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Conserved domains on  [gi|920138083|ref|WP_052955148|]
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GNAT family N-acetyltransferase [Enterobacter kobei]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11441181)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

CATH:  3.40.630.30
EC:  2.3.-.-
Gene Ontology:  GO:0016746|GO:0008080
PubMed:  27367672|26818562|15581578|10940244
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
2-157 1.68e-19

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 79.65  E-value: 1.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920138083   2 DFRFRLITAEDRPFMVQMLYEATIASEQTFDIDnienfPHSY----AYIENFPEAGEVGIIAEStDGTPAGAAWLRNFPE 77
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETE-----PPSEeereAWFAAILAPGRPVLVAEE-DGEVVGFASLGPFRP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920138083  78 GDKPGISGpELTIAIAPSYRRQRLAKRIMAQLYQAANALNIKTLKLGVYQKNVPALAFYKNDGWEP----------DVIF 147
Cdd:COG1247   75 RPAYRGTA-EESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEvgtlpevgfkFGRW 153

                        170
                 ....*....|
gi 920138083 148 GDYVMMKRAI 157
Cdd:COG1247  154 LDLVLMQKRL 163
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
2-157 1.68e-19

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 79.65  E-value: 1.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920138083   2 DFRFRLITAEDRPFMVQMLYEATIASEQTFDIDnienfPHSY----AYIENFPEAGEVGIIAEStDGTPAGAAWLRNFPE 77
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETE-----PPSEeereAWFAAILAPGRPVLVAEE-DGEVVGFASLGPFRP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920138083  78 GDKPGISGpELTIAIAPSYRRQRLAKRIMAQLYQAANALNIKTLKLGVYQKNVPALAFYKNDGWEP----------DVIF 147
Cdd:COG1247   75 RPAYRGTA-EESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEvgtlpevgfkFGRW 153

                        170
                 ....*....|
gi 920138083 148 GDYVMMKRAI 157
Cdd:COG1247  154 LDLVLMQKRL 163
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 25-141 1.21e-11

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: 57.91  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920138083   25 IASEQTFDIDNIENFPHSYAYIENFPEAGEVGIIAEStDGTPAGAAWLRNFPEGDKPGIsgpELTIAIAPSYRRQRLAKR 104
Cdd:pfam00583   4 LYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEE-DGELVGFASLSIIDDEPPVGE---IEGLAVAPEYRGKGIGTA 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 920138083  105 IMAQLYQAANALNIKTLKLGVYQKNVPALAFYKNDGW 141
Cdd:pfam00583  80 LLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 57-123 5.71e-05

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: 39.18  E-value: 5.71e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 920138083  57 IIAEStDGTPAGAAWLRNFPEGDKpgisGPELT-IAIAPSYRRQRLAKRIMAQLYQAANALNIKTLKL 123
Cdd:cd04301    2 LVAED-DGEIVGFASLSPDGSGGD----TAYIGdLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
PRK03624 PRK03624
putative acetyltransferase; Provisional
 91-148 4.21e-04

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 38.37  E-value: 4.21e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 920138083  91 AIAPSYRRQRLAKRIMAQLYQAANALNIKTLKLGVYQKNVPALAFYKNDGWEPD--VIFG 148
Cdd:PRK03624  75 AVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQdrISLG 134
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
2-157 1.68e-19

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 79.65  E-value: 1.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920138083   2 DFRFRLITAEDRPFMVQMLYEATIASEQTFDIDnienfPHSY----AYIENFPEAGEVGIIAEStDGTPAGAAWLRNFPE 77
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETE-----PPSEeereAWFAAILAPGRPVLVAEE-DGEVVGFASLGPFRP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920138083  78 GDKPGISGpELTIAIAPSYRRQRLAKRIMAQLYQAANALNIKTLKLGVYQKNVPALAFYKNDGWEP----------DVIF 147
Cdd:COG1247   75 RPAYRGTA-EESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEvgtlpevgfkFGRW 153

                        170
                 ....*....|
gi 920138083 148 GDYVMMKRAI 157
Cdd:COG1247  154 LDLVLMQKRL 163
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 25-141 1.21e-11

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: 57.91  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920138083   25 IASEQTFDIDNIENFPHSYAYIENFPEAGEVGIIAEStDGTPAGAAWLRNFPEGDKPGIsgpELTIAIAPSYRRQRLAKR 104
Cdd:pfam00583   4 LYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEE-DGELVGFASLSIIDDEPPVGE---IEGLAVAPEYRGKGIGTA 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 920138083  105 IMAQLYQAANALNIKTLKLGVYQKNVPALAFYKNDGW 141
Cdd:pfam00583  80 LLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 89-157 2.43e-11

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 56.59  E-value: 2.43e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 920138083  89 TIAIAPSYRRQRLAKRIMAQLYQAANALNIKTLKLGVYQKNVPALAFYKNDGWEPDVIFGDY-----VMMKRAI 157
Cdd:COG0456   18 DLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYygddaLVMEKEL 91
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-137 2.77e-09

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: 53.08  E-value: 2.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920138083   1 MDFRFRLITAEDRPFMVQMLYEATIASEQTFDIDNIENFPHSYAYIENFPEAGEVG--IIAESTDGTPAGAAWLRNFPEG 78
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLADWADGGALpfAIEDKEDGELIGVVGLYDIDRA 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 920138083  79 DKpgisGPELTIAIAPSYRRQRLAKRIMAQLYQAA-NALNIKTLKLGVYQKNVPALAFYK 137
Cdd:COG1670   86 NR----SAEIGYWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDNTASIRVLE 141
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 3-143 5.29e-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: 48.83  E-value: 5.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920138083   3 FRFRLITAEDRPFMVQMLYEATIAseqtfdiDNIENFphsyayienfpeagevgIIAEStDGTPAGAAWLRNFPEGDkpg 82
Cdd:COG1246    1 MTIRPATPDDVPAILELIRPYALE-------EEIGEF-----------------WVAEE-DGEIVGCAALHPLDEDL--- 52

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 920138083  83 isgPELT-IAIAPSYRRQRLAKRIMAQLYQAANALNIKTLKLGVYQknvPALAFYKNDGWEP 143
Cdd:COG1246   53 ---AELRsLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTS---AAIHFYEKLGFEE 108
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 57-143 6.02e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 47.45  E-value: 6.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920138083   57 IIAEStDGTPAGAAWLRNFPEGDKPGisgpELTIAIAPSYRRQRLAKRIMAQLYQAANALNIKTLKLGVYQknvPALAFY 136
Cdd:pfam13508   6 FVAED-DGKIVGFAALLPLDDEGALA----ELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTN---RAAAFY 77


                  ....*..
gi 920138083  137 KNDGWEP 143
Cdd:pfam13508  78 EKLGFEE 84
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
90-155 4.18e-07

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 45.28  E-value: 4.18e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 920138083  90 IAIAPSYRRQRLAKRIMAQLYQAANALNIKTLKLGVYQKNVPALAFYKNDGWEPDVIFGDYVMMKR 155
Cdd:COG3393   21 VYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEYATVLFRKP 86
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
63-143 1.40e-05

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 42.09  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920138083  63 DGTPAGAAwlRNFPEGDKPG-ISGpeltIAIAPSYRRQRLAKRIMAQLYQAANALNIKTLKLGVyQknVPALAFYKNDGW 141
Cdd:COG2153   42 DGELVATA--RLLPPGDGEAkIGR----VAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSA-Q--AHAVGFYEKLGF 112


                 ..
gi 920138083 142 EP 143
Cdd:COG2153  113 VP 114
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 57-123 5.71e-05

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: 39.18  E-value: 5.71e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 920138083  57 IIAEStDGTPAGAAWLRNFPEGDKpgisGPELT-IAIAPSYRRQRLAKRIMAQLYQAANALNIKTLKL 123
Cdd:cd04301    2 LVAED-DGEIVGFASLSPDGSGGD----TAYIGdLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
5-143 1.87e-04

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 39.30  E-value: 1.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920138083   5 FRLITAEDRPFMVQMLYEATIASEQTFDIDNIENFPhsyayienfpeAGEVGIIAEsTDGTPAGAAWL-RNFPEGDKPGI 83
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPGREAELVDRLREDP-----------AAGLSLVAE-DDGEIVGHVALsPVDIDGEGPAL 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 920138083  84 S-GPeltIAIAPSYRRQRLAKRIMAQLYQAANALNIKTLKLGVyqkNVPALAFYKNDGWEP 143
Cdd:COG3153   69 LlGP---LAVDPEYRGQGIGRALMRAALEAARERGARAVVLLG---DPSLLPFYERFGFRP 123
PRK03624 PRK03624
putative acetyltransferase; Provisional
 91-148 4.21e-04

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 38.37  E-value: 4.21e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 920138083  91 AIAPSYRRQRLAKRIMAQLYQAANALNIKTLKLGVYQKNVPALAFYKNDGWEPD--VIFG 148
Cdd:PRK03624  75 AVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQdrISLG 134
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 90-140 6.37e-04

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 37.99  E-value: 6.37e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 920138083  90 IAIAPSYRRQRLAKRIMAQLYQAANALNIKTLKLGVYQKNVPALAFYKNDG 140
Cdd:PRK09491  69 IAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLG 119
PRK10562 PRK10562
putative acetyltransferase; Provisional
 92-140 2.98e-03

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 35.81  E-value: 2.98e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 920138083  92 IAPSYRRQRLAKRIMAQLYQAANALNiktlkLGVYQKNVPALAFYKNDG 140
Cdd:PRK10562  76 VAPKAVRRGIGKALMQHVQQRYPHLS-----LEVYQKNQRAVNFYHAQG 119
 
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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