1QSN,1BO4,1FY7,1GHE,1I1D,1IB1,1LRZ,1LRZ,1M4I,1MK4,1N71,1OZP,1OZP,1RO5,1RXT,1RXT,1S3Z,1S7N,1SQH,1SQH,1TIQ,1U6M,1UFH,1VHS,1VKC,1WWZ,1XEB,1Y9K,1Y9W,1YK3,1YLE,1YX0,1Z4E,1ZO0,2AE6,2AJ6,2ATR,2CXA,2CY2,2D4P,2DXQ,2EUI,2FE7,2FIA,2FIW,2FL4,2GAN,2GE3,2HV2,2HV2,2I79,2JDC,2KCW,2OZG,2OZG,2OZH,2Q44,2R8V,2REE,2VI7,3C26,3DDD,3EC4,3FNC,3FRM,3FYN,3G8W,3H4Q


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
Aligned: 948 rows
Threshold Bit Score: 28.7809
Created: 12-Dec-2003
Updated: 2-Oct-2020
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:
Feature 1                                                       ###            ##                
1QSN_A        48 SMVILknk--qkVIGGICFRqykp---------------qrfAEVAfLAVTaneq---vrgyGTRLMNKFKDhmqk-qni 106 Tetrahymena the...
AAF96308      77 EIYLGl-----aRVGVLRLSysn-----------------dvTFLRdFQILpefq---gcgiGSKCLELVVRhald-rqs 130 Vibrio cholerae...
AAV45943     442 FISFEdfe-ndvLVGFCRLRfpndpvrrelqdaaivrelhvyGNAVgVGQEgddedhqhkgyGKKLLEKAEVlard-agf 519 Haloarcula mari...
YP_425643     68 YILFQdsg--arPVGFVILAglt----------------nphHAVElVRMIavrp---glgiGKAMMEAVIDhafsglga 126 Rhodospirillum ...
ABG58429      57 IQFVYdae--naLVGYVILIkywsne-----------yqgylLFIDeLYIVpdkr---slgyGRTCITLIEKtfh---di 117 Cytophaga hutch...
YP_869541     48 DILFEe-----kLVGVVRLSfdi-----------------eeCWLRdLQVDqsyq---nrgiGSIAIAEAERlake-hgs 101 Shewanella sp. ...
YP_001320069  52 IGIVKledlklgFVGFVRLDne-------------------tLYLTaVYLLevyq---rqgyGKKIINTIEKeayk-egi 108 Alkaliphilus me...
YP_001857604  57 NFILEvd---geRIGVLRITeeg-----------------dsLHIRdVQIAeghr---rrgaGTYLLDTSHRwara-rgl 112 Burkholderia ph...
YP_001995891  67 DQLFVdd----lFSGYCAYGpdge---------------pgtLKLHkLYLKpsvh---gfglGQKLLTHVRNyaqq-agf 123 Chloroherpeton ...
YP_003095030  61 YFLLFne---neAVGFIGFEnhyk---------------astTKLHrLYLVpaak---gkgiGKAALTFLKKtvpe-sgd 118 Flavobacteriace...
Feature 1              
1QSN_A       107 eYLLTY 112 Tetrahymena thermophila
AAF96308     131 tKLVLR 136 Vibrio cholerae O1 biovar eltor str. N16961
AAV45943     520 pKLAVI 525 Haloarcula marismortui ATCC 43049
YP_425643    127 nRLWLD 132 Rhodospirillum rubrum ATCC 11170
ABG58429     118 qALALE 123 Cytophaga hutchinsonii ATCC 33406
YP_869541    102 hILKLK 107 Shewanella sp. ANA-3
YP_001320069 109 kRVVLL 114 Alkaliphilus metalliredigens QYMF
YP_001857604 113 sELQLR 118 Burkholderia phymatum STM815
YP_001995891 124 eRILLQ 129 Chloroherpeton thalassium ATCC 35110
YP_003095030 119 iKIILN 124 Flavobacteriaceae bacterium 3519-10

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