Conserved Protein Domain Family
NAT_SF

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cd04301: NAT_SF 
Click on image for an interactive view with Cn3D
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate
NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.
Statistics
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PSSM-Id: 173926
View PSSM: cd04301
Aligned: 948 rows
Threshold Bit Score: 27.2401
Threshold Setting Gi: 15615892
Created: 12-Dec-2003
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
Coenzyme A
Conserved site includes 5 residues -Click on image for an interactive view with Cn3D
Feature 1:Coenzyme A binding pocket [chemical binding site]
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                       ###            ##                
1QSN_A        48 SMVILknk--qkVIGGICFRqykp---------------qrfAEVAfLAVTaneq---vrgyGTRLMNKFKDhmqk-qni 106
gi 9657803    77 EIYLGl-----aRVGVLRLSysn-----------------dvTFLRdFQILpefq---gcgiGSKCLELVVRhald-rqs 130
gi 55230524  442 FISFEdfe-ndvLVGFCRLRfpndpvrrelqdaaivrelhvyGNAVgVGQEgddedhqhkgyGKKLLEKAEVlard-agf 519
gi 83591891   68 YILFQdsg--arPVGFVILAglt----------------nphHAVElVRMIavrp---glgiGKAMMEAVIDhafsglga 126
gi 110280243  57 IQFVYdae--naLVGYVILIkywsne-----------yqgylLFIDeLYIVpdkr---slgyGRTCITLIEKtfh---di 117
gi 117920349  48 DILFEe-----kLVGVVRLSfdi-----------------eeCWLRdLQVDqsyq---nrgiGSIAIAEAERlake-hgs 101
gi 150390020  52 IGIVKledlklgFVGFVRLDne-------------------tLYLTaVYLLevyq---rqgyGKKIINTIEKeayk-egi 108
gi 186476134  57 NFILEvd---geRIGVLRITeeg-----------------dsLHIRdVQIAeghr---rrgaGTYLLDTSHRwara-rgl 112
gi 193214692  67 DQLFVdd----lFSGYCAYGpdge---------------pgtLKLHkLYLKpsvh---gfglGQKLLTHVRNyaqq-agf 123
gi 255534659  61 YFLLFne---neAVGFIGFEnhyk---------------astTKLHrLYLVpaak---gkgiGKAALTFLKKtvpe-sgd 118

                 ....*.
Feature 1              
1QSN_A       107 eYLLTY 112
gi 9657803   131 tKLVLR 136
gi 55230524  520 pKLAVI 525
gi 83591891  127 nRLWLD 132
gi 110280243 118 qALALE 123
gi 117920349 102 hILKLK 107
gi 150390020 109 kRVVLL 114
gi 186476134 113 sELQLR 118
gi 193214692 124 eRILLQ 129
gi 255534659 119 iKIILN 124

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