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Conserved domains on  [gi|658548469|ref|WP_029740934|]
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MULTISPECIES: GNAT family N-acetyltransferase [Enterobacter]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10013485)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10314 PRK10314
GNAT family N-acetyltransferase;
1-153 2.13e-107

GNAT family N-acetyltransferase;


:

Pssm-ID: 182373 [Multi-domain]  Cd Length: 153  Bit Score: 302.53  E-value: 2.13e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548469   1 MIQWQDLHHSDLTVHSLYALLKLRCEVFVVEQTCPYQDIDGDDLVGENRHILGWRDNELVAYARILKSEDDFEPVVIGRV 80
Cdd:PRK10314   1 MIEWQDLHHSELSVSQLYALLQLRCAVFVVEQNCPYQDIDGDDLTGDNRHILGWKNDELVAYARILKSDDDLEPVVIGRV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548469  81 IISGKARGEKLGYQLMEKTLEACHKQWPDKALYLGAQAHLQSFYAHFGFTPVTEVYDEDGIPHIGMARETKQA 153
Cdd:PRK10314  81 IVSEALRGEKVGQQLMSKTLESCTRHWPDKPVYLGAQAHLQNFYQSFGFIPVTEVYEEDGIPHIGMAREVIQA 153
 
Name Accession Description Interval E-value
PRK10314 PRK10314
GNAT family N-acetyltransferase;
1-153 2.13e-107

GNAT family N-acetyltransferase;


Pssm-ID: 182373 [Multi-domain]  Cd Length: 153  Bit Score: 302.53  E-value: 2.13e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548469   1 MIQWQDLHHSDLTVHSLYALLKLRCEVFVVEQTCPYQDIDGDDLVGENRHILGWRDNELVAYARILKSEDDFEPVVIGRV 80
Cdd:PRK10314   1 MIEWQDLHHSELSVSQLYALLQLRCAVFVVEQNCPYQDIDGDDLTGDNRHILGWKNDELVAYARILKSDDDLEPVVIGRV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548469  81 IISGKARGEKLGYQLMEKTLEACHKQWPDKALYLGAQAHLQSFYAHFGFTPVTEVYDEDGIPHIGMARETKQA 153
Cdd:PRK10314  81 IVSEALRGEKVGQQLMSKTLESCTRHWPDKPVYLGAQAHLQNFYQSFGFIPVTEVYEEDGIPHIGMAREVIQA 153
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
17-149 3.51e-51

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 159.58  E-value: 3.51e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548469  17 LYALLKLRCEVFVVEQT-CPYQDIDGDDLvgENRHILGWRDNELVAYARILKSEDDFepVVIGRVIISGKARGEKLGYQL 95
Cdd:COG2153    4 LYDALALRREVFVVEQGvPPYLELDGKDE--DARHLLAYDDGELVATARLLPPGDGE--AKIGRVAVLPEYRGQGLGRAL 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 658548469  96 MEKTLEACHKQwPDKALYLGAQAHLQSFYAHFGFTPVTEVYDEDGIPHIGMARE 149
Cdd:COG2153   80 MEAAIEEARER-GARRIVLSAQAHAVGFYEKLGFVPVGEEFLEAGIPHIDMRKP 132
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 25-149 5.13e-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: 61.90  E-value: 5.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548469   25 CEVF--VVEQTCPYQDIDGddlvGENRHILGWRDNELVAYARILkseddfEPVVIGRVIISGKARGEKLGYQLMEKTLEA 102
Cdd:pfam13673  10 IETFyeFISPEALRERIDQ----GEYFFFVAFEGGQIVGVIALR------DRGHISLLFVDPDYQGQGIGKALLEAVEDY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 658548469  103 CHKQWPDK-ALYLGAQAHLQSFYAHFGFTPVTEVYDEDGIPHIGMARE 149
Cdd:pfam13673  80 AEKDGIKLsELTVNASPYAVPFYEKLGFRATGPEQEFNGIRFVPMEKE 127
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 50-106 1.13e-03

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: 35.71  E-value: 1.13e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 658548469  50 HILGWRDNELVAYARILKSEDDFEPVVIGRVIISGKARGEKLGYQLMEKTLEACHKQ 106
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARER 57
 
Name Accession Description Interval E-value
PRK10314 PRK10314
GNAT family N-acetyltransferase;
1-153 2.13e-107

GNAT family N-acetyltransferase;


Pssm-ID: 182373 [Multi-domain]  Cd Length: 153  Bit Score: 302.53  E-value: 2.13e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548469   1 MIQWQDLHHSDLTVHSLYALLKLRCEVFVVEQTCPYQDIDGDDLVGENRHILGWRDNELVAYARILKSEDDFEPVVIGRV 80
Cdd:PRK10314   1 MIEWQDLHHSELSVSQLYALLQLRCAVFVVEQNCPYQDIDGDDLTGDNRHILGWKNDELVAYARILKSDDDLEPVVIGRV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548469  81 IISGKARGEKLGYQLMEKTLEACHKQWPDKALYLGAQAHLQSFYAHFGFTPVTEVYDEDGIPHIGMARETKQA 153
Cdd:PRK10314  81 IVSEALRGEKVGQQLMSKTLESCTRHWPDKPVYLGAQAHLQNFYQSFGFIPVTEVYEEDGIPHIGMAREVIQA 153
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
17-149 3.51e-51

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 159.58  E-value: 3.51e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548469  17 LYALLKLRCEVFVVEQT-CPYQDIDGDDLvgENRHILGWRDNELVAYARILKSEDDFepVVIGRVIISGKARGEKLGYQL 95
Cdd:COG2153    4 LYDALALRREVFVVEQGvPPYLELDGKDE--DARHLLAYDDGELVATARLLPPGDGE--AKIGRVAVLPEYRGQGLGRAL 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 658548469  96 MEKTLEACHKQwPDKALYLGAQAHLQSFYAHFGFTPVTEVYDEDGIPHIGMARE 149
Cdd:COG2153   80 MEAAIEEARER-GARRIVLSAQAHAVGFYEKLGFVPVGEEFLEAGIPHIDMRKP 132
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 25-149 5.13e-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: 61.90  E-value: 5.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548469   25 CEVF--VVEQTCPYQDIDGddlvGENRHILGWRDNELVAYARILkseddfEPVVIGRVIISGKARGEKLGYQLMEKTLEA 102
Cdd:pfam13673  10 IETFyeFISPEALRERIDQ----GEYFFFVAFEGGQIVGVIALR------DRGHISLLFVDPDYQGQGIGKALLEAVEDY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 658548469  103 CHKQWPDK-ALYLGAQAHLQSFYAHFGFTPVTEVYDEDGIPHIGMARE 149
Cdd:pfam13673  80 AEKDGIKLsELTVNASPYAVPFYEKLGFRATGPEQEFNGIRFVPMEKE 127
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
54-149 8.34e-11

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 56.25  E-value: 8.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548469  54 WRDNELVAYARILKSEDDFEP--VVIGRVIISGKARGEKLGYQLMEKTLEAChKQWPDKALYLGAQAHLQSFYAHFGFTP 131
Cdd:COG3153   45 EDDGEIVGHVALSPVDIDGEGpaLLLGPLAVDPEYRGQGIGRALMRAALEAA-RERGARAVVLLGDPSLLPFYERFGFRP 123

                         90
                 ....*....|....*...
gi 658548469 132 VTEVYDEDGIPHIGMARE 149
Cdd:COG3153  124 AGELGLTLGPDEVFLAKE 141
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 17-129 3.74e-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: 48.67  E-value: 3.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548469   17 LYALLKLRCEVF-VVEQTCPYQDIDGDDLVGENRHILGWRDNELVAYARILKSEDDFEPVVIGRVIISGKARGEKLGYQL 95
Cdd:pfam00583   1 LEALYELLSEEFpEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 658548469   96 MEKTLEAChKQWPDKALYLGAQAH---LQSFYAHFGF 129
Cdd:pfam00583  81 LQALLEWA-RERGCERIFLEVAADnlaAIALYEKLGF 116
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 47-131 1.21e-06

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 43.98  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548469   47 ENRHILGWRDNELVAYARILKSEDDFEPVVIgRVIISGKARGEKLGYQLMEKtLEACHKQWPDKALYLGAQAHLQSFYAH 126
Cdd:pfam13508   2 GGRFFVAEDDGKIVGFAALLPLDDEGALAEL-RLAVHPEYRGQGIGRALLEA-AEAAAKEGGIKLLELETTNRAAAFYEK 79


                  ....*
gi 658548469  127 FGFTP 131
Cdd:pfam13508  80 LGFEE 84
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 54-134 1.80e-06

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: 44.60  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548469  54 WRDNELVAYARILKSEDDFepVVIGRVIISGKARGEKLGYQLMEKTLEACHKQwPDKALYLGAQAHLQSFYAHFGFTPVT 133
Cdd:COG1246   34 EEDGEIVGCAALHPLDEDL--AELRSLAVHPDYRGRGIGRRLLEALLAEAREL-GLKRLFLLTTSAAIHFYEKLGFEEID 110


                 .
gi 658548469 134 E 134
Cdd:COG1246  111 K 111
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 77-149 2.12e-04

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 38.10  E-value: 2.12e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658548469  77 IGRVIISGKARGEKLGYQLMEKTLEAChKQWPDKALYLGAQAH---LQSFYAHFGFTPVTEVYDEDGIPHIGMARE 149
Cdd:COG0456   16 IEDLAVDPEYRGRGIGRALLEAALERA-RERGARRLRLEVREDneaAIALYEKLGFEEVGERPNYYGDDALVMEKE 90
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 50-106 1.13e-03

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: 35.71  E-value: 1.13e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 658548469  50 HILGWRDNELVAYARILKSEDDFEPVVIGRVIISGKARGEKLGYQLMEKTLEACHKQ 106
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARER 57
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
47-135 8.96e-03

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 34.59  E-value: 8.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548469  47 ENRHILGWrdnelvAYARILKSEDDFEPVVIGRVIISGKARGEKLGYQLMEKTLEAChKQWPDKALYLGAQAHLQ---SF 123
Cdd:COG1247   59 EDGEVVGF------ASLGPFRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERA-RARGYRRLVAVVLADNEasiAL 131

                         90
                 ....*....|..
gi 658548469 124 YAHFGFTPVTEV 135
Cdd:COG1247  132 YEKLGFEEVGTL 143
 
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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