glutaredoxin family protein [Photobacterium leiognathi]
Protein Classification
glutaredoxin family protein( domain architecture ID 10002164)
glutaredoxin (GRX) family protein similar to GRX, a glutathione dependent reductase that catalyzes the reduction of disulfides in target proteins using an active site dithiol, present in a CXXC motif
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| GrxC | COG0695 | Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; |
3-74 | 5.62e-16 | ||
Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; : Pssm-ID: 440459 [Multi-domain] Cd Length: 74 Bit Score: 65.22 E-value: 5.62e-16
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| Name | Accession | Description | Interval | E-value | ||
| GrxC | COG0695 | Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; |
3-74 | 5.62e-16 | ||
Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440459 [Multi-domain] Cd Length: 74 Bit Score: 65.22 E-value: 5.62e-16
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| NrdH | cd02976 | NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ... |
3-73 | 1.61e-15 | ||
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: 64.17 E-value: 1.61e-15
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| GlrX_YruB | TIGR02196 | Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ... |
3-74 | 6.83e-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: 6.83e-12
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| Glutaredoxin | pfam00462 | Glutaredoxin; |
4-60 | 9.02e-08 | ||
Glutaredoxin; Pssm-ID: 425695 [Multi-domain] Cd Length: 60 Bit Score: 44.03 E-value: 9.02e-08
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| Uxx_star | NF041212 | Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like ... |
4-65 | 5.70e-05 | ||
Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like folds, a length of about 75 amino acids, and a CxxC, C/UxxT, or CxxS motif near the N-terminus end with a UXX-COOH motif. That final motif typically is missed during coding region feature prediction by genome annotation pipelines. This HMM covers proteins from several distinctive families with this feature. The seed alignment illustrates the final selenocysteine or aligned Cys or Ser residues, but the HMM also hits proteins that lack an equivalent motif at the C-terminus. This C-terminal selenocysteine-containing motif has not yet been described in the literature. Pssm-ID: 469116 [Multi-domain] Cd Length: 70 Bit Score: 37.06 E-value: 5.70e-05
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| PRK10329 | PRK10329 | glutaredoxin-like protein NrdH; |
3-58 | 1.38e-03 | ||
glutaredoxin-like protein NrdH; Pssm-ID: 182381 Cd Length: 81 Bit Score: 33.73 E-value: 1.38e-03
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| Name | Accession | Description | Interval | E-value | ||
| GrxC | COG0695 | Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; |
3-74 | 5.62e-16 | ||
Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440459 [Multi-domain] Cd Length: 74 Bit Score: 65.22 E-value: 5.62e-16
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| NrdH | cd02976 | NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ... |
3-73 | 1.61e-15 | ||
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: 64.17 E-value: 1.61e-15
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| GlrX_YruB | TIGR02196 | Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ... |
3-74 | 6.83e-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: 6.83e-12
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| Glutaredoxin | pfam00462 | Glutaredoxin; |
4-60 | 9.02e-08 | ||
Glutaredoxin; Pssm-ID: 425695 [Multi-domain] Cd Length: 60 Bit Score: 44.03 E-value: 9.02e-08
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| GRX_family | cd02066 | Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ... |
3-63 | 7.98e-06 | ||
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: 39.37 E-value: 7.98e-06
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| Uxx_star | NF041212 | Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like ... |
4-65 | 5.70e-05 | ||
Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like folds, a length of about 75 amino acids, and a CxxC, C/UxxT, or CxxS motif near the N-terminus end with a UXX-COOH motif. That final motif typically is missed during coding region feature prediction by genome annotation pipelines. This HMM covers proteins from several distinctive families with this feature. The seed alignment illustrates the final selenocysteine or aligned Cys or Ser residues, but the HMM also hits proteins that lack an equivalent motif at the C-terminus. This C-terminal selenocysteine-containing motif has not yet been described in the literature. Pssm-ID: 469116 [Multi-domain] Cd Length: 70 Bit Score: 37.06 E-value: 5.70e-05
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| PRK10329 | PRK10329 | glutaredoxin-like protein NrdH; |
3-58 | 1.38e-03 | ||
glutaredoxin-like protein NrdH; Pssm-ID: 182381 Cd Length: 81 Bit Score: 33.73 E-value: 1.38e-03
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