MULTISPECIES: thiol:disulfide interchange protein DsbE [Klebsiella]
Protein Classification
thioredoxin domain-containing protein( domain architecture ID 144)
thioredoxin domain-containing protein may function as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| Thioredoxin_like super family | cl00388 | Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ... |
1-184 | 1.45e-130 | ||||
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is 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 the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others. The actual alignment was detected with superfamily member PRK15412: Pssm-ID: 469754 [Multi-domain] Cd Length: 185 Bit Score: 363.54 E-value: 1.45e-130
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| Name | Accession | Description | Interval | E-value | ||||
| PRK15412 | PRK15412 | thiol:disulfide interchange protein DsbE; Provisional |
1-184 | 1.45e-130 | ||||
thiol:disulfide interchange protein DsbE; Provisional Pssm-ID: 185310 [Multi-domain] Cd Length: 185 Bit Score: 363.54 E-value: 1.45e-130
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| dsbE | TIGR00385 | periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ... |
6-178 | 2.70e-98 | ||||
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the biogenesis of c-type cytochromes as well as in disulfide bond formation in some periplasmic proteins. [Protein fate, Protein folding and stabilization] Pssm-ID: 129481 [Multi-domain] Cd Length: 173 Bit Score: 281.67 E-value: 2.70e-98
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| TlpA_like_DsbE | cd03010 | TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ... |
43-169 | 1.18e-68 | ||||
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, periplasmic TRX-like reductase containing a CXXC motif that specifically donates reducing equivalents to apocytochrome c via CcmH, another cytochrome c maturation (Ccm) factor with a redox active CXXC motif. Assembly of cytochrome c requires the ligation of heme to reduced thiols of the apocytochrome. In bacteria, this assembly occurs in the periplasm. The reductase activity of DsbE in the oxidizing environment of the periplasm is crucial in the maturation of cytochrome c. Pssm-ID: 239308 [Multi-domain] Cd Length: 127 Bit Score: 204.73 E-value: 1.18e-68
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| TrxA | COG0526 | Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
41-178 | 1.54e-45 | ||||
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 146.76 E-value: 1.54e-45
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| Redoxin | pfam08534 | Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. |
42-164 | 5.37e-24 | ||||
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. Pssm-ID: 400717 [Multi-domain] Cd Length: 148 Bit Score: 92.05 E-value: 5.37e-24
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| Name | Accession | Description | Interval | E-value | ||||
| PRK15412 | PRK15412 | thiol:disulfide interchange protein DsbE; Provisional |
1-184 | 1.45e-130 | ||||
thiol:disulfide interchange protein DsbE; Provisional Pssm-ID: 185310 [Multi-domain] Cd Length: 185 Bit Score: 363.54 E-value: 1.45e-130
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| dsbE | TIGR00385 | periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ... |
6-178 | 2.70e-98 | ||||
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the biogenesis of c-type cytochromes as well as in disulfide bond formation in some periplasmic proteins. [Protein fate, Protein folding and stabilization] Pssm-ID: 129481 [Multi-domain] Cd Length: 173 Bit Score: 281.67 E-value: 2.70e-98
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| TlpA_like_DsbE | cd03010 | TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ... |
43-169 | 1.18e-68 | ||||
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, periplasmic TRX-like reductase containing a CXXC motif that specifically donates reducing equivalents to apocytochrome c via CcmH, another cytochrome c maturation (Ccm) factor with a redox active CXXC motif. Assembly of cytochrome c requires the ligation of heme to reduced thiols of the apocytochrome. In bacteria, this assembly occurs in the periplasm. The reductase activity of DsbE in the oxidizing environment of the periplasm is crucial in the maturation of cytochrome c. Pssm-ID: 239308 [Multi-domain] Cd Length: 127 Bit Score: 204.73 E-value: 1.18e-68
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| TrxA | COG0526 | Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
41-178 | 1.54e-45 | ||||
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 146.76 E-value: 1.54e-45
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| TlpA_like_family | cd02966 | TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ... |
48-161 | 2.24e-34 | ||||
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: 117.34 E-value: 2.24e-34
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| Bcp | COG1225 | Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
45-166 | 1.39e-26 | ||||
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440838 [Multi-domain] Cd Length: 136 Bit Score: 98.01 E-value: 1.39e-26
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| Redoxin | pfam08534 | Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. |
42-164 | 5.37e-24 | ||||
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. Pssm-ID: 400717 [Multi-domain] Cd Length: 148 Bit Score: 92.05 E-value: 5.37e-24
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| AhpC-TSA | pfam00578 | AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ... |
41-158 | 8.79e-16 | ||||
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: 69.95 E-value: 8.79e-16
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| PRK03147 | PRK03147 | thiol-disulfide oxidoreductase ResA; |
1-166 | 6.25e-14 | ||||
thiol-disulfide oxidoreductase ResA; Pssm-ID: 179545 [Multi-domain] Cd Length: 173 Bit Score: 66.18 E-value: 6.25e-14
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| PRK14018 | PRK14018 | bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide ... |
52-164 | 1.02e-07 | ||||
bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide reductase MsrB; Pssm-ID: 184456 [Multi-domain] Cd Length: 521 Bit Score: 50.64 E-value: 1.02e-07
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| TlpA_like_ScsD_MtbDsbE | cd03011 | TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ... |
57-154 | 2.04e-07 | ||||
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE homolog subfamily; composed of ScsD, the DsbE homolog of Mycobacterium tuberculosis (MtbDsbE) and similar proteins, all containing a redox-active CXXC motif. The Salmonella typhimurium ScsD is a thioredoxin-like protein which confers copper tolerance to copper-sensitive mutants of E. coli. MtbDsbE has been characterized as an oxidase in vitro, catalyzing the disulfide bond formation of substrates like hirudin. The reduced form of MtbDsbE is more stable than its oxidized form, consistent with an oxidase function. This is in contrast to the function of DsbE from gram-negative bacteria which is a specific reductase of apocytochrome c. Pssm-ID: 239309 [Multi-domain] Cd Length: 123 Bit Score: 47.68 E-value: 2.04e-07
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| PRX_like1 | cd02969 | Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ... |
42-166 | 2.21e-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: 45.69 E-value: 2.21e-06
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| CnoX | COG3118 | Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ... |
60-104 | 7.39e-06 | ||||
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 442352 [Multi-domain] Cd Length: 105 Bit Score: 42.88 E-value: 7.39e-06
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| TRX_family | cd02947 | TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ... |
63-101 | 1.19e-05 | ||||
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins. Pssm-ID: 239245 [Multi-domain] Cd Length: 93 Bit Score: 42.16 E-value: 1.19e-05
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| Thioredoxin_8 | pfam13905 | Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ... |
68-155 | 1.75e-05 | ||||
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Pssm-ID: 464033 [Multi-domain] Cd Length: 95 Bit Score: 41.52 E-value: 1.75e-05
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| PRX_AhpE_like | cd03018 | Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ... |
41-175 | 4.15e-05 | ||||
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: 41.88 E-value: 4.15e-05
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| Thioredoxin_2 | pfam13098 | Thioredoxin-like domain; |
66-155 | 9.11e-05 | ||||
Thioredoxin-like domain; Pssm-ID: 379034 [Multi-domain] Cd Length: 103 Bit Score: 40.10 E-value: 9.11e-05
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| DsbDgamma | cd02953 | DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ... |
64-83 | 9.21e-05 | ||||
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein DsbD. It contains a CXXC motif in a TRX fold and shuttles the reducing potential from the membrane domain (DsbD beta) to the N-terminal periplasmic domain (DsbD alpha). DsbD beta, a transmembrane domain comprising of eight helices, acquires its reducing potential from the cytoplasmic thioredoxin. DsbD alpha transfers the acquired reducing potential from DsbD gamma to target proteins such as the periplasmic protein disulphide isomerases, DsbC and DsbG. This flow of reducing potential from the cytoplasm through DsbD allows DsbC and DsbG to act as isomerases in the oxidizing environment of the bacterial periplasm. DsbD also transfers reducing potential from the cytoplasm to specific reductases in the periplasm which are involved in the maturation of cytochromes. Pssm-ID: 239251 [Multi-domain] Cd Length: 104 Bit Score: 39.89 E-value: 9.21e-05
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| DsbD | COG4232 | Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ... |
11-85 | 1.58e-04 | ||||
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443376 [Multi-domain] Cd Length: 416 Bit Score: 41.33 E-value: 1.58e-04
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| PRX_family | cd02971 | Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ... |
68-165 | 2.71e-04 | ||||
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins originally known as bacterioferritin comigratory proteins (BCP), based on their electrophoretic mobility before their function was identified. PRXs are thiol-specific antioxidant (TSA) proteins also known as TRX peroxidases and alkyl hydroperoxide reductase C22 (AhpC) proteins. They 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 TRX, glutathione, trypanothione and AhpF. They are distinct from other peroxidases in that they have no cofactors such as metals or prosthetic groups. The first step of catalysis, common to all PRXs, is the nucleophilic attack by the catalytic cysteine (also known as the peroxidatic cysteine) on the peroxide leading to cleavage of the oxygen-oxygen bond and the formation of a cysteine sulfenic acid intermediate. The second step of the reaction, the resolution of the intermediate, distinguishes the different types of PRXs. The presence or absence of a second cysteine (the resolving cysteine) classifies PRXs as either belonging to the 2-cys or 1-cys type. The resolving cysteine of 2-cys PRXs is either on the same chain (atypical) or on the second chain (typical) of a functional homodimer. Structural and motif analysis of this growing family supports the need for a new classification system. The peroxidase activity of PRXs is regulated in vivo by irreversible cysteine over-oxidation into a sulfinic acid, phosphorylation and limited proteolysis. Pssm-ID: 239269 [Multi-domain] Cd Length: 140 Bit Score: 39.45 E-value: 2.71e-04
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| TRX_superfamily | cd01659 | Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ... |
72-157 | 2.66e-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: 34.98 E-value: 2.66e-03
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| Thioredoxin_7 | pfam13899 | Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ... |
64-85 | 3.08e-03 | ||||
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Pssm-ID: 433567 [Multi-domain] Cd Length: 84 Bit Score: 35.41 E-value: 3.08e-03
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| TxlA | cd02950 | TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ... |
64-132 | 5.28e-03 | ||||
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium Synechococcus. It is found only in oxygenic photosynthetic organisms. TRX is a small enzyme that participate in redox reactions, via the reversible oxidation of an active site dithiol present in a CXXC motif. Disruption of the txlA gene suggests that the protein is involved in the redox regulation of the structure and function of photosynthetic apparatus. The plant homolog (designated as HCF164) is localized in the chloroplast and is involved in the assembly of the cytochrome b6f complex, which takes a central position in photosynthetic electron transport. Pssm-ID: 239248 [Multi-domain] Cd Length: 142 Bit Score: 35.78 E-value: 5.28e-03
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