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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812636  67 DPIPDLSLLNEDNDSISLKKITeNNRVVVFFvYPRASTPGCTRQACGFRDNYQELKKY-AAVFGLSADSVTSQKKFQSKQ 145
Cdd:cd03017    1 DKAPDFTLPDQDGETVSLSDLR-GKPVVLYF-YPKDDTPGCTKEACDFRDLYEEFKALgAVVIGVSPDSVESHAKFAEKY 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 285812636 146 NLPYHLLSDPKREFIGLLGA---KKTPLSGSIRSHFIFV-DGKLKFKRVKISPEVSVndakKEVLE 207
Cdd:cd03017   79 GLPFPLLSDPDGKLAKAYGVwgeKKKKYMGIERSTFLIDpDGKIVKVWRKVKPKGHA----EEVLE 140

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812636  67 DPIPDLSLLNEDNDSISLKKITeNNRVVVFFvYPRASTPGCTRQACGFRDNYQELKKY-AAVFGLSADSVTSQKKFQSKQ 145
Cdd:cd03017    1 DKAPDFTLPDQDGETVSLSDLR-GKPVVLYF-YPKDDTPGCTKEACDFRDLYEEFKALgAVVIGVSPDSVESHAKFAEKY 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 285812636 146 NLPYHLLSDPKREFIGLLGA---KKTPLSGSIRSHFIFV-DGKLKFKRVKISPEVSVndakKEVLE 207
Cdd:cd03017   79 GLPFPLLSDPDGKLAKAYGVwgeKKKKYMGIERSTFLIDpDGKIVKVWRKVKPKGHA----EEVLE 140

thioredoxin-dependent thiol peroxidase; Reviewed

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812636  61 NELEIGDPIPDLSLLNEDNDSISLKKITeNNRVVVFFvYPRASTPGCTRQACGFRDNYQELKKY-AAVFGLSADSVTSQK 139
Cdd:PRK09437   2 NPLKAGDIAPKFSLPDQDGEQVSLTDFQ-GQRVLVYF-YPKAMTPGCTVQACGLRDNMDELKKAgVVVLGISTDKPEKLS 79

                         90       100       110
                 ....*....|....*....|....*....|.
gi 285812636 140 KFQSKQNLPYHLLSDPKR---EFIGLLGAKK 167
Cdd:PRK09437  80 RFAEKELLNFTLLSDEDHqvaEQFGVWGEKK 110

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812636  67 DPIPDLSLLNEDNDSISLKKITeNNRVVVFFvYPRASTPGCTRQACGFRDNYQELKKY-AAVFGLSADSVTSQKKFQSKQ 145
Cdd:cd03017    1 DKAPDFTLPDQDGETVSLSDLR-GKPVVLYF-YPKDDTPGCTKEACDFRDLYEEFKALgAVVIGVSPDSVESHAKFAEKY 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 285812636 146 NLPYHLLSDPKREFIGLLGA---KKTPLSGSIRSHFIFV-DGKLKFKRVKISPEVSVndakKEVLE 207
Cdd:cd03017   79 GLPFPLLSDPDGKLAKAYGVwgeKKKKYMGIERSTFLIDpDGKIVKVWRKVKPKGHA----EEVLE 140

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812636  68 PIPDLSLLNEDNDSISLKKitENNRVVVFFVYPRASTPGCTRQACGFRDNYQELKK-YAAVFGLSADSVTSQKKFQSKQ- 145
Cdd:cd02971    1 KAPDFTLPATDGGEVSLSD--FKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKgGAEVLGVSVDSPFSHKAWAEKEg 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812636 146 NLPYHLLSDPKREF---IGLLGAKKTPLSGSIRSHFIFV-DGKLKFKRVKISPEVSVNDA 201
Cdd:cd02971   79 GLNFPLLSDPDGEFakaYGVLIEKSAGGGLAARATFIIDpDGKIRYVEVEPLPTGRNAEE 138

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812636  69 IPDLSLLNEDNDSISLKKITENNRVVVFFvypRASTPGCTRQACGFRDNYQELKKY-AAVFGLSADSVTSQKKFQSKQNL 147
Cdd:COG1225    1 APDFTLPDLDGKTVSLSDLRGKPVVLYFY---ATWCPGCTAELPELRDLYEEFKDKgVEVLGVSSDSDEAHKKFAEKYGL 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 285812636 148 PYHLLSDPKREFIGLLGAKKTPlsgsirsHFIFVD--GKLKFKRV-KISPEVSVNDAKKEVLE 207
Cdd:COG1225   78 PFPLLSDPDGEVAKAYGVRGTP-------TTFLIDpdGKIRYVWVgPVDPRPHLEEVLEALLA 133

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812636   66 GDPIPDLSL--LNEDNDSISLKKitENNRVVVFFVYPRASTPGCTRQACGFRDNYQELK-KYAAVFGLSADSVT-SQKKF 141
Cdd:pfam08534   3 GDKAPDFTLpdAATDGNTVSLSD--FKGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKeKGVDVVAVNSDNDAfFVKRF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 285812636  142 QSKQNLPYHLLSDPKREF---IGLLGAKKTPLSGSIRSHFIFV-DGKLKFKRVKISPEVSVNDAKK 203
Cdd:pfam08534  81 WGKEGLPFPFLSDGNAAFtkaLGLPIEEDASAGLRSPRYAVIDeDGKVVYLFVGPEPGVDVSDAEA 146

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812636  68 PIPDLSLLNEDNDSISLKKITENNRVVVFFvYPRASTPGCTRQACGFRDNYQELKKY-AAVFGLSADSVTSQKKFQSKQN 146
Cdd:cd02970    1 TAPDFELPDAGGETVTLSALLGEGPVVVVF-YRGFGCPFCREYLRALSKLLPELDALgVELVAVGPESPEKLEAFDKGKF 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 285812636 147 LPYHLLSDPKREFIGLLGAKKTPLSGSIRSHF 178
Cdd:cd02970   80 LPFPVYADPDRKLYRALGLVRSLPWSNTPRAL 111

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812636  65 IGDPIPDLSLLNEDND---SISLKKITENNRVVVFFVyPRASTPGCTRQAC-GFRDNYQELKK--YAAVFGLSADS--VT 136
Cdd:cd03013    1 VGDKLPNVTLFEYVPGppnPVNLSELFKGKKVVIFGV-PGAFTPTCSAQHLpGYVENADELKAkgVDEVICVSVNDpfVM 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 285812636 137 SQ--KKFQSKQNLpyHLLSDPKREF---IGLLgAKKTPLSGSIRSH---FIFVDGKLKF 187
Cdd:cd03013   80 KAwgKALGAKDKI--RFLADGNGEFtkaLGLT-LDLSAAGGGIRSKryaLIVDDGKVKY 135

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812636  65 IGDPIPDLSLLNEDNDSIsLKKITEN---NRVVVFFVYPRASTPGCTRQACGFRDNYQELKKY-AAVFGLSADSVTSQKK 140
Cdd:cd03015    1 VGKKAPDFKATAVVPNGE-FKEISLSdykGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLnAEVLGVSTDSHFSHLA 79

                         90       100
                 ....*....|....*....|....*
gi 285812636 141 FQS---KQ----NLPYHLLSDPKRE 158
Cdd:cd03015   80 WRNtprKEgglgKINFPLLADPKKK 104

putative peroxiredoxin; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812636  65 IGDPIPDLSLlNEDNDSISLKKitENNRVVVFFVYPRASTPGCTRQACGFRDNYQELKKYAA-VFGLSADSVTS------ 137
Cdd:PRK13190   4 LGQKAPDFTV-NTTKGPIDLSK--YKGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVeLVGLSVDSIYShiawlr 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 285812636 138 --QKKFQSKqnLPYHLLSDPKREFIGLLGAKKTPLSGSIRSHFI 179
Cdd:PRK13190  81 diEERFGIK--IPFPVIADIDKELAREYNLIDENSGATVRGVFI 122