrdH; NrdH-redoxin is a representative of a class of small redox ...
 3-58 1.70e-03

Glutaredoxin-like protein NrdH; NrdH-redoxin is a representative of a class of small redox proteins that contain a conserved CXXC motif and are characterized by a glutaredoxin-like amino acid sequence and thioredoxin-like activity profile. Unlike other the glutaredoxins to which it is most closely related, NrdH aparrently does not interact with glutathione/glutathione reductase, but rather with thioredoxin reductase to catalyze the reduction of ribonucleotide reductase.


Pssm-ID: 131249  Cd Length: 72  Bit Score: 33.55  E-value: 1.70e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446792482   3 VVLYTKNDCGLCVKAKQVLQevqcEYSFQIEEIDIYEDNDLLEKYHLM----IPVVEIDG 58
Cdd:TIGR02194  1 ITVYSKNNCVQCKMTKKALE----EHGIAFEEINIDEQPEAIDYVKAQgfrqVPVIVADG 56
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 3-63 9.34e-03

Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include TRX, protein disulfide isomerase (PDI), tlpA-like, glutaredoxin, NrdH redoxin, and the bacterial Dsb (DsbA, DsbC, DsbG, DsbE, DsbDgamma) protein families. Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins and glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 31.51  E-value: 9.34e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446792482  3 VVLYTKNDCGLCVKAKQVLQEVQCEYS-FQIEEIDIYEDNDLLEK----YHLMIPVVEIDGKQVEY 63
Cdd:cd01659   1 LVLFYAPWCPFCQALRPVLAELALLNKgVKFEAVDVDEDPALEKElkryGVGGVPTLVVFGPGIGV 66
 
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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