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Conserved domains on  [gi|15218876|ref|NP_176772|]
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thioredoxin-dependent peroxidase 2 [Arabidopsis thaliana]

Protein Classification

peroxiredoxin family protein( domain architecture ID 10122413)

peroxiredoxin family protein such as peroxiredoxin 5, a thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively, playing a role in cell protection against oxidative stress by detoxifying peroxides

CATH:  3.40.30.10
EC:  1.11.1.-
Gene Ontology:  GO:0004601
PubMed:  15518547|12517450|15558583|10049365
SCOP:  4000042

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
 6-160 4.84e-78

Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, PRX5, a homodimeric TRX peroxidase, widely expressed in tissues and found cellularly in mitochondria, peroxisomes and the cytosol. The cellular location of PRX5 suggests that it may have an important antioxidant role in organelles that are major sources of reactive oxygen species (ROS), as well as a role in the control of signal transduction. PRX5 has been shown to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. As with all other PRXs, the N-terminal peroxidatic cysteine of PRX5 is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Human PRX5 is able to resolve this intermediate by forming an intramolecular disulfide bond with its C-terminal cysteine (the resolving cysteine), which can then be reduced by TRX, just like an atypical 2-cys PRX. This resolving cysteine, however, is not conserved in other members of the subfamily. In such cases, it is assumed that the oxidized cysteine is directly resolved by an external small-molecule or protein reductant, typical of a 1-cys PRX. In the case of the H. influenza PRX5 hybrid, the resolving glutaredoxin domain is on the same protein chain as PRX. PRX5 homodimers show an A-type interface, similar to atypical 2-cys PRXs.


:

Pssm-ID: 239311 [Multi-domain]  Cd Length: 155  Bit Score: 228.60  E-value: 4.84e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218876   6 VGDVVPDGTIsFFDENDQLQTVSVHSIAAGKKVILFGVPGAFTPTCSMSHVPGFIGKAEELKSKGIDEIICFSVNDPFVM 85
Cdd:cd03013   1 VGDKLPNVTL-FEYVPGPPNPVNLSELFKGKKVVIFGVPGAFTPTCSAQHLPGYVENADELKAKGVDEVICVSVNDPFVM 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218876  86 KAWGKTYPENKHVKFVADGSGEYTHLLGLELDLKDKGLGIRSRRFALLLDNLKVTVANVESG-GEFTVSSAEDILK 160
Cdd:cd03013  80 KAWGKALGAKDKIRFLADGNGEFTKALGLTLDLSAAGGGIRSKRYALIVDDGKVKYLFVEEDpGDVEVSSAENVLK 155
 
Name Accession Description Interval E-value
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
 6-160 4.84e-78

Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, PRX5, a homodimeric TRX peroxidase, widely expressed in tissues and found cellularly in mitochondria, peroxisomes and the cytosol. The cellular location of PRX5 suggests that it may have an important antioxidant role in organelles that are major sources of reactive oxygen species (ROS), as well as a role in the control of signal transduction. PRX5 has been shown to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. As with all other PRXs, the N-terminal peroxidatic cysteine of PRX5 is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Human PRX5 is able to resolve this intermediate by forming an intramolecular disulfide bond with its C-terminal cysteine (the resolving cysteine), which can then be reduced by TRX, just like an atypical 2-cys PRX. This resolving cysteine, however, is not conserved in other members of the subfamily. In such cases, it is assumed that the oxidized cysteine is directly resolved by an external small-molecule or protein reductant, typical of a 1-cys PRX. In the case of the H. influenza PRX5 hybrid, the resolving glutaredoxin domain is on the same protein chain as PRX. PRX5 homodimers show an A-type interface, similar to atypical 2-cys PRXs.


Pssm-ID: 239311 [Multi-domain]  Cd Length: 155  Bit Score: 228.60  E-value: 4.84e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218876   6 VGDVVPDGTIsFFDENDQLQTVSVHSIAAGKKVILFGVPGAFTPTCSMSHVPGFIGKAEELKSKGIDEIICFSVNDPFVM 85
Cdd:cd03013   1 VGDKLPNVTL-FEYVPGPPNPVNLSELFKGKKVVIFGVPGAFTPTCSAQHLPGYVENADELKAKGVDEVICVSVNDPFVM 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218876  86 KAWGKTYPENKHVKFVADGSGEYTHLLGLELDLKDKGLGIRSRRFALLLDNLKVTVANVESG-GEFTVSSAEDILK 160
Cdd:cd03013  80 KAWGKALGAKDKIRFLADGNGEFTKALGLTLDLSAAGGGIRSKRYALIVDDGKVKYLFVEEDpGDVEVSSAENVLK 155
AHP1 COG0678
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
3-162 7.55e-78

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440442  Cd Length: 160  Bit Score: 228.44  E-value: 7.55e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218876   3 PITVGDVVPDGTISFFdENDQLQTVSVHSIAAGKKVILFGVPGAFTPTCSMSHVPGFIGKAEELKSKGIDEIICFSVNDP 82
Cdd:COG0678   1 TIKVGDKLPDVTFKTR-TADGPEDVTTDDLFAGKKVVLFAVPGAFTPTCSSAHLPGFVELADAFKAKGVDEIACVSVNDA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218876  83 FVMKAWGKTYPENKHVKFVADGSGEYTHLLGLELDLKDKGLGIRSRRFALLLDNLKVTVANVE-SGGEFTVSSAEDILKA 161
Cdd:COG0678  80 FVMNAWGKAQGAEGKITMLADGNGEFTKALGLEVDKSALGFGKRSQRYAMLVEDGVVKKLNVEpAPGPFEVSDAETLLAQ 159


                .
gi 15218876 162 L 162
Cdd:COG0678 160 L 160
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 5-159 5.05e-33

Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 114.39  E-value: 5.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218876     5 TVGDVVPDgtISFFDENDQLQTVSVhSIAAGKKVILFGVPGAFTPTCSMSHVpgFIGK-AEELKSKGIDEIICFSVNDPF 83
Cdd:pfam08534   1 KAGDKAPD--FTLPDAATDGNTVSL-SDFKGKKVVLNFWPGAFCPTCSAEHP--YLEKlNELYKEKGVDVVAVNSDNDAF 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15218876    84 -VMKAWGKtypENKHVKFVADGSGEYTHLLGLELDLkDKGLGIRSRRFALLLDNLKVTVANVESGGEFTVSSAEDIL 159
Cdd:pfam08534  76 fVKRFWGK---EGLPFPFLSDGNAAFTKALGLPIEE-DASAGLRSPRYAVIDEDGKVVYLFVGPEPGVDVSDAEAVL 148
PRK13599 PRK13599
peroxiredoxin;
34-136 2.92e-05

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 42.39  E-value: 2.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218876   34 AGKKVILFGVPGAFTPTCSMSHVPgFIGKAEELKSKGIdEIICFSVNDPFVMKAWGKTYPENKHVKF----VADGSGEYT 109
Cdd:PRK13599  27 AGKWFVLFSHPADFTPVCTTEFVE-FARKANDFKELNT-ELIGLSVDQVFSHIKWVEWIKDNTNIAIpfpvIADDLGKVS 104

                         90       100
                 ....*....|....*....|....*..
gi 15218876  110 HLLGleldLKDKGLGIRSRRFALLLDN 136
Cdd:PRK13599 105 NQLG----MIHPGKGTNTVRAVFIVDD 127
 
Name Accession Description Interval E-value
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
 6-160 4.84e-78

Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, PRX5, a homodimeric TRX peroxidase, widely expressed in tissues and found cellularly in mitochondria, peroxisomes and the cytosol. The cellular location of PRX5 suggests that it may have an important antioxidant role in organelles that are major sources of reactive oxygen species (ROS), as well as a role in the control of signal transduction. PRX5 has been shown to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. As with all other PRXs, the N-terminal peroxidatic cysteine of PRX5 is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Human PRX5 is able to resolve this intermediate by forming an intramolecular disulfide bond with its C-terminal cysteine (the resolving cysteine), which can then be reduced by TRX, just like an atypical 2-cys PRX. This resolving cysteine, however, is not conserved in other members of the subfamily. In such cases, it is assumed that the oxidized cysteine is directly resolved by an external small-molecule or protein reductant, typical of a 1-cys PRX. In the case of the H. influenza PRX5 hybrid, the resolving glutaredoxin domain is on the same protein chain as PRX. PRX5 homodimers show an A-type interface, similar to atypical 2-cys PRXs.


Pssm-ID: 239311 [Multi-domain]  Cd Length: 155  Bit Score: 228.60  E-value: 4.84e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218876   6 VGDVVPDGTIsFFDENDQLQTVSVHSIAAGKKVILFGVPGAFTPTCSMSHVPGFIGKAEELKSKGIDEIICFSVNDPFVM 85
Cdd:cd03013   1 VGDKLPNVTL-FEYVPGPPNPVNLSELFKGKKVVIFGVPGAFTPTCSAQHLPGYVENADELKAKGVDEVICVSVNDPFVM 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218876  86 KAWGKTYPENKHVKFVADGSGEYTHLLGLELDLKDKGLGIRSRRFALLLDNLKVTVANVESG-GEFTVSSAEDILK 160
Cdd:cd03013  80 KAWGKALGAKDKIRFLADGNGEFTKALGLTLDLSAAGGGIRSKRYALIVDDGKVKYLFVEEDpGDVEVSSAENVLK 155
AHP1 COG0678
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
3-162 7.55e-78

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440442  Cd Length: 160  Bit Score: 228.44  E-value: 7.55e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218876   3 PITVGDVVPDGTISFFdENDQLQTVSVHSIAAGKKVILFGVPGAFTPTCSMSHVPGFIGKAEELKSKGIDEIICFSVNDP 82
Cdd:COG0678   1 TIKVGDKLPDVTFKTR-TADGPEDVTTDDLFAGKKVVLFAVPGAFTPTCSSAHLPGFVELADAFKAKGVDEIACVSVNDA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218876  83 FVMKAWGKTYPENKHVKFVADGSGEYTHLLGLELDLKDKGLGIRSRRFALLLDNLKVTVANVE-SGGEFTVSSAEDILKA 161
Cdd:COG0678  80 FVMNAWGKAQGAEGKITMLADGNGEFTKALGLEVDKSALGFGKRSQRYAMLVEDGVVKKLNVEpAPGPFEVSDAETLLAQ 159


                .
gi 15218876 162 L 162
Cdd:COG0678 160 L 160
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 5-159 5.05e-33

Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 114.39  E-value: 5.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218876     5 TVGDVVPDgtISFFDENDQLQTVSVhSIAAGKKVILFGVPGAFTPTCSMSHVpgFIGK-AEELKSKGIDEIICFSVNDPF 83
Cdd:pfam08534   1 KAGDKAPD--FTLPDAATDGNTVSL-SDFKGKKVVLNFWPGAFCPTCSAEHP--YLEKlNELYKEKGVDVVAVNSDNDAF 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15218876    84 -VMKAWGKtypENKHVKFVADGSGEYTHLLGLELDLkDKGLGIRSRRFALLLDNLKVTVANVESGGEFTVSSAEDIL 159
Cdd:pfam08534  76 fVKRFWGK---EGLPFPFLSDGNAAFTKALGLPIEE-DASAGLRSPRYAVIDEDGKVVYLFVGPEPGVDVSDAEAVL 148
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 10-159 3.91e-29

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: 104.17  E-value: 3.91e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218876  10 VPDGTIsffdENDQLQTVSVHSIAaGKKVILFGVPGAFTPTCSMShVPGFIGKAEELKsKGIDEIICFSVNDPFVMKAWG 89
Cdd:cd02971   2 APDFTL----PATDGGEVSLSDFK-GKWVVLFFYPKDFTPVCTTE-LCAFRDLAEEFA-KGGAEVLGVSVDSPFSHKAWA 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218876  90 KTYpENKHVKFVADGSGEYTHLLGLELDlkDKGLGIRSRRFALLLD-NLKVTVANVESGGefTVSSAEDIL 159
Cdd:cd02971  75 EKE-GGLNFPLLSDPDGEFAKAYGVLIE--KSAGGGLAARATFIIDpDGKIRYVEVEPLP--TGRNAEELL 140
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 6-127 2.70e-11

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: 57.62  E-value: 2.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218876     6 VGDVVPDgtisfFDENDQL-QTVSVHSIAaGKKVILFGVPGAFTPTCSMsHVPGFIGKAEELKSKGIdEIICFSVNDPFV 84
Cdd:pfam00578   1 VGDKAPD-----FELPDGDgGTVSLSDYR-GKWVVLFFYPADWTPVCTT-ELPALADLYEEFKKLGV-EVLGVSVDSPES 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 15218876    85 MKAWGKTYPENKHVkfVADGSGEYTHLLGLELDlkDKGLGIRS 127
Cdd:pfam00578  73 HKAFAEKYGLPFPL--LSDPDGEVARAYGVLNE--EEGGALRA 111
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 4-92 1.77e-07

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: 47.65  E-value: 1.77e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218876   4 ITVGDVVPDgtisfFDENDQ-LQTVSVHSIAAGKKVILFGVPGAFTPTCSMsHVPGFIGKAEELKSKGIdEIICFSVNDP 82
Cdd:cd03018   1 LEVGDKAPD-----FELPDQnGQEVRLSEFRGRKPVVLVFFPLAFTPVCTK-ELCALRDSLELFEAAGA-EVLGISVDSP 73

                        90
                ....*....|
gi 15218876  83 FVMKAWGKTY 92
Cdd:cd03018  74 FSLRAWAEEN 83
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
1-113 7.75e-07

Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];


Pssm-ID: 440219  Cd Length: 196  Bit Score: 46.61  E-value: 7.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218876   1 MAPItVGDVVPDgtisfFD----ENDQLQTVSVHSIAaGKKVILFGVPGAFTPTC-----SMSHvpgfigKAEELKSKGI 71
Cdd:COG0450   1 MMPL-IGDKAPD-----FTaeatHGGEFKKISLSDYK-GKWVVLFFHPADFTFVCptelgAFAK------RYEEFKKLGV 67

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15218876  72 dEIICFSVNDPFVMKAWGKTYPEN---KHVKF--VADGSGEYTHLLG 113
Cdd:COG0450  68 -EVIGLSVDSVFSHKAWHETIKEKggiVKIKFpiIADPTGKIARAYG 113
PRK13599 PRK13599
peroxiredoxin;
34-136 2.92e-05

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 42.39  E-value: 2.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218876   34 AGKKVILFGVPGAFTPTCSMSHVPgFIGKAEELKSKGIdEIICFSVNDPFVMKAWGKTYPENKHVKF----VADGSGEYT 109
Cdd:PRK13599  27 AGKWFVLFSHPADFTPVCTTEFVE-FARKANDFKELNT-ELIGLSVDQVFSHIKWVEWIKDNTNIAIpfpvIADDLGKVS 104

                         90       100
                 ....*....|....*....|....*..
gi 15218876  110 HLLGleldLKDKGLGIRSRRFALLLDN 136
Cdd:PRK13599 105 NQLG----MIHPGKGTNTVRAVFIVDD 127
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 6-127 1.49e-04

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: 40.18  E-value: 1.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218876   6 VGDVVPDGTISFFDENDQLQTVSVHSIAaGKKVILFGVPGAFTPTCSmSHVPGFIGKAEELKSKGIdEIICFSVNDPFVM 85
Cdd:cd03015   1 VGKKAPDFKATAVVPNGEFKEISLSDYK-GKWVVLFFYPLDFTFVCP-TEIIAFSDRYEEFKKLNA-EVLGVSTDSHFSH 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15218876  86 KAWGKTYPEN---KHVKF--VADGSGEYTHLLGLELDlkDKGLGIRS 127
Cdd:cd03015  78 LAWRNTPRKEgglGKINFplLADPKKKISRDYGVLDE--EEGVALRG 122
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 7-114 1.50e-04

Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one conserved cysteine, which serves as the peroxidatic cysteine. They are homodimeric thiol-specific antioxidant (TSA) proteins that confer a protective role in cells by reducing and detoxifying hydrogen peroxide, peroxynitrite, and organic hydroperoxides. As with all other PRXs, a cysteine sulfenic acid intermediate is formed upon reaction of 1-cys PRX with its substrates. Having no resolving cysteine, the oxidized enzyme is resolved by an external small-molecule or protein reductant such as thioredoxin or glutaredoxin. Similar to typical 2-cys PRX, 1-cys PRX forms a functional dimeric unit with a B-type interface, as well as a decameric structure which is stabilized in the reduced form of the enzyme. Other oligomeric forms, tetramers and hexamers, have also been reported. Mammalian 1-cys PRX is localized cellularly in the cytosol and is expressed at high levels in brain, eye, testes and lung. The seed-specific plant 1-cys PRXs protect tissues from reactive oxygen species during desiccation and are also called rehydrins.


Pssm-ID: 239314  Cd Length: 203  Bit Score: 40.22  E-value: 1.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218876   7 GDVVPD-------GTISFFDendqlqtvsvhsIAAGKKVILFGVPGAFTPTCSmSHVPGFIGKAEELKSKGIdEIICFSV 79
Cdd:cd03016   2 GDTAPNfeadtthGPIKFHD------------YLGDSWGILFSHPADFTPVCT-TELGAFAKLAPEFKKRNV-KLIGLSV 67

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15218876  80 NDPFVMKAWGKTYPENKHVKF----VADGSGEYTHLLGL 114
Cdd:cd03016  68 DSVESHIKWIEDIEEYTGVEIpfpiIADPDREVAKLLGM 106
PRK13189 PRK13189
peroxiredoxin; Provisional
 34-114 4.89e-04

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 38.81  E-value: 4.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218876   34 AGKKVILFGVPGAFTPTCSMSHVpGFIGKAEELKSKGIdEIICFSVNDPFVMKAWGKTYPENKHV--KF--VADGSGEYT 109
Cdd:PRK13189  34 KGKWFVLFSHPADFTPVCTTEFV-AFQKRYDEFRELNT-ELIGLSIDQVFSHIKWVEWIKEKLGVeiEFpiIADDRGEIA 111


                 ....*
gi 15218876  110 HLLGL 114
Cdd:PRK13189 112 KKLGM 116
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 3-128 6.44e-04

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 38.68  E-value: 6.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218876    3 PITVGDVVPD-------GTISFFDENdqlqtvsvhsiaaGKKVILFGVPGAFTPTCSMSHVpGFIGKAEELKSKGIdEII 75
Cdd:PRK13190   1 PVKLGQKAPDftvnttkGPIDLSKYK-------------GKWVLLFSHPADFTPVCTTEFI-AFSRRYEDFKKLGV-ELV 65

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15218876   76 CFSVNDPFVMKAWGKTYPENKHVKF----VADGSGEythlLGLELDLKDKGLGIRSR 128
Cdd:PRK13190  66 GLSVDSIYSHIAWLRDIEERFGIKIpfpvIADIDKE----LAREYNLIDENSGATVR 118
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 6-127 9.16e-03

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: 34.48  E-value: 9.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218876   6 VGDVVPDGTISffdeNDQLQTVSVhSIAAGKKVILFGVPGAFTPTCSMShVPGFIGKAEELksKGIDeIICFSVNDPFVM 85
Cdd:cd03014   2 VGDKAPDFTLV----TSDLSEVSL-ADFAGKVKVISVFPSIDTPVCATQ-TKRFNKEAAKL--DNTV-VLTISADLPFAQ 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15218876  86 KAWGKTYpENKHVKFVADgsgEYTHLLGLE--LDLKDKGLGIRS 127
Cdd:cd03014  73 KRWCGAE-GVDNVTTLSD---FRDHSFGKAygVLIKDLGLLARA 112
 
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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