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Conserved domains on  [gi|507058506|ref|WP_016129412|]
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GNAT family N-acetyltransferase [Bacillus nitratireducens]

Protein Classification

GNAT family protein( domain architecture ID 106742)

GNAT (Gcn5-related N-acetyltransferase) family protein similar to N-acetyltransferases that catalyze the transfer of an acetyl group from acetyl-CoA to a substrate

PubMed:  15581578

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NAT_SF super family cl17182
N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of ...
 12-130 1.60e-17

N-Acyltransferase superfamily: Various enyzmes that characteristicly 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, 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 mechanism is an ordered Bi-Bi ternary complex kinetic mechanism for most GNATs: 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 then 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/ph enylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


The actual alignment was detected with superfamily member pfam13527:

Pssm-ID: 473072 [Multi-domain]  Cd Length: 124  Bit Score: 76.84  E-value: 1.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507058506   12 LEEPEREQLFPLFDEVFGITSQTLHDFsekgYWDYTYKALSFI---QDDKVIANVAAFSLPLLINGEKINAAGIQSVMTH 88
Cdd:pfam13527   4 LTEDEFDEVLRLLEYAFQDEDSPELRE----YFRPLLEEGRVLgafDDGELVSTLALYPFELNVPGKTLPAAGITGVATY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 507058506   89 PDFRRQGLMTQLLNKMIEEIDKQCEC-AFLFTETPELYKSFGF 130
Cdd:pfam13527  80 PEYRGRGVMSRLLRRSLEEMRERGVPlSFLYPSSYPIYRRFGY 122
 
Name Accession Description Interval E-value
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 12-130 1.60e-17

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 76.84  E-value: 1.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507058506   12 LEEPEREQLFPLFDEVFGITSQTLHDFsekgYWDYTYKALSFI---QDDKVIANVAAFSLPLLINGEKINAAGIQSVMTH 88
Cdd:pfam13527   4 LTEDEFDEVLRLLEYAFQDEDSPELRE----YFRPLLEEGRVLgafDDGELVSTLALYPFELNVPGKTLPAAGITGVATY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 507058506   89 PDFRRQGLMTQLLNKMIEEIDKQCEC-AFLFTETPELYKSFGF 130
Cdd:pfam13527  80 PEYRGRGVMSRLLRRSLEEMRERGVPlSFLYPSSYPIYRRFGY 122
Eis COG4552
Predicted acetyltransferase [General function prediction only];
12-130 2.74e-13

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 69.54  E-value: 2.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507058506  12 LEEPEREQLFPLFDEVFGITsqtlHDFSEKGYWDYTYK---ALSFIQDDKVIANVAAFSLPLLINGEKINAAGIQSVMTH 88
Cdd:COG4552    6 LTEDDLDAFARLLAYAFGPE----PDDEELEAYRPLLEpgrVLGVFDDGELVGTLALYPFTLNVGGARVPMAGITGVAVA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 507058506  89 PDFRRQGLMTQLLNKMIEEI-DKQCECAFLFTETPELYKSFGF 130
Cdd:COG4552   82 PEHRRRGVARALLREALAELrERGQPLSALYPFEPGFYRRFGY 124
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 53-117 1.00e-04

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: 39.57  E-value: 1.00e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507058506  53 FIQDDKVIANVAafslpLLINGEKINAAGIQSVMTHPDFRRQGLMTQLLNKMIEEIDKQ-CECAFL 117
Cdd:cd04301    4 AEDDGEIVGFAS-----LSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERgAKRLRL 64
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 40-133 3.26e-04

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 40.00  E-value: 3.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507058506   40 EKGYWDYTYKALSFIQDDKVIAnVAAFSLPLLiNGEKINAAgiqsvmTHPDFRRQGLMTQLLNKMIEEIdKQCECAFLFT 119
Cdd:TIGR01575  23 AEELANYHLCYLLARIGGKVVG-YAGVQIVLD-EAHILNIA------VKPEYQGQGIGRALLRELIDEA-KGRGVNEIFL 93

                          90       100
                  ....*....|....*....|.
gi 507058506  120 ETPE-------LYKSFGFQIV 133
Cdd:TIGR01575  94 EVRVsniaaqaLYKKLGFNEI 114
 
Name Accession Description Interval E-value
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 12-130 1.60e-17

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 76.84  E-value: 1.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507058506   12 LEEPEREQLFPLFDEVFGITSQTLHDFsekgYWDYTYKALSFI---QDDKVIANVAAFSLPLLINGEKINAAGIQSVMTH 88
Cdd:pfam13527   4 LTEDEFDEVLRLLEYAFQDEDSPELRE----YFRPLLEEGRVLgafDDGELVSTLALYPFELNVPGKTLPAAGITGVATY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 507058506   89 PDFRRQGLMTQLLNKMIEEIDKQCEC-AFLFTETPELYKSFGF 130
Cdd:pfam13527  80 PEYRGRGVMSRLLRRSLEEMRERGVPlSFLYPSSYPIYRRFGY 122
Eis COG4552
Predicted acetyltransferase [General function prediction only];
12-130 2.74e-13

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 69.54  E-value: 2.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507058506  12 LEEPEREQLFPLFDEVFGITsqtlHDFSEKGYWDYTYK---ALSFIQDDKVIANVAAFSLPLLINGEKINAAGIQSVMTH 88
Cdd:COG4552    6 LTEDDLDAFARLLAYAFGPE----PDDEELEAYRPLLEpgrVLGVFDDGELVGTLALYPFTLNVGGARVPMAGITGVAVA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 507058506  89 PDFRRQGLMTQLLNKMIEEI-DKQCECAFLFTETPELYKSFGF 130
Cdd:COG4552   82 PEHRRRGVARALLREALAELrERGQPLSALYPFEPGFYRRFGY 124
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
12-136 6.67e-10

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 56.25  E-value: 6.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507058506  12 LEEPEREQLFPLFDEVFGIT--SQTLHDFSEKGYWDYTYKALsfiQDDKVIANVAAFslPLLINGEkINAAGIQSVMTHP 89
Cdd:COG3153    4 ATPEDAEAIAALLRAAFGPGreAELVDRLREDPAAGLSLVAE---DDGEIVGHVALS--PVDIDGE-GPALLLGPLAVDP 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 507058506  90 DFRRQGLMTQLLNKMIEEIDKQ-CECAFLFTETP--ELYKSFGFQIVQEY 136
Cdd:COG3153   78 EYRGQGIGRALMRAALEAARERgARAVVLLGDPSllPFYERFGFRPAGEL 127
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
78-140 7.67e-10

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 54.53  E-value: 7.67e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507058506  78 NAAGIQSVMTHPDFRRQGLMTQLLNKMIEEIDKQ-CECAFLFT--ETPE---LYKSFGFQIVQEYLMTV 140
Cdd:COG3393   14 GVAEISGVYTHPEYRGRGLASALVAALAREALARgARTPFLYVdaDNPAarrLYERLGFRPVGEYATVL 82
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 18-130 1.28e-08

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: 52.13  E-value: 1.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507058506   18 EQLFPLFDEVFGITSQTLHDFSEKGYWDYTYKALSFIQDDKVIANVAAFSlpllINGEKINAAGIQSVMTHPDFRRQGLM 97
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLS----IIDDEPPVGEIEGLAVAPEYRGKGIG 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 507058506   98 TQLLNKMIEE-IDKQCECAFLFTETP-----ELYKSFGF 130
Cdd:pfam00583  78 TALLQALLEWaRERGCERIFLEVAADnlaaiALYEKLGF 116
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 55-135 4.23e-08

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: 51.15  E-value: 4.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507058506  55 QDDKVIAnVAAfslpLLINGEKInaAGIQSVMTHPDFRRQGLMTQLLNKMIEEIDKQ-CECAFLFT--ETPELYKSFGFQ 131
Cdd:COG1246   35 EDGEIVG-CAA----LHPLDEDL--AELRSLAVHPDYRGRGIGRRLLEALLAEARELgLKRLFLLTtsAAIHFYEKLGFE 107


                 ....
gi 507058506 132 IVQE 135
Cdd:COG1246  108 EIDK 111
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 82-135 7.28e-07

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 46.57  E-value: 7.28e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 507058506  82 IQSVMTHPDFRRQGLMTQLLNKMIEEI-DKQCECAFLFTETP-----ELYKSFGFQIVQE 135
Cdd:COG0456   16 IEDLAVDPEYRGRGIGRALLEAALERArERGARRLRLEVREDneaaiALYEKLGFEEVGE 75
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 55-132 1.94e-06

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 45.14  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507058506   55 QDDKVIANVAafslplLINGEKINAAGIQSVMTHPDFRRQGLMTQLLNKmIEEIDKQCECAFLFTETPE----LYKSFGF 130
Cdd:pfam13508  10 DDGKIVGFAA------LLPLDDEGALAELRLAVHPEYRGQGIGRALLEA-AEAAAKEGGIKLLELETTNraaaFYEKLGF 82


                  ..
gi 507058506  131 QI 132
Cdd:pfam13508  83 EE 84
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 53-117 1.00e-04

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: 39.57  E-value: 1.00e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507058506  53 FIQDDKVIANVAafslpLLINGEKINAAGIQSVMTHPDFRRQGLMTQLLNKMIEEIDKQ-CECAFL 117
Cdd:cd04301    4 AEDDGEIVGFAS-----LSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERgAKRLRL 64
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 40-133 3.26e-04

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 40.00  E-value: 3.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507058506   40 EKGYWDYTYKALSFIQDDKVIAnVAAFSLPLLiNGEKINAAgiqsvmTHPDFRRQGLMTQLLNKMIEEIdKQCECAFLFT 119
Cdd:TIGR01575  23 AEELANYHLCYLLARIGGKVVG-YAGVQIVLD-EAHILNIA------VKPEYQGQGIGRALLRELIDEA-KGRGVNEIFL 93

                          90       100
                  ....*....|....*....|.
gi 507058506  120 ETPE-------LYKSFGFQIV 133
Cdd:TIGR01575  94 EVRVsniaaqaLYKKLGFNEI 114
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 81-137 1.33e-03

FR47-like protein; The members of this family are similar to the C-terminal region of the D. melanogaster hypothetical protein FR47. This protein has been found to consist of two N-acyltransferase-like domains swapped with the C-terminal strands.


Pssm-ID: 117022 [Multi-domain]  Cd Length: 86  Bit Score: 36.92  E-value: 1.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507058506   81 GIQSVMTHPDFRRQGLMTQLLNKMIEEIDKQCECAFLF---TETP--ELYKSFGFQIVQEYL 137
Cdd:pfam08445  23 ELGALQTLPEHRRRGLGSRLVAALARGIAERGITPFAVvvaGNTPsrRLYEKLGFRKIDETY 84
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
84-133 1.37e-03

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 38.44  E-value: 1.37e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 507058506  84 SVMTHPDFRRQGLMTQLLNKMIEEIDKQ-CECAFLFTETP-----ELYKSFGFQIV 133
Cdd:COG1247   85 SIYVDPDARGRGIGRALLEALIERARARgYRRLVAVVLADneasiALYEKLGFEEV 140
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
85-137 3.10e-03

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 37.09  E-value: 3.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 507058506  85 VMTHPDFRRQGLMTQLLNKMIEEI-DKQCECAFLFTETP--ELYKSFGFQIV-QEYL 137
Cdd:COG2153   64 VAVLPEYRGQGLGRALMEAAIEEArERGARRIVLSAQAHavGFYEKLGFVPVgEEFL 120
 
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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