1HYU,1ZYP


Conserved Protein Domain Family
AhpF_NTD_C

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cd03026: AhpF_NTD_C 
Click on image for an interactive view with Cn3D
TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) subfamily, C-terminal TRX-fold subdomain; AhpF is a homodimeric flavoenzyme which catalyzes the NADH-dependent reduction of the peroxiredoxin AhpC, which then reduces hydrogen peroxide and organic hydroperoxides. AhpF contains an NTD containing two contiguous TRX-fold subdomains similar to Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO). It also contains a catalytic core similar to TRX reductase containing FAD and NADH binding domains with an active site disulfide. The proposed mechanism of action of AhpF is similar to a TRX/TRX reductase system. The flow of reducing equivalents goes from NADH -> catalytic core of AhpF -> NTD of AhpF -> AhpC -> peroxide substrates. The catalytic CXXC motif of the NTD of AhpF is contained in its C-terminal TRX subdomain.
Statistics
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PSSM-Id: 239324
Aligned: 23 rows
Threshold Bit Score: 125.486
Created: 15-Mar-2005
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
catalytic
Conserved site includes 2 residues -Click on image for an interactive view with Cn3D
Feature 1:catalytic residues [active site]
Evidence:
  • Comment:CXXC motif
  • Comment:The N-terminal domain (NTD) of AhpF, which contains two contiguous TRX folds, mediates electron transfer from the catalytic core of AhpF to its substrate AhpC. The active site CXXC motif of AhpF NTD resides in its C-terminal TRX-fold subdomain.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                              #  #                                                     
1HYU_A      106 QSLLEQIRDIdgDFEFETYYSLSCHNCPDVVQALNLMAVLNPRIKHTAIDGGTFQNEITERNVMGVPAVFVNG----KEF 181 Salmonella typhi...
BAB80489    466 EGVLDEIKKLdkKTNIKVCVSLSCHLCPDVVVSAQRIAKENKNIEAEMIDLANFKDIKDEFKIMSVPALIVNN----KDV 541 Clostridium perf...
NP_602775   454 TESLEKIEKInkPVNIKIGISLSCTKCPKTVQATQRIATLNKNVEMEMINIFTFQDFKNRYDIMSVPAIIVDD----QHI 529 Fusobacterium nu...
ZP_00063808 471 TELVQRIQRLp-KTDLNIGVSLTCHFCPDVVAACQHIAAINDNVTAEMIDLQLFPELRESHHIMSVPAMIINNs---DNV 546 Leuconostoc mese...
NP_695801   543 DDLVERAKSItdPLNIMILVSLTCTMCPETVLASQRIASLSPAVRAEAYDVSHFPELKDQYGAMSVPCIVITHadgtQQV 622 Bifidobacterium ...
AAO77917    111 EAVCNRVKALkgPIHLVTYVSLTCTNCPDVVQALNAMTTLNPSITHEMVDGALYQDEVDALKIQGVPSVFADG----KLL 186 Bacteroides thet...
AAQ65803    105 EGVQDRIRRIngPIELKTYVSLSCTNCPDVVQTLNMIAILNPTINHTMVDGSFFPDEVESLGIASVPTVMAGD----EVI 180 Porphyromonas gi...
NP_969325   106 SVIADRVRRLnkNITIQSYISLTCENCPEVVQALNQIALIHGSLRHEIIDGGYVQDDIKTLGIQGVPSLVANA----KMF 181 Bdellovibrio bac...
ZP_00375687 106 QDVLEQIRALegPLDFEMFFSLSCHNCPDVVQALTLMALENPNISATLIEGGTFQDEVDRRDVMAVPATFLNG----EPF 181 Erythrobacter li...
ZP_00560203 485 EETLAKIRRVsrKVNFKIGVSLSCTLCPDVVTLAQLMALKNPLIEAEMIDVAHYPDFKNKYGIMSVPAIVVND----EKV 560 Desulfitobacteri...
Feature 1                       
1HYU_A      182 GQGRMt---LTEIVAK 194 Salmonella typhimurium
BAB80489    542 YFGSKk---IEEILEI 554 Clostridium perfringens str. 13
NP_602775   530 YFGEKtvedMLEIINK 545 Fusobacterium nucleatum subsp. nucleatum ATCC 25586
ZP_00063808 547 IFGSQs---LEEIVSA 559 Leuconostoc mesenteroides subsp. mesenteroides ATCC 8293
NP_695801   623 EFGKKsipqMLELVGA 638 Bifidobacterium longum NCC2705
AAO77917    187 HVGRGe---FGELLAK 199 Bacteroides thetaiotaomicron VPI-5482
AAQ65803    181 HVGRGd---MAALLNK 193 Porphyromonas gingivalis W83
NP_969325   182 HSGRIq---LLDLVSK 194 Bdellovibrio bacteriovorus HD100
ZP_00375687 182 FNGKMs---LEEVLAK 194 Erythrobacter litoralis HTCC2594
ZP_00560203 561 VFGKKn---LEELLEL 573 Desulfitobacterium hafniense DCB-2

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