1VK6


Conserved Protein Domain Family
NADH_pyrophosphatase

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cd03429: NADH_pyrophosphatase 
Click on image for an interactive view with Cn3D
NADH pyrophosphatase, a member of the Nudix hydrolase superfamily, catalyzes the cleavage of NADH into reduced nicotinamide mononucleotide (NMNH) and AMP. Like other members of the Nudix family, it requires a divalent cation, such as Mg2+ or Mn2+, for activity. Members of this family are also recognized by the Nudix motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as a metal binding and catalytic site. A block of 8 conserved amino acids downstream of the nudix motif is thought to give NADH pyrophosphatase its specificity for NADH. NADH pyrophosphatase forms a dimer.
Statistics
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PSSM-Id: 239521
View PSSM: cd03429
Aligned: 85 rows
Threshold Bit Score: 118.023
Threshold Setting Gi: 68128356
Created: 13-Sep-2005
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
Feature 1:putative NADH binding site [chemical binding site]
Evidence:
  • Structure:1VK6; E. coli NADH pyrophosphatase binds inhibitor 2-methyl-2,4-pentanediol; defined at 5A contacts.
    View structure with Cn3D
  • Comment:residues supported by substrate binding sites in other members of the family
  • Citation:PMID 9063868

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1        #                                 ###                                  #  #  # 
1VK6_A      141 PCIIVAIRRd------DSILLAQHtrhrngVHTVLAGFVEVGETLEQAVAREVXEESGIKV-KNLRYVTSQPWPFP-QSL 212
gi 18144253  18 PCIVVAVIKg-----dEIILLKQSyiy-enSKVLISGYVGVDECAEETVYREVKEETGITV-KDIKYLGSDFVKGK-ELL 89
gi 62516466  24 PVFSVAVSMivmneggDQVLLIKQyw--kdSYILVAGYVNKGENAEDSCRRELMEELHLTA-KSLHFNRSQYFAPS-NTL 99
gi 24379306  38 LAVSMIVYDeq----mQKILLIQQyh--mrQYILVAGYVNKGEKLEEAVKREVLEETCLTV-EIIAFNASSFYEKN-QVL 109
gi 15022972  40 PCVLVAVIKg-----qEILLLKQEytf-kdSKILVSGYVANGETVEETVVREVKEEVGIIV-EKPEYLGSYYFKPK-ELI 111
gi 68128356 177 PAVLVAVLDgk----gNVILSQRRke--skVLTLLSGFVLHGESAEETVRREVEEESGARV-SKVRYIGSQPWPYP-YLM 248
gi 11527981 186 PVSITLITDpt----nEHALLVRHrgsaggVFTAVAGFAHSGESMAECARREIAEEVGIEVdSIRSLDMSQPWPMPdSSL 261
gi 33284852 127 PVVIVLVSDg------SRCLLARQamfppgMYSALSGFCDMGESVEEALHREVAEEVGLEV-ENLQYSGSQHWPFPqSSF 199
gi 72016605 385 PIVITLVTNg------DRCLVARQpqfpigMYSALAGFCDMGETLEDTVRREVAEEVGLEV-EDITYCFSQHWPIPsSGL 457
gi 50593112 200 PVAITLVSDg------TRCLLARQssfpkgMYSALAGFCDIGESVEETIRREVAEEVGLEV-ESLQYYASQHWPFPsGSL 272
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
Feature 1       #                                                                              
1VK6_A      213 XTAFXAEYds--gDIVIDPKELLEANWYRYdd--------------------------lpLLPPPGTVARRLIEDTVAX 263
gi 18144253  90 MLTYLAYYe---sGEIEKSTEVEGAAWYNIed--------------------------alCELNEDSIGKRVVKKVLKE 139
gi 62516466 100 MLNYTVTVdq--aEKVSPNEEIDAWNWLSIde--------------------------arRQIRPNSLARTFLLEYLNK 150
gi 24379306 110 MVNFVCRAkk--aSDLKLNHEVEAANWFHPdq--------------------------akEAILSPSLAKNFLLNWLDK 160
gi 15022972 112 MLTFMVRYv---sGEITKSQEVDEAYWVNMrd--------------------------vlQEMNEDKVGKDVVKKVFKR 161
gi 68128356 249 MMCYYAVAda-spSLVVDASELERVMWVSKqdvrral----------------egqhsdmELRGPGTTPYAMLKPWVDG 310
gi 11527981 262 MIAHVAVAki-dqKISVCPDELETAQWFTRhqvkealtttladpllknlprtlddrqtlhYIPPAGAIAHQMIRQWVDG 339
gi 33284852 200 MLACHATVnpnktQVNIDKAELEDARWFTLeeittalqnpp---------rnpreqppvfWVPPSYAIANQLIREWANQ 269
gi 72016605 458 MLGCYATVke-ddQILIDRNELEDAKWMDReevqsilq--------------qspgqgsqWFPPRYAIAHQLIAGWAFK 521
gi 50593112 273 MIACHATVkpgqtEIQVNLRELETAAWFSHdevatalkrkgp-------ytqqqngtfpfWLPPKLAISHQLIKEWVEK 344

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