Conserved Protein Domain Family
PDI_a_QSOX

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cd02992: PDI_a_QSOX 
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein containing an N-terminal redox active TRX domain, similar to that of PDI, and a small C-terminal flavin adenine dinucleotide (FAD)-binding domain homologous to the yeast ERV1p protein. QSOX oxidizes thiol groups to disulfides like PDI, however, unlike PDI, this oxidation is accompanied by the reduction of oxygen to hydrogen peroxide. QSOX is localized in high concentrations in cells with heavy secretory load and prefers peptides and proteins as substrates, not monothiols like glutathione. Inside the cell, QSOX is found in the endoplasmic reticulum and Golgi. The flow of reducing equivalents in a QSOX-catalyzed reaction goes from the dithiol substrate -> dithiol of the QSOX TRX domain -> dithiols of the QSOX ERV1p domain -> FAD -> oxygen.
Statistics
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PSSM-Id: 239290
Aligned: 18 rows
Threshold Bit Score: 140.481
Created: 8-Feb-2005
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
catalytic
Feature 1:catalytic residues [active site]
Evidence:
  • Comment:CXXC motif
  • Comment:The flow of reducing equivalents in the oxidation of the substrate goes from the dithiol substrate to the active site dithiol of the QSOX TRX domain, then to the dithiols of the QSOX ERV1p domain, then to FAD and finally to molecular oxygen.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                      #  #                                           
NP_502314  51 EPIMHLDQmTFNDTVFSdr----aFLVEFYADWCGHCRAFAPYFRQFANmv----rdWYPVVTVAVINCADSFNQAACRE 122 nematode
NP_508653  48 DPILELDVdTFSAAIYGsk---kaHFIEFYSSWCGACIGYAPTFKKFAKql----ekWAPLVQVTVVNCADDKNMPLCRE 120 nematode
NP_508419  34 DSVLQLDEaTFNDTIFGaqsgaagYLVEFYSDWCGHCRAFAPTYKNLAKdv----dgWQNIVKIAAINCADPVNEPVCRS 109 nematode
AAF55938   40 DNIHVVVGaSLKKILAEpa---mgKLVQFLNSYCGNCRRFAHTFRKMAVdl----qkWNRVLRIYAVDCARLENVKLCRD 112 fruit fly
AAF58400   49 DKVIRLSVdNFNATVLDqn---rgALVEFYNTYCGHCRRFAPTYKSVAEhl----lpWSEVLIVAAIDCAAEENNGICRN 121 fruit fly
AAN13954   32 DNVVQLDFaSFESGLSEpt---sgKLVQFFNGFCEESQNFIPAFKNLSRkl----ykWHRLLKVHVLDCGKDENDMICSI 104 fruit fly
CAC85331   61 DAVWVLDSgSVRGATANss---aaWLVQFYSSWCGHCIAYAPTWRALAGdv----rdWASAIRVAALDCMEEKNQAVCHD 133 human
AAF55939   40 DNVIMLDIeSLRPALNLkn----sKLVQFLNSFCGDCHRFAPVFKTLSRdl----ykWRRILRIYAVDCAQERNAQLCRE 111 fruit fly
EAL41780    7 DSVISLTAaNLKQRVFNqp---haSLVEFYNSYCGFCRRFAPIWKQLASdi----lgWQKLVHVTALDCSRDENNAICRE 79  Anopheles gambiae ...
AAF31025   41 DNAIELNAtNFDSVFQDspa--kyAVLEFFAHWCPACRNYKPHYEKVARlfngadavYPGVVLMTRVDCAIKMNVKLCDK 118 thale cress
Feature 1                                                  
NP_502314 123 NGVTYFPMMKYFARta--ttATQGKLFETPh---sAEQIRDALLR 162 nematode
NP_508653 121 HSVSSYPSLRYFKYns--hnKDDGMKYSGDky--dINKLAHDIAG 161 nematode
NP_508419 110 NGVRFFPLIKYFPRds--lnSTEGSQIKPYs---tVSEMRGQLTK 149 nematode
AAF55938  113 FRITLTPTIRYYPSkfqrirHGIGTDIETTi----PSEIADQLIE 153 fruit fly
AAF58400  122 YEVMGYPTLRYLGPgf--qpGPQHYGQSLHtq--dKNEIREILAG 162 fruit fly
AAN13954  105 YSIRKTPTLRYFPPsy--klAPDNLGTEIThr--nPKEIQSKLAL 145 fruit fly
CAC85331  134 YDIHFYPTFRYFKAft--keFTTGENFKGPdr--eLRTVRQTMID 174 human
AAF55939  112 FNIRQTPSLRFFGPdm--rkNDDVLGAVIPgq--dPEFISSTLAE 152 fruit fly
EAL41780   80 FEVMAYPTIRFFSPyyadgeQKIGEPVKEHdeqriIDRLVEYMQR 124 Anopheles gambiae str. PEST
AAF31025  119 FSINHYPMLFWAPPkrf-vgGSWGPKQEKNei-svVNEWRTADLL 161 thale cress

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