1PPX,1TUM


Conserved Protein Domain Family
MutT_pyrophosphohydrolase

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cd03425: MutT_pyrophosphohydrolase 
Click on image for an interactive view with Cn3D
The MutT pyrophosphohydrolase is a prototypical Nudix hydrolase that catalyzes the hydrolysis of nucleoside and deoxynucleoside triphosphates (NTPs and dNTPs) by substitution at a beta-phosphorus to yield a nucleotide monophosphate (NMP) and inorganic pyrophosphate (PPi). This enzyme requires two divalent cations for activity; one coordinates the phosphoryl groups of the NTP/dNTP substrate, and the other coordinates to the enzyme. It also contains the Nudix motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as metal binding and catalytic site. MutT pyrophosphohydrolase is important in preventing errors in DNA replication by hydrolyzing mutagenic nucleotides such as 8-oxo-dGTP (a product of oxidative damage), which can mispair with template adenine during DNA replication, to guanine nucleotides.
Statistics
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PSSM-Id: 239517
View PSSM: cd03425
Aligned: 115 rows
Threshold Bit Score: 114.511
Threshold Setting Gi: 21623099
Created: 12-Sep-2005
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 11 residues -Click on image for an interactive view with Cn3D
Feature 1:active site [active site]
Evidence:
  • Structure:1TUM; Escherichia coli MutT binds AMPCPP (a non hydrolyzable substrate analog), Mg2+, and Co2+; defined at 3.5A contacts.
    View structure with Cn3D
  • Citation:PMID 9063868
  • Structure:1PPX_A; Escherichia coli MutT binds 8-Oxo-dGMP and Mg2+; defined at 3.5A contacts.
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1       # #                               ## #           #  ##                      #   
1PPX_A        4 LQIAVGIIRNEnNEIFITRRAadahmaNKLEFPGGKIEMGETPEQAVVRELQEEVGITPqhfsLFEKLEYEFpdRHITLW 83
1TUM          4 LQIAVGIIRNEnNEIFITRRAadahmaNKLEFPGGKIEMGETPEQAVVRELQEEVGITPqhfsLFEKLEYEFpdRHITLW 83
gi 35211432   3 KAIAIGIVCFA-GKVLIDRRPvdaalgGLWEFPGGKILPGETPEACVAREVLEEVGLTVtvgeLLAILEHDYsdFFVRIR 81
gi 46448110 236 LDVVSGVLVHE-GRIFVQRRPdtgvwaGFWEFPGGRIEPGETPEEAIIREFREETDFAVrptdKLAVIRHGYttYRVVLH 314
gi 71673691   6 KLIGVAVIWDEtGKILIDKRRlgdsfgGLWEFPGGKKEAGETIENCIKREVLEELGIEVavekHLITIEYNYseIRLILH 85
gi 72002893 251 QEIGIGLVFNQkGELLIDQRLenssmgGMWEFPGGKKIPNESIVKTIERELKEELGIVVnvgeKLLSFEHAYthKRLNFT 330
gi 78168021 213 QVIGIGVVINEaGDVLIDQRLeegllgGMWEFPGGKQEPDEPIEACIVRELMEELGIKVsvgeGLITVDHAYshKKLQFV 292
gi 78217664 233 IEVATGFLVHQ-GRIFIQKRPemgvwaGFWEFPGGCIEQGETAEEAVRREFMEETEFDVvpreKIAVVRHGYttYRATLH 311
gi 83816513 221 EDIAVGLVFDDnDRLLIQRRPdegllgGLWEFPGGKQEGDESMEAACRREVREELGVGMtdvePFYTLSHAYshFKITLH 300
gi 84519058 265 AVIGVGLILNKnQDVLIDQRLdegsmgGMWEFPGGKKEKDESIEMTIARELREELGVEVkvgkKLIEFDHSYthKKLHFI 344
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
Feature 1                            #                    #        
1PPX_A       84 FWLVERWEGEpw-------gkEGQPGEWMSLVGlnaddfppANEPVIAKLK 127
1TUM         84 FWLVERWEGEpw-------gkEGQPGEWMSLVGlnaddfppANEPVIAKLK 127
gi 35211432  82 AYLCHSESDAar-------aiACDAVEWVEPREldgytfpvANAPLIPLIQ 125
gi 46448110 315 CYLLHIDASSrsappehpvitAATDHRWATLADidaltlpaGHRKLADLLA 365
gi 71673691  86 VYHCRYLRGIpk-------aiECDEFRWVTLDEidrftfpeANEQIITALK 129
gi 72002893 331 VHICAWISGQpk-------plASQKLLWVSPDKlfdfpfpaANTKIISELH 374
gi 78168021 293 VHLCRWISGEpq-------plASQQVRWVRPEQlkdypfpaANGRIIEALL 336
gi 78217664 312 CYLLELRGGSdvp-----vlhAATESRWVRFAEldgytlpaGHRKLVDMMA 357
gi 83816513 301 AFRGRLADGPpe-------arEDQPFRWVTVDElddyafprANRRLIEELV 344
gi 84519058 345 VHLCELISGKpk-------plSSQEVRWVKLSDlqnypfpkANSYMISALK 388

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