MULTISPECIES: thiol peroxidase [Enterococcus]
peroxiredoxin( domain architecture ID 10005271)
atypical 2-Cys peroxiredoxin similar to thioredoxin-dependent thiol peroxidase (Tpx), a thiol-specific antioxidant (TSA) protein with substrate specificity toward alkyl hydroperoxides over hydrogen peroxide
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
Tpx | COG2077 | Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
1-161 | 7.01e-71 | ||||
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; : Pssm-ID: 441680 Cd Length: 168 Bit Score: 211.10 E-value: 7.01e-71
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Name | Accession | Description | Interval | E-value | ||||
Tpx | COG2077 | Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
1-161 | 7.01e-71 | ||||
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 441680 Cd Length: 168 Bit Score: 211.10 E-value: 7.01e-71
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PRX_Atyp2cys | cd03014 | Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ... |
18-158 | 7.24e-60 | ||||
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing peroxidatic and resolving cysteines, similar to the homodimeric thiol specific antioxidant (TSA) protein also known as TRX-dependent thiol peroxidase (Tpx). Tpx is a bacterial periplasmic peroxidase which differs from other PRXs in that it shows substrate specificity toward alkyl hydroperoxides over hydrogen peroxide. As with all other PRXs, the peroxidatic cysteine (N-terminal) of Tpx is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Tpx is able to resolve this intermediate by forming an intramolecular disulfide bond with a conserved C-terminal cysteine (the resolving cysteine), which can then be reduced by thioredoxin. This differs from the typical 2-cys PRX which resolves the oxidized cysteine by forming an intermolecular disulfide bond with the resolving cysteine from the other subunit of the homodimer. Atypical 2-cys PRX homodimers have a loop-based interface (A-type for alternate), in contrast with the B-type interface of typical 2-cys and 1-cys PRXs. Pssm-ID: 239312 [Multi-domain] Cd Length: 143 Bit Score: 182.40 E-value: 7.24e-60
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tpx | PRK00522 | thiol peroxidase; |
1-161 | 3.04e-53 | ||||
thiol peroxidase; Pssm-ID: 179055 Cd Length: 167 Bit Score: 166.23 E-value: 3.04e-53
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AhpC-TSA | pfam00578 | AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ... |
19-140 | 1.86e-24 | ||||
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA). Pssm-ID: 425763 [Multi-domain] Cd Length: 124 Bit Score: 91.52 E-value: 1.86e-24
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Name | Accession | Description | Interval | E-value | ||||
Tpx | COG2077 | Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
1-161 | 7.01e-71 | ||||
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 441680 Cd Length: 168 Bit Score: 211.10 E-value: 7.01e-71
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PRX_Atyp2cys | cd03014 | Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ... |
18-158 | 7.24e-60 | ||||
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing peroxidatic and resolving cysteines, similar to the homodimeric thiol specific antioxidant (TSA) protein also known as TRX-dependent thiol peroxidase (Tpx). Tpx is a bacterial periplasmic peroxidase which differs from other PRXs in that it shows substrate specificity toward alkyl hydroperoxides over hydrogen peroxide. As with all other PRXs, the peroxidatic cysteine (N-terminal) of Tpx is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Tpx is able to resolve this intermediate by forming an intramolecular disulfide bond with a conserved C-terminal cysteine (the resolving cysteine), which can then be reduced by thioredoxin. This differs from the typical 2-cys PRX which resolves the oxidized cysteine by forming an intermolecular disulfide bond with the resolving cysteine from the other subunit of the homodimer. Atypical 2-cys PRX homodimers have a loop-based interface (A-type for alternate), in contrast with the B-type interface of typical 2-cys and 1-cys PRXs. Pssm-ID: 239312 [Multi-domain] Cd Length: 143 Bit Score: 182.40 E-value: 7.24e-60
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tpx | PRK00522 | thiol peroxidase; |
1-161 | 3.04e-53 | ||||
thiol peroxidase; Pssm-ID: 179055 Cd Length: 167 Bit Score: 166.23 E-value: 3.04e-53
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AhpC-TSA | pfam00578 | AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ... |
19-140 | 1.86e-24 | ||||
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA). Pssm-ID: 425763 [Multi-domain] Cd Length: 124 Bit Score: 91.52 E-value: 1.86e-24
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Redoxin | pfam08534 | Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. |
18-156 | 3.25e-21 | ||||
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. Pssm-ID: 400717 [Multi-domain] Cd Length: 148 Bit Score: 83.96 E-value: 3.25e-21
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Bcp | COG1225 | Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
23-163 | 1.28e-20 | ||||
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440838 [Multi-domain] Cd Length: 136 Bit Score: 82.22 E-value: 1.28e-20
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PRX_AhpE_like | cd03018 | Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ... |
17-158 | 1.61e-18 | ||||
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium tuberculosis AhpE. AhpE is described as a 1-cys PRX because of the absence of a resolving cysteine. The structure and sequence of AhpE, however, show greater similarity to 2-cys PRXs than 1-cys PRXs. PRXs are thiol-specific antioxidant (TSA) proteins that confer a protective 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. The first step of catalysis is the nucleophilic attack by the peroxidatic cysteine on the peroxide leading to the formation of a cysteine sulfenic acid intermediate. The absence of a resolving cysteine suggests that functional AhpE is regenerated by an external reductant. The solution behavior and crystal structure of AhpE show that it forms dimers and octamers. Pssm-ID: 239316 [Multi-domain] Cd Length: 149 Bit Score: 76.93 E-value: 1.61e-18
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PRX_Typ2cys | cd03015 | Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ... |
19-142 | 1.49e-12 | ||||
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant (TSA) proteins, which confer a protective role in cells through its peroxidase activity by reducing hydrogen peroxide, peroxynitrite, and organic hydroperoxides. The functional unit of typical 2-cys PRX is a homodimer. A unique intermolecular redox-active disulfide center is utilized for its activity. Upon reaction with peroxides, its peroxidatic cysteine is oxidized into a sulfenic acid intermediate which is resolved by bonding with the resolving cysteine from the other subunit of the homodimer. This intermolecular disulfide bond is then reduced by thioredoxin, tryparedoxin or AhpF. Typical 2-cys PRXs, like 1-cys PRXs, form decamers which are stabilized by reduction of the active site cysteine. Typical 2-cys PRX interacts through beta strands at one edge of the monomer (B-type interface) to form the functional homodimer, and uses an A-type interface (similar to the dimeric interface in atypical 2-cys PRX and PRX5) at the opposite end of the monomer to form the stable decameric (pentamer of dimers) structure. Pssm-ID: 239313 Cd Length: 173 Bit Score: 61.75 E-value: 1.49e-12
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PRX_BCP | cd03017 | Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ... |
21-140 | 2.72e-11 | ||||
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of thioredoxin-dependent thiol peroxidases, widely expressed in pathogenic bacteria, that protect cells against toxicity from reactive oxygen species by reducing and detoxifying hydroperoxides. The protein was named BCP based on its electrophoretic mobility before its function was known. BCP shows substrate selectivity toward fatty acid hydroperoxides rather than hydrogen peroxide or alkyl hydroperoxides. BCP contains the peroxidatic cysteine but appears not to possess a resolving cysteine (some sequences, not all, contain a second cysteine but its role is still unknown). Unlike other PRXs, BCP exists as a monomer. The plant homolog of BCP is PRX Q, which is expressed only in leaves and is cellularly localized in the chloroplasts and the guard cells of stomata. Also included in this subfamily is the fungal nuclear protein, Dot5p (for disrupter of telomere silencing protein 5), which functions as an alkyl-hydroperoxide reductase during post-diauxic growth. Pssm-ID: 239315 Cd Length: 140 Bit Score: 57.94 E-value: 2.72e-11
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TlpA_like_family | cd02966 | TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ... |
25-140 | 1.65e-08 | ||||
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases. Pssm-ID: 239264 [Multi-domain] Cd Length: 116 Bit Score: 49.93 E-value: 1.65e-08
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PRX_like1 | cd02969 | Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ... |
20-162 | 1.88e-06 | ||||
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a conserved cysteine that aligns to the first cysteine in the CXXC motif of TRX. This does not correspond to the peroxidatic cysteine found in PRXs, which aligns to the second cysteine in the CXXC motif of TRX. In addition, these proteins do not contain the other two conserved residues of the catalytic triad of PRX. PRXs 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. Pssm-ID: 239267 [Multi-domain] Cd Length: 171 Bit Score: 45.31 E-value: 1.88e-06
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bcp | PRK09437 | thioredoxin-dependent thiol peroxidase; Reviewed |
18-140 | 3.85e-06 | ||||
thioredoxin-dependent thiol peroxidase; Reviewed Pssm-ID: 181857 Cd Length: 154 Bit Score: 44.16 E-value: 3.85e-06
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PRK10382 | PRK10382 | alkyl hydroperoxide reductase subunit C; Provisional |
35-145 | 4.06e-05 | ||||
alkyl hydroperoxide reductase subunit C; Provisional Pssm-ID: 182423 Cd Length: 187 Bit Score: 41.90 E-value: 4.06e-05
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SCO | cd02968 | SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ... |
23-137 | 7.64e-05 | ||||
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to Sco1, a membrane-anchored protein possessing a soluble domain with a TRX fold. Members of this family are required for the proper assembly of cytochrome c oxidase (COX). They contain a metal binding motif, typically CXXXC, which is located in a flexible loop. COX, the terminal enzyme in the respiratory chain, is imbedded in the inner mitochondrial membrane of all eukaryotes and in the plasma membrane of some prokaryotes. It is composed of two subunits, COX I and COX II. It has been proposed that Sco1 specifically delivers copper to the CuA site, a dinuclear copper center, of the COX II subunit. Mutations in human Sco1 and Sco2 cause fatal infantile hepatoencephalomyopathy and cardioencephalomyopathy, respectively. Both disorders are associated with severe COX deficiency in affected tissues. More recently, it has been argued that the redox sensitivity of the copper binding properties of Sco1 implies that it participates in signaling events rather than functioning as a chaperone that transfers copper to COX II. Pssm-ID: 239266 Cd Length: 142 Bit Score: 40.66 E-value: 7.64e-05
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PTZ00253 | PTZ00253 | tryparedoxin peroxidase; Provisional |
34-142 | 2.16e-03 | ||||
tryparedoxin peroxidase; Provisional Pssm-ID: 140280 Cd Length: 199 Bit Score: 37.19 E-value: 2.16e-03
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Blast search parameters | ||||
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