1QMV,1XVW,1PRX,1OC3,1PSQ,1NM3,1H4O,1XIY,1TP9,1QXH,1PSQ,1QXH,1XVQ,1Q98,1E2Y,1KYG,1QQ2,1UUL,1WE0,2BMX,1XCC,2CV4,1XXU


Conserved Protein Domain Family
PRX_family
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cd02971: PRX_family 
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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.
Links
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Statistics
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PSSM-Id: 239269
Aligned: 427 rows
Threshold Bit Score: 50.6244
Created: 7-Dec-2004
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
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catalytic triad
Conserved site includes 3 residues -Click on image for an interactive view with Cn3D
Feature 1:catalytic triad [active site]
Evidence:
  • Comment:Deprotonation of the catalytic cysteine thiol is facilitated by H-bonding with the threonine or serine hydroxyl group, and the positive charge of the arginine sidechain.
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Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
Feature 1                                            #  #                                       
1QMV_A       10 PAPDFKATAvvdgafKEVKLsdykgKYVVLFFYPLDFTFVXPTeIIAFSNRaedfrklgCEVLGVSVDSQFTHLAWINtp 89  human
NP_965009    22 EMPNFAVLNkn---nQEFTKsdllgKFSLISVVPDINTPVCSIqTKTFNKTmdk--fpeINFLTISTNTVEDQQTWCAae 96  Lactobacillus jo...
NP_757783    21 KAPDFCLAKldnfaiCDVSLedfgkKIKIISCFPSIDTGVCDMqTKKLFSEygn--nekIVLLNVSSDSLFAFNKWCLan 98  Mycoplasma penet...
NP_785797    22 QLPKFKVFTth---dEKIKTkdllgKPVLLSVMPDIDTRVCSIqTKKFNQQadk--yphVQFLAISNNAVADQAGWCAke 96  Lactobacillus pl...
YP_015976    24 KVTFKATSKt----lESVTIdk-leKITVLTIFPSISTSICDVqTSEMSKIase--ftnFNFVAISLDLPFTLKEWCGtk 96  Mycoplasma mobil...
NP_266460    22 DAPDFELTDlk---gNKIKLsk-leKPVLISVFPDINTRVCSLqTKHFNLEaak--hseIDFLSISNNTADEQKNWCAte 95  Lactococcus lact...
NP_816550    22 KAPVFSLKNln---nQEINLadykgKTVLISVVPDIDTRVCSLqTKRFNQEaak--ldgVQIITISNNTVEEQANWCAae 96  Enterococcus fae...
NP_326539    23 KLTFEATTTs----lENYEFdv-pgKLTVVSVFPAINTSVCDFqTQEISAIakky-gdkLQVLTISVDLPFTLNEWCAah 96  Mycoplasma pulmo...
YP_115796    22 KLEFSVSDTn----fDVVEFns-fgKTTLISVFPSINTKICDFqTVSIRDLsvk--ypqFRFISVSLDLPSAIAQWKDan 94  Mycoplasma hyopn...
ZP_00385080  22 QLPTFTVTNaq---aKPVTTqdlskRLTLISVVPDINTRVCSIsTKHFNEDmda--fdhTDFYTISTNTPQEQQSWCAae 96  Lactobacillus ca...

Feature 1                                               #                              
1QMV_A       90 rkegglgplNIPLLADVtr-rLSEDYGVLktde---giaYRGLFIIDgkGVLRQITVNdlp-vgrSVDEAL 155 human
NP_965009    97 d------vkNMQLMSDKnf-sFGKATGLLipes---gilARSVWVLDpnGKILYRELVdeithepNYDAVL 157 Lactobacillus johnsonii N...
NP_757783    99 e------aqNTVMLSDYrdhtFAKAYGVNikda---nliYRSIFIIDefNFVKYIQLSkgltdelDFVQIK 160 Mycoplasma penetrans HF-2
NP_785797    97 g------vkNLTVASDEel-sFGYATNLYlpnn---gtlTRAIYVADaaGKIVYHEIVpdvshepNYVAAL 157 Lactobacillus plantarum W...
YP_015976    97 n------vkNIEVLSDYrereFGKKYGFLiddl---fllSRGTIVLDksNKVIYIEQLkqvktqiDFEKLR 158 Mycoplasma mobile 163K
NP_266460    96 -------gvDMTILADDg--tFGKAYGLIlnggplegrlARSVFVVKn-GQIVYSEVLselsdepNYEKAL 156 Lactococcus lactis subsp....
NP_816550    97 -------gvEMEMLHDTed-sFGAAYGLYipem---grlARAIFVIDpeGTLVYEEIVsevssepDYQQAL 156 Enterococcus faecalis V583
NP_326539    97 g------vnNIVPLSDHkklvFGKRNGLLieel---gllARTVIITDekGIVKYIDINknvheqvDFDKFN 158 Mycoplasma pulmonis UAB CTIP
YP_115796    95 l------adNLEIYSDYrlrsFGLATGFLiedv---fllNRGYIIVDsgGRVLAVESNsdvhdqiDFVKLE 156 Mycoplasma hyopneumoniae 232
ZP_00385080  97 g------vkKMQLLSDQng-dFGKAMGLFvadn---htdARSVWIVDgtGTVKYRELIteqthepDYTSAL 157 Lactobacillus casei ATCC 334

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