1VK6,2GB5,5IW4,5ISY


Conserved Protein Domain Family
NUDIX_NADH_pyrophosphatase_Nudt13

?
cd03429: NUDIX_NADH_pyrophosphatase_Nudt13 
NADH pyrophosphatase
NADH pyrophosphatase, also known as NUDIX (nucleoside diphosphate linked moiety X)) motif 13/Nudt13, is thought to have NADH pyrophosphatase activity, be involved in NADH metabolic process and NADP catabolic process, catalyzing the cleavage of NADH into reduced nicotinamide mononucleotide (NMNH) and AMP, and located in mitochondrion. 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
?
PSSM-Id: 467535
Aligned: 154 rows
Threshold Bit Score: 106.419
Created: 13-Sep-2005
Updated: 27-Apr-2023
Structure
?
Program:
Drawing:
Aligned Rows:
 
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
Feature 1:putative NAD binding site [chemical binding site]
Evidence:
  • Structure:1VK6: Escherichia coli NADH pyrophosphatase binds inhibitor 2-methyl-2,4-pentanediol, contacts at 5A
  • Comment:residues supported by substrate binding sites in other members of the family
  • Citation:PMID 9063868

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
Feature 1       #                                 ###                                 #  # # #
1VK6_A    140 APCIIVAIRRd--DSILLAQHtrh----rngVHTVLAGFVEVGETLEQAVAREVXEESGIKVkNLRYVTSQPWPFPQSLX 213 Escherichia coli
ADB46437   39 YSCIIILLCNe-qDEVVLCKQphl----sqeYESITSGFIMPGETAEETAHREVREELGLTLeRMIPEGTYWFSKGQMLM 113 Acidaminococcus fe...
EGN37884   39 STCIIALVVNe-yGEAALLRQgyi----shqYYNLVSGYMKPGETAEYTAAREVEEEIGVPVeKLRFVGTYWFGKKDMLM 113 Lachnospiraceae ba...
CBK96633   39 YNCVIVLARRg--DKYALIRQhsgdgsisedRFVCVSGYIMTNETAEQAAVREVTEELGLKPvKVRLVATYAYQKKQMLM 116 Eubacterium siraeu...
EFQ05326   39 NVAVSMIVVDeetGKILLIQQyg------ksSYILVAGYVNRGEAEEHAAVREVREETGLEVeHLRFNRTKFFEPSNTLM 112 Faecalibacterium c...
CBK81973   38 NTAVSMICIDvknQKILLIKQyg------rpDYILVAGYISRGEDAEAAVKREVFEETGMTVdRLQFNKTSFFEPSNTLM 111 Coprococcus catus ...
EFV02466   42 NTAVSMIVLNehkDQVLLIKQyg------rdAYILVAGYVSRGEDVEVTVRREVMEEMGLEVkALRFNHSHFFEPTNTLM 115 Pseudoramibacter a...
EHO80658   37 NTAVSLVALSpdeKQILLIQQyg------eqRNVLVAGYVNQKESVEDAVCREMTEEIGRRVvAYRYLKSEYFEKTNTLM 110 Eubacterium sp. 3_...
EFR37786   37 STAISMVTLNpkrDKILMIQQyg------kpNNILVAGYVNKEECAEDAMIREMQEEIGRKVlEYRFLRSEYFPKTNTLI 110 Clostridium sp. HGF2
EEF93986   37 NSAVSALVLNpkkDKILLIQQyg------rkDNILIAGYVTKGENAKQALFREIKEETGLTIsSYEFNDNEYYARTNTYI 110 Catenibacterium mi...
Feature 1                                                         
1VK6_A    214 TAFXAEYds-gDIVIDPKELLEANWYRYddlpll---pppgtVARRLIEDTV 261 Escherichia coli
ADB46437  114 HGFLGFVr--kQPFRLSQEVTSAHWVPIldlpqtaypetpenVIYPLWRKLL 163 Acidaminococcus fermentans DSM 20731
EGN37884  114 IGFIAEAk--kRELKLSGEVDAAEWVDAsraidm--vhpggsVSYALLEYYL 161 Lachnospiraceae bacterium 3_1_57FAA_CT1
CBK96633  117 TGFLAELp--eGDFSLSDELIAAQWFDEsevgvr---ladssVAKLLFNDIK 163 Eubacterium siraeum 70/3
EFQ05326  113 CNFTAFVrt-aKALHINHEVDRCKWFTPqearen---irpnsLAAEFLNVYL 160 Faecalibacterium cf. prausnitzii KLE1255
CBK81973  112 VNFACMIeh-pEDLKVNEEVDNFKWFAFdearan---ikknsLAERFLLHYL 159 Coprococcus catus GD/7
EFV02466  116 LNFTVVVg--gEKPRPNWEIDDYDWFSIaearkn---ilspsLAKDFLVGYL 162 Pseudoramibacter alactolyticus ATCC 23263
EHO80658  111 LSFAVLLdstsLADISDWEIDEAKWYSFdealka---iapasLAQRFLLNFI 159 Eubacterium sp. 3_1_31
EFR37786  111 FNFAVVIdsecLENVSTWEVDRAAWFTFdearas---vkpasLAQRFLLNFL 159 Clostridium sp. HGF2
EEF93986  111 NNYIVVVe--dESFHCNEEVDYAKWYDLkdamni---ikpdsLAQELLRRYL 157 Catenibacterium mitsuokai DSM 15897

| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap