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Conserved domains on  [gi|494040524|ref|WP_006982649|]
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peroxiredoxin [Chthoniobacter flavus]

Protein Classification

peroxiredoxin( domain architecture ID 10122458)

peroxiredoxin belonging to the bacterioferritin comigratory protein (BCP) subfamily is a thioredoxin-dependent thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively

CATH:  3.40.30.10
EC:  1.11.1.24
Gene Ontology:  GO:0051920|GO:0008379
PubMed:  15518547|12517450|10644761|15558583
SCOP:  4000042

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 28-161 7.79e-52

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: 161.95  E-value: 7.79e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524  28 APAPAVTAPDEAGQPVHFADYYSKGVtLVYFYPKADTPGCTKEACSLRDSFDGLKARGLQILGVSEDQPDAQKKFRDKYH 107
Cdd:cd03017    1 DKAPDFTLPDQDGETVSLSDLRGKPV-VLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAEKYG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 494040524 108 LPFVLVADSDGAVAKAFGVPTF----LGFAKRQSFLV-KEGKIVWRDLSVSPGTHVAEV 161
Cdd:cd03017   80 LPFPLLSDPDGKLAKAYGVWGEkkkkYMGIERSTFLIdPDGKIVKVWRKVKPKGHAEEV 138
 
Name Accession Description Interval E-value
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 28-161 7.79e-52

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: 161.95  E-value: 7.79e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524  28 APAPAVTAPDEAGQPVHFADYYSKGVtLVYFYPKADTPGCTKEACSLRDSFDGLKARGLQILGVSEDQPDAQKKFRDKYH 107
Cdd:cd03017    1 DKAPDFTLPDQDGETVSLSDLRGKPV-VLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAEKYG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 494040524 108 LPFVLVADSDGAVAKAFGVPTF----LGFAKRQSFLV-KEGKIVWRDLSVSPGTHVAEV 161
Cdd:cd03017   80 LPFPLLSDPDGKLAKAYGVWGEkkkkYMGIERSTFLIdPDGKIVKVWRKVKPKGHAEEV 138
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
30-169 7.69e-39

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 128.83  E-value: 7.69e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524  30 APAVTAPDEAGQPVHFADYYSKGVtLVYFYpKADTPGCTKEACSLRDSFDGLKARGLQILGVSEDQPDAQKKFRDKYHLP 109
Cdd:COG1225    1 APDFTLPDLDGKTVSLSDLRGKPV-VLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFAEKYGLP 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494040524 110 FVLVADSDGAVAKAFGVptflgFAKRQSFLV-KEGKIVWRDLS-VSPGTHVAEV-NKALDTLK 169
Cdd:COG1225   79 FPLLSDPDGEVAKAYGV-----RGTPTTFLIdPDGKIRYVWVGpVDPRPHLEEVlEALLAELK 136
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 26-148 6.06e-37

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: 123.49  E-value: 6.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524   26 IGAPAPAVTAPDEAGQPVHFADYYSKGVtLVYFYPKADTPGCTKEACSLRDSFDGLKARGLQILGVSEDQPDAQKKFRDK 105
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDYRGKWV-VLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEK 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 494040524  106 YHLPFVLVADSDGAVAKAFGVP-TFLGFAKRQSFLV-KEGKIVWR 148
Cdd:pfam00578  80 YGLPFPLLSDPDGEVARAYGVLnEEEGGALRATFVIdPDGKVRYI 124
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 27-145 1.28e-36

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 123.89  E-value: 1.28e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524  27 GAPAPAVTAPDEAGQPVHFADYYSKGVtLVYFYPKADTPGCTKEACSLRDSFDGLKARGLQILGVSEDQPDAQKKFRDKY 106
Cdd:PRK09437   7 GDIAPKFSLPDQDGEQVSLTDFQGQRV-LVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDKPEKLSRFAEKE 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 494040524 107 HLPFVLVADSDGAVAKAFGV---PTFLGfaK------RQSFLVKE-GKI 145
Cdd:PRK09437  86 LLNFTLLSDEDHQVAEQFGVwgeKKFMG--KtydgihRISFLIDAdGKI 132
 
Name Accession Description Interval E-value
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 28-161 7.79e-52

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: 161.95  E-value: 7.79e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524  28 APAPAVTAPDEAGQPVHFADYYSKGVtLVYFYPKADTPGCTKEACSLRDSFDGLKARGLQILGVSEDQPDAQKKFRDKYH 107
Cdd:cd03017    1 DKAPDFTLPDQDGETVSLSDLRGKPV-VLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAEKYG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 494040524 108 LPFVLVADSDGAVAKAFGVPTF----LGFAKRQSFLV-KEGKIVWRDLSVSPGTHVAEV 161
Cdd:cd03017   80 LPFPLLSDPDGKLAKAYGVWGEkkkkYMGIERSTFLIdPDGKIVKVWRKVKPKGHAEEV 138
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 29-161 3.27e-39

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: 129.98  E-value: 3.27e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524  29 PAPAVTAPDEAGQPVHFADYYSKGVtLVYFYPKADTPGCTKEACSLRDSFDGLKARGLQILGVSEDQPDAQKKFRDKY-H 107
Cdd:cd02971    1 KAPDFTLPATDGGEVSLSDFKGKWV-VLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAWAEKEgG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 494040524 108 LPFVLVADSDGAVAKAFGVP----TFLGFAKRQSFLV-KEGKIVWRDLSVSPGTHVAEV 161
Cdd:cd02971   80 LNFPLLSDPDGEFAKAYGVLieksAGGGLAARATFIIdPDGKIRYVEVEPLPTGRNAEE 138
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
30-169 7.69e-39

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 128.83  E-value: 7.69e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524  30 APAVTAPDEAGQPVHFADYYSKGVtLVYFYpKADTPGCTKEACSLRDSFDGLKARGLQILGVSEDQPDAQKKFRDKYHLP 109
Cdd:COG1225    1 APDFTLPDLDGKTVSLSDLRGKPV-VLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFAEKYGLP 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494040524 110 FVLVADSDGAVAKAFGVptflgFAKRQSFLV-KEGKIVWRDLS-VSPGTHVAEV-NKALDTLK 169
Cdd:COG1225   79 FPLLSDPDGEVAKAYGV-----RGTPTTFLIdPDGKIRYVWVGpVDPRPHLEEVlEALLAELK 136
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 26-148 6.06e-37

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: 123.49  E-value: 6.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524   26 IGAPAPAVTAPDEAGQPVHFADYYSKGVtLVYFYPKADTPGCTKEACSLRDSFDGLKARGLQILGVSEDQPDAQKKFRDK 105
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDYRGKWV-VLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEK 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 494040524  106 YHLPFVLVADSDGAVAKAFGVP-TFLGFAKRQSFLV-KEGKIVWR 148
Cdd:pfam00578  80 YGLPFPLLSDPDGEVARAYGVLnEEEGGALRATFVIdPDGKVRYI 124
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 27-145 1.28e-36

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 123.89  E-value: 1.28e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524  27 GAPAPAVTAPDEAGQPVHFADYYSKGVtLVYFYPKADTPGCTKEACSLRDSFDGLKARGLQILGVSEDQPDAQKKFRDKY 106
Cdd:PRK09437   7 GDIAPKFSLPDQDGEQVSLTDFQGQRV-LVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDKPEKLSRFAEKE 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 494040524 107 HLPFVLVADSDGAVAKAFGV---PTFLGfaK------RQSFLVKE-GKI 145
Cdd:PRK09437  86 LLNFTLLSDEDHQVAEQFGVwgeKKFMG--KtydgihRISFLIDAdGKI 132
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 24-148 3.25e-30

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: 107.36  E-value: 3.25e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524  24 IDIGAPAPAVTAPDEAGQPVHFADYYSKGVTLVYFYPKADTPGCTKEACSLRDSFDGLKARGLQILGVSEDQPDAQKKFR 103
Cdd:cd03018    1 LEVGDKAPDFELPDQNGQEVRLSEFRGRKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLRAWA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 494040524 104 DKYHLPFVLVADS--DGAVAKAFGV-PTFLGFAKRQSFLV-KEGKIVWR 148
Cdd:cd03018   81 EENGLTFPLLSDFwpHGEVAKAYGVfDEDLGVAERAVFVIdRDGIIRYA 129
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 27-165 3.09e-23

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 89.35  E-value: 3.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524   27 GAPAPAVTAPDEA--GQPVHFADYYSKgVTLVYFYPKADTPGCTKEACSLRDSFDGLKARGLQILGVSEDQ-PDAQKKFR 103
Cdd:pfam08534   3 GDKAPDFTLPDAAtdGNTVSLSDFKGK-KVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNdAFFVKRFW 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494040524  104 DKYHLPFVLVADSDGAVAKAFGVPTFLGF-----AKRQSFLVKEGKIVWRDLSVSPGTHVAEVNKAL 165
Cdd:pfam08534  82 GKEGLPFPFLSDGNAAFTKALGLPIEEDAsaglrSPRYAVIDEDGKVVYLFVGPEPGVDVSDAEAVL 148
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 26-168 4.29e-17

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 73.19  E-value: 4.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524  26 IGAPAPAVTAPDEAGQPVHFADYySKGVTLVYFYpkADT-PGCTKEACSLRDSFDglKARGLQILGVS-EDQPDAQKKFR 103
Cdd:COG0526    4 VGKPAPDFTLTDLDGKPLSLADL-KGKPVLVNFW--ATWcPPCRAEMPVLKELAE--EYGGVVFVGVDvDENPEAVKAFL 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494040524 104 DKYHLPFVLVADSDGAVAKAFGV---PTFLgfakrqsFLVKEGKIVWRdlsVSPGTHVAEVNKALDTL 168
Cdd:COG0526   79 KELGLPYPVLLDPDGELAKAYGVrgiPTTV-------LIDKDGKIVAR---HVGPLSPEELEEALEKL 136
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
26-146 4.21e-14

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 66.64  E-value: 4.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524  26 IGAPAPAVTAP---DEAGQPVHFADYYSKGVtLVYFYPKADTPGCTKEACSLRDSFDGLKARGLQILGVSEDQPDAQKKF 102
Cdd:COG0450    5 IGDKAPDFTAEathGGEFKKISLSDYKGKWV-VLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHKAW 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 494040524 103 RD-------KYHLPFVLVADSDGAVAKAFGV-PTFLGFAKRQSFLV-KEGKIV 146
Cdd:COG0450   84 HEtikekggIVKIKFPIIADPTGKIARAYGMlHPEDGVAVRGVFIIdPDGKIR 136
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 32-148 5.36e-13

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: 61.87  E-value: 5.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524  32 AVTAPDEAGQPVHFADYYSKgVTLVYFYpkADT-PGCTKEACSLRDSFDGLKARGLQILGVSEDQPDAQ--KKFRDKYHL 108
Cdd:cd02966    1 DFSLPDLDGKPVSLSDLKGK-VVLVNFW--ASWcPPCRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAavKAFLKKYGI 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 494040524 109 PFVLVADSDGAVAKAFGV---PTflgfakrqSFLV-KEGKIVWR 148
Cdd:cd02966   78 TFPVLLDPDGELAKAYGVrglPT--------TFLIdRDGRIRAR 113
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 29-148 1.21e-12

Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two 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. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins.


Pssm-ID: 239268 [Multi-domain]  Cd Length: 149  Bit Score: 61.99  E-value: 1.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524  29 PAPAVTAPDEAGQPVHFADYYSKGVTLVYFYPKADTPGCTKEACSLRDSFDGLKARGLQILGVSEDQPDAQKKFRDKYHL 108
Cdd:cd02970    1 TAPDFELPDAGGETVTLSALLGEGPVVVVFYRGFGCPFCREYLRALSKLLPELDALGVELVAVGPESPEKLEAFDKGKFL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 494040524 109 PFVLVADSDGAVAKAFGVPTFLGFAKRQSFLVKEGKIVWR 148
Cdd:cd02970   81 PFPVYADPDRKLYRALGLVRSLPWSNTPRALWKNAAIGFR 120
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 26-169 7.72e-11

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: 57.51  E-value: 7.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524  26 IGAPAPAVTA----PDEAGQPVHFADYYSKGVtLVYFYPKADTPGCTKEACSLRDSFDGLKARGLQILGVSEDQPDAQKK 101
Cdd:cd03015    1 VGKKAPDFKAtavvPNGEFKEISLSDYKGKWV-VLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524 102 FRDKYH-------LPFVLVADSDGAVAKAFGVptfL----GFAKRQSFLV-KEGKIVW---RDLSVspGTHVAEVNKALD 166
Cdd:cd03015   80 WRNTPRkegglgkINFPLLADPKKKISRDYGV---LdeeeGVALRGTFIIdPEGIIRHitvNDLPV--GRSVDETLRVLD 154


                 ...
gi 494040524 167 TLK 169
Cdd:cd03015  155 ALQ 157
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
23-146 3.89e-09

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 53.08  E-value: 3.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524  23 AIDIGAPAPAVTAPDEAGQPVHFADYYSKGVTLvYFYPKADTPgCTKEACSLRDSFDGLKARGLQILGVSEDQPD-AQKK 101
Cdd:PRK03147  34 KVQVGKEAPNFVLTDLEGKKIELKDLKGKGVFL-NFWGTWCKP-CEKEMPYMNELYPKYKEKGVEIIAVNVDETElAVKN 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 494040524 102 FRDKYHLPFVLVADSDGAVAKAFGV---PTflgfakrqSFLV-KEGKIV 146
Cdd:PRK03147 112 FVNRYGLTFPVAIDKGRQVIDAYGVgplPT--------TFLIdKDGKVV 152
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 27-168 6.48e-09

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: 52.24  E-value: 6.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524  27 GAPAPAVTAPDEAGQPVHFADYYSKGVTLVYF------YPKADTPGCTKEAcslRDsfdgLKARGLQILGVS-------- 92
Cdd:cd02969    1 GSPAPDFSLPDTDGKTYSLADFADGKALVVMFicnhcpYVKAIEDRLNRLA---KE----YGAKGVAVVAINsndieayp 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524  93 EDQPDAQKKFRDKYHLPFVLVADSDGAVAKAFGV---PTFLGFAkrqsflvKEGKIVWR----DLSVSPGTHV--AEVNK 163
Cdd:cd02969   74 EDSPENMKAKAKEHGYPFPYLLDETQEVAKAYGAactPDFFLFD-------PDGKLVYRgridDSRPGNDPPVtgRDLRA 146


                 ....*
gi 494040524 164 ALDTL 168
Cdd:cd02969  147 ALDAL 151
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 46-145 2.39e-07

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 48.79  E-value: 2.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524  46 ADYYSKGVTLVYFYPKADTPGCTKEACSLRDSFDGLKARGLQILGVSEDQPDAQKKFRDK-------YHLPFVLVADSDG 118
Cdd:PTZ00137  93 SDYFKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSPFSHKAWKELdvrqggvSPLKFPLFSDISR 172

                         90       100
                 ....*....|....*....|....*...
gi 494040524 119 AVAKAFGVPTFLGFAKRQSFLV-KEGKI 145
Cdd:PTZ00137 173 EVSKSFGLLRDEGFSHRASVLVdKAGVV 200
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 26-125 1.78e-06

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: 45.99  E-value: 1.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524  26 IGAPAPAVTAPDEAGqPVHFADYYSKGVTLVYFYPKADTPGCTKEACSLRDSFDGLKARGLQILGVSEDQPDAQKK-FRD 104
Cdd:cd03016    1 LGDTAPNFEADTTHG-PIKFHDYLGDSWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKwIED 79

                         90       100
                 ....*....|....*....|....*.
gi 494040524 105 -----KYHLPFVLVADSDGAVAKAFG 125
Cdd:cd03016   80 ieeytGVEIPFPIIADPDREVAKLLG 105
PRK15000 PRK15000
peroxiredoxin C;
30-169 3.88e-06

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 45.05  E-value: 3.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524  30 APAVTAPDEAGQPVHFADYYSKGVTLVYFYPKADTPGCTKEACSLRDSFDGLKARGLQILGVSEDQPDAQKKFRDKY--- 106
Cdd:PRK15000  13 AAAVLGSGEIVDKFNFKQHTNGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVHNAWRNTPvdk 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524 107 ----HLPFVLVADSDGAVAKAFGVP-TFLGFAKRQSFLVKEGKIVWRDL--SVSPGTHVAEVNKALDTLK 169
Cdd:PRK15000  93 ggigPVKYAMVADVKREIQKAYGIEhPDEGVALRGSFLIDANGIVRHQVvnDLPLGRNIDEMLRMVDALQ 162
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 24-124 1.11e-05

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 43.69  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524  24 IDIGAPAPAVTAPDEAGqPVHFADYYSKGVtLVYFYPKADTPGCTKEACSLRDSFDGLKARGLQILGVSEDQ-------- 95
Cdd:PRK13190   2 VKLGQKAPDFTVNTTKG-PIDLSKYKGKWV-LLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSiyshiawl 79

                         90       100
                 ....*....|....*....|....*....
gi 494040524  96 PDAQKKFRDKyhLPFVLVADSDGAVAKAF 124
Cdd:PRK13190  80 RDIEERFGIK--IPFPVIADIDKELAREY 106
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 26-150 8.00e-05

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: 40.65  E-value: 8.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524  26 IGAPAPAVTAPDEAGQPVHFADYYSKgVTLVYFYPKADTPGCTKEACSLRDSFDGLKarGLQILGVSEDQPDAQKKFRDK 105
Cdd:cd03014    2 VGDKAPDFTLVTSDLSEVSLADFAGK-VKVISVFPSIDTPVCATQTKRFNKEAAKLD--NTVVLTISADLPFAQKRWCGA 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 494040524 106 YHLPFVLVAdSD---GAVAKAFGV--PTfLGFAKRQSFLVKE-GKIVWRDL 150
Cdd:cd03014   79 EGVDNVTTL-SDfrdHSFGKAYGVliKD-LGLLARAVFVIDEnGKVIYVEL 127
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 37-168 3.20e-03

Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441602  Cd Length: 156  Bit Score: 36.03  E-value: 3.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524  37 DEAGQPVHFADYYSKgVTLVYF-YPKadtpgCTkEACS-----LRDSFDGLKARG---LQILGVS----EDQPDAQKKFR 103
Cdd:COG1999    7 DQDGKPVTLADLRGK-PVLVFFgYTS-----CP-DVCPttlanLAQVQEALGEDGgddVQVLFISvdpeRDTPEVLKAYA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524 104 DKYHLP--FVLVADSDG--AVAKAFGVPtflgFAKRQS-----------FLV-KEGKIVwrdLSVSPGTHVAEVNKALDT 167
Cdd:COG1999   80 EAFGAPrwIGLTGDPEEiaALAKAFGVY----YEKVPDgdytfdhsaavYLVdPDGRLR---GYYPAGEDPEELAADLKA 152


                 .
gi 494040524 168 L 168
Cdd:COG1999  153 L 153
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 26-126 5.49e-03

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 35.98  E-value: 5.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040524  26 IGAPAPAVTAPDEAGQpVHFADYYsKGVTLVYF-YPKADTPGCTKEACSLRDSFDGLKARGLQILGVSEDQPDAQKKFRD 104
Cdd:PRK13191   9 IGEKFPEMEVITTHGK-IKLPDDY-KGRWFVLFsHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNISHIEWVM 86

                         90       100
                 ....*....|....*....|....*...
gi 494040524 105 ------KYHLPFVLVADSDGAVAKAFGV 126
Cdd:PRK13191  87 wieknlKVEVPFPIIADPMGNVAKRLGM 114
 
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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