1HYU,1ZYP


Conserved Protein Domain Family
AhpF_NTD_N

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cd02974: AhpF_NTD_N 
Click on image for an interactive view with Cn3D
Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) family, N-terminal TRX-fold subdomain; AhpF is a homodimeric flavoenzyme which catalyzes the NADH-dependent reduction of the peroxiredoxin AhpC, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. AhpF contains an NTD forming two contiguous TRX-fold subdomain 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 N-terminal TRX-fold subdomain of AhpF NTD is redox inactive, but is proposed to contain an important residue that aids in the catalytic function of the redox-active CXXC motif contained in the C-terminal TRX-fold subdomain.
Statistics
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PSSM-Id: 239272
Aligned: 35 rows
Threshold Bit Score: 86.8629
Created: 8-Aug-2005
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
catalytic
Conserved site include 1 residue -Click on image for an interactive view with Cn3D
Feature 1:catalytic residue [active site]
Evidence:
  • Comment:The conserved glutamic acid residue in the N-terminal TRX-fold subdomain is proposed to be important in the catalytic activity of the N-terminal domain (NTD) of AhpF by acting as a proton sink during acid-base catalysis of the active site thiolate in a way similar to Asp26 of E. coli TRX. The active site thiolate is located in the C-terminal TRX-fold subdomain of AhpF NTD.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                                                       
1HYU_A        1 MLDTNMKTQLRAYLEKLTKPVELIATLDDs-AKSAEIKELLAEIAELs-DKVTFKEDNTlp----------vrKPSFLIT 68  Salmonella typhi...
NP_266494     2 ILDETLRAQLMPYMDLLENPIILKVDADLesENGKKIVEFTDELASLs-EMISKETAKLn------------rKTAFSIE 68  Lactococcus lact...
BAB80489    349 LLNDVLRAQLKGILSKIENEVTLVSIVDRsnTKSIELRDLVLDISDLg-EKINAKIFNRgenkeveekinadkYPIVALL 427 Clostridium perf...
NP_602775   336 FLDNELRQQLVAVVDRFENPVEIVVFKDPnnEESVNIENAVKDIASIspEKLKFSSYNEgenkeletkvkvtrTPTIAIL 415 Fusobacterium nu...
ZP_00063808 357 WFAKEIIQALQPIFDKLTQDVTLHQLTDDs-SKSHELSSFLEEFSQLs-SHLKFKMEPTsteles--kyhvhhMPNFRLL 432 Leuconostoc mese...
AAO77917      7 MLEPALKEQLKGIFAGLEADFTFDISVSAshESRAELLELLSDVAECs-DHITCMVNEGsg-----------lKFTIGKN 74  Bacteroides thet...
NP_816368   354 WFPESMRQQLSGIFAKLTKKVTLLQFLDAsdEKSLELQSFLTEFASLd-QKITLETILKdtepakellygiekMPSVVLL 432 Enterococcus fae...
AAQ65803      1 MLDKDTLAQVGSYFAQLKKSYTLRLNAHTshPSYNEAKEMLDGLASVs-DHVRAEYNAAdd-----------fRIDLLVD 68  Porphyromonas gi...
NP_969325     1 MLDSSLLEQLRSVFGSLENTVELVYENSSh-EDQKDLLDMLQSVASTs-DKITLTQNTSgt----------spMPQFRID 68  Bdellovibrio bac...
ZP_00560203 368 LLDDSLKEQLVPILERLENRIGLLAFLEGssGFSEELRSFLSEFAGLt-DKVEVEFLNRgedavrekeakitlFPAVAVL 446 Desulfitobacteri...
Feature 1                         #         
1HYU_A       69 npg-sqQGPRFAGSPLGHEFTSLVLALL 95  Salmonella typhimurium
NP_266494    69 re--gvSGVLFSGLPLGHELNSLVLALV 94  Lactococcus lactis subsp. lactis Il1403
BAB80489    428 denenySGIKFHGVPGGHELNSFILAIY 455 Clostridium perfringens str. 13
NP_602775   416 dkdgnyTGLKYSSLPSGHELNSFILGLY 443 Fusobacterium nucleatum subsp. nucleatum ATCC 25586
ZP_00063808 433 tdnnedTGIQFSGIPTGHELNSLVLALY 460 Leuconostoc mesenteroides subsp. mesenteroides ATCC 8293
AAO77917     75 gk---pTEITFRAIPNGHEFTSLLLAIL 99  Bacteroides thetaiotaomicron VPI-5482
NP_816368   433 daagnyTGIKFSGIPSGHEVNSLVLAVY 460 Enterococcus faecalis V583
AAQ65803     69 ga---dSGIGFRGIPGGHEFSSLLLAIL 93  Porphyromonas gingivalis W83
NP_969325    69 ykg-khTGIVFKGIPGGHEFTSLILAIL 95  Bdellovibrio bacteriovorus HD100
ZP_00560203 447 gpdgvyTGVQFHGIPGGHEINSFILALY 474 Desulfitobacterium hafniense DCB-2

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