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Conserved domains on  [gi|1513198437|gb|RNT50458|]
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acetyltransferase [Klebsiella pneumoniae]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10013546)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate, similar to Escherichia coli putative N-acetyltransferase YjaB

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10514 PRK10514
putative acetyltransferase; Provisional
 2-146 2.60e-108

putative acetyltransferase; Provisional


:

Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 304.23  E-value: 2.60e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513198437   2 VINIRRSRPDEGDKLTAIWCRSVDATHDFLTKAYRKELEEMVRAFLPEAPLWVAVNTEDQPIAFMLLTGEHMDALFVDPD 81
Cdd:PRK10514    1 MISIRRSRHEEGERLVAIWRRSVDATHDFLSAEDRAEIEELVRSFLPEAPLWVAVDERDQPVGFMLLSGGHMEALFVDPD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1513198437  82 VRGCGVGKLLIEHALSLTPKLTTNVNEQNEQAVGFYQKMGFRVTGRSETDDLGQPYPLLNLMYEQ 146
Cdd:PRK10514   81 VRGCGVGRMLVEHALSLHPELTTDVNEQNEQAVGFYKKMGFKVTGRSEVDDQGRPYPLLHLAYVG 145
 
Name Accession Description Interval E-value
PRK10514 PRK10514
putative acetyltransferase; Provisional
 2-146 2.60e-108

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 304.23  E-value: 2.60e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513198437   2 VINIRRSRPDEGDKLTAIWCRSVDATHDFLTKAYRKELEEMVRAFLPEAPLWVAVNTEDQPIAFMLLTGEHMDALFVDPD 81
Cdd:PRK10514    1 MISIRRSRHEEGERLVAIWRRSVDATHDFLSAEDRAEIEELVRSFLPEAPLWVAVDERDQPVGFMLLSGGHMEALFVDPD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1513198437  82 VRGCGVGKLLIEHALSLTPKLTTNVNEQNEQAVGFYQKMGFRVTGRSETDDLGQPYPLLNLMYEQ 146
Cdd:PRK10514   81 VRGCGVGRMLVEHALSLHPELTTDVNEQNEQAVGFYKKMGFKVTGRSEVDDQGRPYPLLHLAYVG 145
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-127 5.39e-18

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 75.80  E-value: 5.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513198437   3 INIRRSRPDEGDKLTAIWCRSVDAThdflTKAYRKE---LEEMVRAF----LPEAPLWVAVNtEDQPIAFMLL------- 68
Cdd:COG1247     2 MTIRPATPEDAPAIAAIYNEAIAEG----TATFETEppsEEEREAWFaailAPGRPVLVAEE-DGEVVGFASLgpfrprp 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1513198437  69 ----TGEHmdALFVDPDVRGCGVGKLLIEHALSLTP-----KLTTNVNEQNEQAVGFYQKMGFRVTGR 127
Cdd:COG1247    77 ayrgTAEE--SIYVDPDARGRGIGRALLEALIERARargyrRLVAVVLADNEASIALYEKLGFEEVGT 142
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 30-132 1.05e-13

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 63.44  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513198437  30 FLTKAYRKELEEMVRAflPEAPLWVAvnTEDQPIAFM--LLTGEHMDALFVDPDVRGCGVGKLLIEHALSLTPKL----- 102
Cdd:pfam13673  13 FYEFISPEALRERIDQ--GEYFFFVA--FEGGQIVGViaLRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDgikls 88

                          90       100       110
                  ....*....|....*....|....*....|
gi 1513198437 103 TTNVNEQNeQAVGFYQKMGFRVTGRSETDD 132
Cdd:pfam13673  89 ELTVNASP-YAVPFYEKLGFRATGPEQEFN 117
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 52-96 3.09e-06

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.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 42.26  E-value: 3.09e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1513198437  52 LWVAVNtEDQPIAFMLLTGE-------HMDALFVDPDVRGCGVGKLLIEHAL 96
Cdd:cd04301     1 FLVAED-DGEIVGFASLSPDgsggdtaYIGDLAVLPEYRGKGIGSALLEAAE 51
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 53-127 4.32e-03

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this family are members of the pfam00583 (GNAT) superfamily of acetyltransferases and are proposed to perform a N-acetylation step in the process of pseudaminic acid biosynthesis in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci. Significantly, many genomes containing other components of this pathway lack this gene, indicating that some other N-acetyl transferases may be incolved and/or the step is optional, resulting in a non-acetylated pseudaminic acid variant sugar.


Pssm-ID: 274661 [Multi-domain]  Cd Length: 152  Bit Score: 35.41  E-value: 4.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513198437  53 WVaVNTEDQPIAFMLLTG-----EHMD-ALFVDPDVRGcGVGKLLIEHALSLT------PKLTTNVNEQNEQAVGFYQKM 120
Cdd:TIGR03585  54 WI-VCQESRPIGVISFTDinlvhKSAFwGIYANPFCKP-GVGSVLEEAALEYAfehlglHKLSLEVLESNNKALKLYEKF 131


                  ....*..
gi 1513198437 121 GFRVTGR 127
Cdd:TIGR03585 132 GFEREGV 138
 
Name Accession Description Interval E-value
PRK10514 PRK10514
putative acetyltransferase; Provisional
 2-146 2.60e-108

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 304.23  E-value: 2.60e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513198437   2 VINIRRSRPDEGDKLTAIWCRSVDATHDFLTKAYRKELEEMVRAFLPEAPLWVAVNTEDQPIAFMLLTGEHMDALFVDPD 81
Cdd:PRK10514    1 MISIRRSRHEEGERLVAIWRRSVDATHDFLSAEDRAEIEELVRSFLPEAPLWVAVDERDQPVGFMLLSGGHMEALFVDPD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1513198437  82 VRGCGVGKLLIEHALSLTPKLTTNVNEQNEQAVGFYQKMGFRVTGRSETDDLGQPYPLLNLMYEQ 146
Cdd:PRK10514   81 VRGCGVGRMLVEHALSLHPELTTDVNEQNEQAVGFYKKMGFKVTGRSEVDDQGRPYPLLHLAYVG 145
PRK10562 PRK10562
putative acetyltransferase; Provisional
 5-136 3.29e-24

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 91.28  E-value: 3.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513198437   5 IRRSRPDEGDKLTAIWCRSVDATHDFLTKAYRKELEEMVR-AFLPEAPLWVAVNtEDQPIAFM-LLTGEHMDALFVDPDV 82
Cdd:PRK10562    2 IREYQPSDLPAILQLWLESTIWAHPFIKEQYWRESAPLVRdVYLPAAQTWVWEE-DGKLLGFVsVLEGRFVGALFVAPKA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1513198437  83 RGCGVGKLLIEHALSLTPKLTTNVNEQNEQAVGFYQKMGFRVTGRSETDDLGQP 136
Cdd:PRK10562   81 VRRGIGKALMQHVQQRYPHLSLEVYQKNQRAVNFYHAQGFRIVDSAWQEETQHP 134
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-127 5.39e-18

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 75.80  E-value: 5.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513198437   3 INIRRSRPDEGDKLTAIWCRSVDAThdflTKAYRKE---LEEMVRAF----LPEAPLWVAVNtEDQPIAFMLL------- 68
Cdd:COG1247     2 MTIRPATPEDAPAIAAIYNEAIAEG----TATFETEppsEEEREAWFaailAPGRPVLVAEE-DGEVVGFASLgpfrprp 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1513198437  69 ----TGEHmdALFVDPDVRGCGVGKLLIEHALSLTP-----KLTTNVNEQNEQAVGFYQKMGFRVTGR 127
Cdd:COG1247    77 ayrgTAEE--SIYVDPDARGRGIGRALLEALIERARargyrRLVAVVLADNEASIALYEKLGFEEVGT 142
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 22-135 6.10e-17

N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 72.39  E-value: 6.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513198437  22 RSVDATH-DFLTKayRKELEEMVRAFLPEAP--LWVAVNTEDQPIAFMLLT-----GEHMDALFVDPDVRGCGVGKLLIE 93
Cdd:COG0454     4 RKATPEDiNFILL--IEALDAELKAMEGSLAgaEFIAVDDKGEPIGFAGLRrlddkVLELKRLYVLPEYRGKGIGKALLE 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1513198437  94 HALSLTPK-----LTTNVNEQNEQAVGFYQKMGFRVTGRSETDDLGQ 135
Cdd:COG0454    82 ALLEWARErgctaLELDTLDGNPAAIRFYERLGFKEIERYVAYVGGE 128
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 72-130 9.23e-16

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 68.14  E-value: 9.23e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1513198437  72 HMDALFVDPDVRGCGVGKLLIEHALSL-----TPKLTTNVNEQNEQAVGFYQKMGFRVTGRSET 130
Cdd:COG0456    15 EIEDLAVDPEYRGRGIGRALLEAALERarergARRLRLEVREDNEAAIALYEKLGFEEVGERPN 78
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 30-132 1.05e-13

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 63.44  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513198437  30 FLTKAYRKELEEMVRAflPEAPLWVAvnTEDQPIAFM--LLTGEHMDALFVDPDVRGCGVGKLLIEHALSLTPKL----- 102
Cdd:pfam13673  13 FYEFISPEALRERIDQ--GEYFFFVA--FEGGQIVGViaLRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDgikls 88

                          90       100       110
                  ....*....|....*....|....*....|
gi 1513198437 103 TTNVNEQNeQAVGFYQKMGFRVTGRSETDD 132
Cdd:pfam13673  89 ELTVNASP-YAVPFYEKLGFRATGPEQEFN 117
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 48-124 1.01e-12

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 59.78  E-value: 1.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513198437  48 PEAPLWVAVNtEDQPIAFMLLTGEHMDA------LFVDPDVRGCGVGKLLIEHALSL--TPKLTTNVNEQNEQAVGFYQK 119
Cdd:pfam13508   1 PGGRFFVAED-DGKIVGFAALLPLDDEGalaelrLAVHPEYRGQGIGRALLEAAEAAakEGGIKLLELETTNRAAAFYEK 79


                  ....*
gi 1513198437 120 MGFRV 124
Cdd:pfam13508  80 LGFEE 84
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
5-127 2.39e-11

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 57.79  E-value: 2.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513198437   5 IRRSRPDEGDKLTAIWCRSvdathdfLTKAYRKELEEMVRAFLPEAPLWVAVnTEDQPIAFMLLTGEHMD---------A 75
Cdd:COG3153     1 IRPATPEDAEAIAALLRAA-------FGPGREAELVDRLREDPAAGLSLVAE-DDGEIVGHVALSPVDIDgegpalllgP 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1513198437  76 LFVDPDVRGCGVGKLLIEHALSLTPK-------LTTnvneqNEQAVGFYQKMGFRVTGR 127
Cdd:COG3153    73 LAVDPEYRGQGIGRALMRAALEAARErgaravvLLG-----DPSLLPFYERFGFRPAGE 126
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 36-122 1.68e-10

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 54.83  E-value: 1.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513198437  36 RKELEEMVRAFLPEAPLWVAVNTEDQPIAFMLLTGE-------HMDALFVDPDVRGCGVGKLLIEHALSL-----TPKLT 103
Cdd:pfam00583  18 DEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIddeppvgEIEGLAVAPEYRGKGIGTALLQALLEWarergCERIF 97

                          90
                  ....*....|....*....
gi 1513198437 104 TNVNEQNEQAVGFYQKMGF 122
Cdd:pfam00583  98 LEVAADNLAAIALYEKLGF 116
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 32-129 1.34e-09

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 53.07  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513198437  32 TKAYRKELEEMVRAFLPEAP---LWVAVNtEDQPIAFMLL------TGEhMDALFVDPDVRGCGVGKLLIEHALS----- 97
Cdd:COG1246     7 TPDDVPAILELIRPYALEEEigeFWVAEE-DGEIVGCAALhpldedLAE-LRSLAVHPDYRGRGIGRRLLEALLAearel 84

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1513198437  98 ----LTpkLTTnvneqNEQAVGFYQKMGFRVTGRSE 129
Cdd:COG1246    85 glkrLF--LLT-----TSAAIHFYEKLGFEEIDKED 113
PRK09831 PRK09831
GNAT family N-acetyltransferase;
3-124 3.02e-08

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 49.57  E-value: 3.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513198437   3 INIRRSRPDEGDKLTAIWCRSVD--ATHDFLTK---AYRKELEEMVRAFLPEAPLWVAVnTEDQPIAFMLLTGEHMDALF 77
Cdd:PRK09831    1 IQIRNYQPGDFQQLCAIFIRAVTmtASQHYSPQqiaAWAQIDESRWKEKLAKSQVRVAV-INAQPVGFITCIEHYIDMLF 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1513198437  78 VDPDVRGCGVGKLLIEHALSLTPKLTTNVneqNEQAVGFYQKMGFRV 124
Cdd:PRK09831   80 VDPEYTRRGVASALLKPLIKSESELTVDA---SITAKPFFERYGFQT 123
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
76-132 6.00e-07

Predicted N-acyltransferase, GNAT family [General function prediction only];


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 45.95  E-value: 6.00e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513198437  76 LFVDPDVRGCGVGKLLIEHALSLTPKLTTN---VNEQnEQAVGFYQKMGFRVTGRSETDD 132
Cdd:COG2153    64 VAVLPEYRGQGLGRALMEAAIEEARERGARrivLSAQ-AHAVGFYEKLGFVPVGEEFLEA 122
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
75-127 7.41e-07

Predicted acetyltransferase, GNAT family [General function prediction only];


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 44.51  E-value: 7.41e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1513198437  75 ALFVDPDVRGCGVGKLLIEHALSL-----TPKLTTNVNEQNEQAVGFYQKMGFRVTGR 127
Cdd:COG3393    20 GVYTHPEYRGRGLASALVAALAREalargARTPFLYVDADNPAARRLYERLGFRPVGE 77
PRK03624 PRK03624
putative acetyltransferase; Provisional
 76-124 2.40e-06

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 44.53  E-value: 2.40e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1513198437  76 LFVDPDVRGCGVGKLLIEHALS-LT----PKLTTNVNEQNEQAVGFYQKMGFRV 124
Cdd:PRK03624   74 LAVHPDFRGRGIGRALVARLEKkLIargcPKINLQVREDNDAVLGFYEALGYEE 127
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 52-96 3.09e-06

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.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 42.26  E-value: 3.09e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1513198437  52 LWVAVNtEDQPIAFMLLTGE-------HMDALFVDPDVRGCGVGKLLIEHAL 96
Cdd:cd04301     1 FLVAED-DGEIVGFASLSPDgsggdtaYIGDLAVLPEYRGKGIGSALLEAAE 51
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 5-129 1.04e-04

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 40.37  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513198437   5 IRRSRPDEGDKLTAIWCRSVDATHDFLTKAYRKELEEMVRAFLPE------APLWVAVNTEDQPIAFMLLTGEHMD---- 74
Cdd:COG1670    10 LRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLADwadggaLPFAIEDKEDGELIGVVGLYDIDRAnrsa 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1513198437  75 --ALFVDPDVRGCGVG----KLLIEHA---LSLTpKLTTNVNEQNEQAVGFYQKMGFRVTGRSE 129
Cdd:COG1670    90 eiGYWLAPAYWGKGYAtealRALLDYAfeeLGLH-RVEAEVDPDNTASIRVLEKLGFRLEGTLR 152
PRK07757 PRK07757
N-acetyltransferase;
75-129 9.78e-04

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 37.48  E-value: 9.78e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1513198437  75 ALFVDPDVRGCGVGKLLIEHAL------------SLTPKlttnvneqneqaVGFYQKMGFRVTGRSE 129
Cdd:PRK07757   70 SLAVSEDYRGQGIGRMLVEACLeearelgvkrvfALTYQ------------PEFFEKLGFREVDKEA 124
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 53-127 4.32e-03

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this family are members of the pfam00583 (GNAT) superfamily of acetyltransferases and are proposed to perform a N-acetylation step in the process of pseudaminic acid biosynthesis in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci. Significantly, many genomes containing other components of this pathway lack this gene, indicating that some other N-acetyl transferases may be incolved and/or the step is optional, resulting in a non-acetylated pseudaminic acid variant sugar.


Pssm-ID: 274661 [Multi-domain]  Cd Length: 152  Bit Score: 35.41  E-value: 4.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513198437  53 WVaVNTEDQPIAFMLLTG-----EHMD-ALFVDPDVRGcGVGKLLIEHALSLT------PKLTTNVNEQNEQAVGFYQKM 120
Cdd:TIGR03585  54 WI-VCQESRPIGVISFTDinlvhKSAFwGIYANPFCKP-GVGSVLEEAALEYAfehlglHKLSLEVLESNNKALKLYEKF 131


                  ....*..
gi 1513198437 121 GFRVTGR 127
Cdd:TIGR03585 132 GFEREGV 138
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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