Conserved Protein Domain Family
VKOR_5

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cd12922: VKOR_5 
Vitamin K epoxide reductase family in bacteria
This family includes vitamin K epoxide reductase (VKOR) mostly present in actinobacteria. VKOR (also named VKORC1) is an integral membrane protein that catalyzes the reduction of vitamin K 2,3-epoxide and vitamin K to vitamin K hydroquinone, an essential co-factor subsequently used in the gamma-carboxylation of glutamic acid residues in blood coagulation enzymes. All homologs of VKOR contain an active site CXXC motif, which is switched between reduced and disulfide-bonded states during the reaction cycle. In some bacterial homologs, the VKOR domain is fused with domains of the thioredoxin family of oxidoreductases which may function as redox partners in initiating the reduction cascade.
Statistics
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PSSM-Id: 240605
Aligned: 63 rows
Threshold Bit Score: 128.469
Created: 22-Jul-2011
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
putative activeredox center
Feature 1:putative active site [active site]
Evidence:
  • Comment:four cysteines and one serine or threonine are inferred to be the active center

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                         #       #     #                                
Q8FLG3        35 LILLVTGIIGWVASGILVLERLALyedaehvttCDINalVSCGKVMGTWQSEl-FGFPNPLIGIVAFAVVITTAMamLAG 113 Corynebacterium...
ACQ79975      58 WLLVVAGVLGTLAAAMLTIDYVNTlldptyvptCDVNplIGCGQFLGSPQARv-FGFPNVVIGLVAFPVLVTTGLafLAG 136 Beutenbergia ca...
EFL15110      36 LLLLAGGLIGALASGILAYDRIRTledplftpgCNINavLSCGNVMTAWQSHl-LGPPNALLGLPAFAALAGLGLavAAG 114 Streptomyces sp. C
EGQ73354      67 WLLIIGSLIGIAACWELMTSELRLirqplanlsCDINplVSCGDSLNVWQGNl-LGVPNSFIGAMAFAVLLFVGAllACG 145 Actinomyces sp....
AEG44739      34 VLLTVLGAIGLAASAWLSVERYLTlldpdrvatCSINvfLSCGAAMGSWQGSl-FGFPNPFLGLATFPVVVTTGVviLTG 112 Isoptericola va...
ADH92722      46 WLVTICGAIGVWAAISLLVAEKQKllhpdsvlpCDINplVGCGKWVGTWQNEvfFGVSNSVYGLAFFAGIVALGLalVSG 125 Arcanobacterium...
EFG48023      35 AYMVVLSVIGLIASFDLSIEKIKKlespdyilsCDMNpfFSCSGVMQFPQSQl-FGFPNQLLGIAAFVFPLLLGVllISR 113 Brevibacterium ...
ZP_05914639   30 IFLVVTSVVGFLASFALAVEKYEKlenpnavlsCDLNpfFSCGSVMEYPESQl-FGFPNQLLGIAAFIFPLLLGVllLAG 108 Brevibacterium ...
YP_003718949 107 VLLIVLTFIAMAASAELVLSEIQTlkhpaehlgCDLNplIGCSASLTTWQAHllFGIPNALVGVGLFAGLAGVFLa-WCS 185 Mobiluncus curt...
EHM89206      39 LGMGLASLVALAVSWELIAAEMAQlknpltqlsCDINplVSCGASLTIWQGNl-LGVPNAFVGAMAYSAFVVLAAliGAQ 117 Actinomyces sp....
Feature 1                                            #  #              
Q8FLG3       114 ARFADWYWggLQAGVSVGLLFIIWLWYQALFvIHILCLYCMVVWAMMIPLFILL 167 Corynebacterium efficiens
ACQ79975     137 ARLARWYWwgLLAGCLAGAVFITWLQVQSLNvIKGLCPYCLVVWAVVIPVVVQT 190 Beutenbergia cavernae DSM 12333
EFL15110     115 ARLPRRLWqgLWAALAAGSALTLWLIGQCLYvIGALCPWCTAVWAVMIPLFWYV 168 Streptomyces sp. C
EGQ73354     146 QRLPRWVWwgLTAGTVIGIGFVVWFLTVSILaFGKLCPFCMVIWAVTIPIAALT 199 Actinomyces sp. oral taxon 448 str. F0400
AEG44739     113 ARLPRWYLnaLLAGTALGQLLIFFLMWTSFYvLHKLCPACMVVWTIMWPLLWFQ 166 Isoptericola variabilis 225
ADH92722     126 ARFARWLWcvLAAALSAGMLWIAWFMYESFAvEGSLCPYCLVTWFVTITLFAHT 179 Arcanobacterium haemolyticum DSM 20595
EFG48023     114 VRIPSWVMvgLNIGLLGGMALVVFLYISSIWvIGIGCPWCIVVWTITIPLFCTT 167 Brevibacterium mcbrellneri ATCC 49030
ZP_05914639  109 ARIPGWVMvgLNVGLALGTTLVMFLFYISIYkIGVGCPWCMVVWTMTIPMFVSV 162 Brevibacterium linens BL2
YP_003718949 186 GQIPRWLGvlIEAGLTGGMVLIAFFLHQSIFeFTKLCPFCFIVWTCTIILWVQL 239 Mobiluncus curtisii ATCC 43063
EHM89206     118 VKLPRWIWqgLAAGAVVNLGFVLWFVSQSVWvLNKLCPWCMVLWAATIPMAWTL 171 Actinomyces sp. C83

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