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Conserved domains on  [gi|1228171435|gb|OXY57476|]
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glutaredoxin [Salmonella enterica subsp. enterica serovar Enteritidis str. SHSE004]

Protein Classification

redoxin NrdH( domain architecture ID 10793377)

redoxin NrdH is a thiol disulfide reductase characterized by a glutaredoxin-like amino acid sequence and a thioredoxin-like activity profile, and it functions as the electron donor for NrdEF ribonucleotide reductase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10329 PRK10329
glutaredoxin-like protein NrdH;
1-81 4.60e-58

glutaredoxin-like protein NrdH;


:

Pssm-ID: 182381  Cd Length: 81  Bit Score: 172.01  E-value: 4.60e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228171435  1 MSITIYTRNNCVQCHATKRAMESRGFEFEMVNVDLVPDAADTLRAQGFRQLPVVMAGDLSWSGFRPDMINRLHPTPHAAN 80
Cdd:PRK10329   1 MRITIYTRNDCVQCHATKRAMESRGFDFEMINVDRVPEAAETLRAQGFRQLPVVIAGDLSWSGFRPDMINRLHPAPHAAS 80

                 .
gi 1228171435 81 A 81
Cdd:PRK10329  81 A 81
 
Name Accession Description Interval E-value
PRK10329 PRK10329
glutaredoxin-like protein NrdH;
1-81 4.60e-58

glutaredoxin-like protein NrdH;


Pssm-ID: 182381  Cd Length: 81  Bit Score: 172.01  E-value: 4.60e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228171435  1 MSITIYTRNNCVQCHATKRAMESRGFEFEMVNVDLVPDAADTLRAQGFRQLPVVMAGDLSWSGFRPDMINRLHPTPHAAN 80
Cdd:PRK10329   1 MRITIYTRNDCVQCHATKRAMESRGFDFEMINVDRVPEAAETLRAQGFRQLPVVIAGDLSWSGFRPDMINRLHPAPHAAS 80

                 .
gi 1228171435 81 A 81
Cdd:PRK10329  81 A 81
GlrX_NrdH TIGR02194
Glutaredoxin-like protein NrdH; NrdH-redoxin is a representative of a class of small redox ...
3-73 1.65e-42

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: 132.54  E-value: 1.65e-42
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1228171435  3 ITIYTRNNCVQCHATKRAMESRGFEFEMVNVDLVPDAADTLRAQGFRQLPVVMA-GDLSWSGFRPDMINRLH 73
Cdd:TIGR02194  1 ITVYSKNNCVQCKMTKKALEEHGIAFEEINIDEQPEAIDYVKAQGFRQVPVIVAdGDLSWSGFRPDKLKALA 72
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
3-72 3.88e-27

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: 93.44  E-value: 3.88e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1228171435  3 ITIYTRNNCVQCHATKRAMESRGFEFEMVNVDLVPDAADTLRAQ-GFRQLPVVMAGDLSWSGFRPDMINRL 72
Cdd:cd02976    2 VTVYTKPDCPYCKATKRFLDERGIPFEEVDVDEDPEALEELKKLnGYRSVPVVVIGDEHLSGFRPDKLRAL 72
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
3-72 2.01e-22

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 81.78  E-value: 2.01e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1228171435  3 ITIYTRNNCVQCHATKRAMESRGFEFEMVNVDLVPDAADTLRAQ-GFRQLPVVMAGDLSWSGFRPDMINRL 72
Cdd:COG0695    2 VTLYTTPGCPYCARAKRLLDEKGIPYEEIDVDEDPEAREELRERsGRRTVPVIFIGGEHLGGFDEGELDAL 72
Glutaredoxin pfam00462
Glutaredoxin;
3-58 1.19e-12

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 56.74  E-value: 1.19e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 1228171435  3 ITIYTRNNCVQCHATKRAMESRGFEFEMVNVDLVPDAADTLRAQ-GFRQLPVVMAGD 58
Cdd:pfam00462  1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREELKELsGWPTVPQVFIDG 57
 
Name Accession Description Interval E-value
PRK10329 PRK10329
glutaredoxin-like protein NrdH;
1-81 4.60e-58

glutaredoxin-like protein NrdH;


Pssm-ID: 182381  Cd Length: 81  Bit Score: 172.01  E-value: 4.60e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228171435  1 MSITIYTRNNCVQCHATKRAMESRGFEFEMVNVDLVPDAADTLRAQGFRQLPVVMAGDLSWSGFRPDMINRLHPTPHAAN 80
Cdd:PRK10329   1 MRITIYTRNDCVQCHATKRAMESRGFDFEMINVDRVPEAAETLRAQGFRQLPVVIAGDLSWSGFRPDMINRLHPAPHAAS 80

                 .
gi 1228171435 81 A 81
Cdd:PRK10329  81 A 81
GlrX_NrdH TIGR02194
Glutaredoxin-like protein NrdH; NrdH-redoxin is a representative of a class of small redox ...
3-73 1.65e-42

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: 132.54  E-value: 1.65e-42
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1228171435  3 ITIYTRNNCVQCHATKRAMESRGFEFEMVNVDLVPDAADTLRAQGFRQLPVVMA-GDLSWSGFRPDMINRLH 73
Cdd:TIGR02194  1 ITVYSKNNCVQCKMTKKALEEHGIAFEEINIDEQPEAIDYVKAQGFRQVPVIVAdGDLSWSGFRPDKLKALA 72
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
3-72 3.88e-27

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: 93.44  E-value: 3.88e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1228171435  3 ITIYTRNNCVQCHATKRAMESRGFEFEMVNVDLVPDAADTLRAQ-GFRQLPVVMAGDLSWSGFRPDMINRL 72
Cdd:cd02976    2 VTVYTKPDCPYCKATKRFLDERGIPFEEVDVDEDPEALEELKKLnGYRSVPVVVIGDEHLSGFRPDKLRAL 72
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
3-72 2.01e-22

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 81.78  E-value: 2.01e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1228171435  3 ITIYTRNNCVQCHATKRAMESRGFEFEMVNVDLVPDAADTLRAQ-GFRQLPVVMAGDLSWSGFRPDMINRL 72
Cdd:COG0695    2 VTLYTTPGCPYCARAKRLLDEKGIPYEEIDVDEDPEAREELRERsGRRTVPVIFIGGEHLGGFDEGELDAL 72
Glutaredoxin pfam00462
Glutaredoxin;
3-58 1.19e-12

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 56.74  E-value: 1.19e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 1228171435  3 ITIYTRNNCVQCHATKRAMESRGFEFEMVNVDLVPDAADTLRAQ-GFRQLPVVMAGD 58
Cdd:pfam00462  1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREELKELsGWPTVPQVFIDG 57
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
3-72 6.64e-12

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: 55.08  E-value: 6.64e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1228171435  3 ITIYTRNNCVQCHATKRAMESRGFEFEMVNVDLVPDAAD-TLRAQGFRQLPVVMAGDLSWSGFRPDMINRL 72
Cdd:TIGR02196  2 VKVYTTPWCPPCVKAKEYLTSKGVAFEEIDVEKDAAAREeLLKVYGQRGVPVIVIGHKIVVGFDPEKLDQL 72
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
3-64 1.30e-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: 41.42  E-value: 1.30e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1228171435  3 ITIYTRNNCVQCHATKRAMESRGFEFEMVNVDLVPDAADTL--RAQGFRQLPVVMAGDLSWSGF 64
Cdd:cd03418    2 VEIYTKPNCPYCVRAKALLDKKGVDYEEIDVDGDPALREEMinRSGGRRTVPQIFIGDVHIGGC 65
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
3-34 9.01e-04

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: 34.36  E-value: 9.01e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 1228171435  3 ITIYTRNNCVQCHATKRAMESRGFEFEMVNVD 34
Cdd:cd02066    2 VVVFSKSTCPYCKRAKRLLESLGIEFEEIDIL 33
GRX_DEP cd03027
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ...
3-37 1.60e-03

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: 33.54  E-value: 1.60e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 1228171435  3 ITIYTRNNCVQCHATKRAMESRGFEFEMVNVDLVP 37
Cdd:cd03027    3 VTIYSRLGCEDCTAVRLFLREKGLPYVEINIDIFP 37
GST_N_SspA cd03059
GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ...
3-59 3.23e-03

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.


Pssm-ID: 239357 [Multi-domain]  Cd Length: 73  Bit Score: 32.69  E-value: 3.23e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 1228171435  3 ITIYTRNNCVQCHATKRAMESRGFEFEMVNVDLVPDAADTLRAQGFRQLPVVMAGDL 59
Cdd:cd03059    1 MTLYSGPDDVYSHRVRIVLAEKGVSVEIIDVDPDNPPEDLAELNPYGTVPTLVDRDL 57
 
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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