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Conserved domains on  [gi|2743330037|ref|WP_349632749|]
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GNAT family N-acetyltransferase [Lujinxingia vulgaris]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10006425)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate; similar to Escherichia coli uncharacterized protein YjdJ

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
47-117 3.42e-11

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


:

Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 55.16  E-value: 3.42e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2743330037  47 DVVVSRIDFRTDGDTFFLDYLWTNPEFRGQGHAREMVDHFSAFVQTRGGRITPICGVARAMMQGDARYTDV 117
Cdd:COG2388    18 GELAGELTYRLEGGVIIITHTEVPPALRGQGIASALVEAALDDARERGLKVVPLCPFVAAYFERHPEYADL 88
 
Name Accession Description Interval E-value
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
47-117 3.42e-11

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 55.16  E-value: 3.42e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2743330037  47 DVVVSRIDFRTDGDTFFLDYLWTNPEFRGQGHAREMVDHFSAFVQTRGGRITPICGVARAMMQGDARYTDV 117
Cdd:COG2388    18 GELAGELTYRLEGGVIIITHTEVPPALRGQGIASALVEAALDDARERGLKVVPLCPFVAAYFERHPEYADL 88
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
45-117 2.39e-09

GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both CoA and acetyl-CoA. They are characterized by highly conserved glycine, a cysteine residue in the acetyl-CoA binding site near the acetyl group, their small size compared with other GNATs and a lack of of an obvious substrate-binding site. It is proposed that they transfer an acetyl group from acetyl-CoA to one or more unidentified aliphatic amines via an acetyl (cysteine) enzyme intermediate. The substrate might be another macromolecule.


Pssm-ID: 434030 [Multi-domain]  Cd Length: 79  Bit Score: 50.21  E-value: 2.39e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2743330037  45 DTDVVVSRIDFRTDGDTFFLDYLWTNPEFRGQGHAREMVDHFSAFVQTRGGRITPICGVARAMMQGDARYTDV 117
Cdd:pfam14542   7 DGGAEVAFLTYRRGDGVLIITHTEVPPALRGQGIASKLVKAALDDAREEGLKIVPLCSYVAAYLEKHPEYADL 79
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
56-96 5.87e-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: 35.71  E-value: 5.87e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2743330037  56 RTDGDTFFLDYLWTNPEFRGQGHAREMVDHFSAFVQTRGGR 96
Cdd:cd04301    20 GSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAK 60
 
Name Accession Description Interval E-value
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
47-117 3.42e-11

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 55.16  E-value: 3.42e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2743330037  47 DVVVSRIDFRTDGDTFFLDYLWTNPEFRGQGHAREMVDHFSAFVQTRGGRITPICGVARAMMQGDARYTDV 117
Cdd:COG2388    18 GELAGELTYRLEGGVIIITHTEVPPALRGQGIASALVEAALDDARERGLKVVPLCPFVAAYFERHPEYADL 88
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
45-117 2.39e-09

GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both CoA and acetyl-CoA. They are characterized by highly conserved glycine, a cysteine residue in the acetyl-CoA binding site near the acetyl group, their small size compared with other GNATs and a lack of of an obvious substrate-binding site. It is proposed that they transfer an acetyl group from acetyl-CoA to one or more unidentified aliphatic amines via an acetyl (cysteine) enzyme intermediate. The substrate might be another macromolecule.


Pssm-ID: 434030 [Multi-domain]  Cd Length: 79  Bit Score: 50.21  E-value: 2.39e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2743330037  45 DTDVVVSRIDFRTDGDTFFLDYLWTNPEFRGQGHAREMVDHFSAFVQTRGGRITPICGVARAMMQGDARYTDV 117
Cdd:pfam14542   7 DGGAEVAFLTYRRGDGVLIITHTEVPPALRGQGIASKLVKAALDDAREEGLKIVPLCSYVAAYLEKHPEYADL 79
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
56-96 5.87e-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: 35.71  E-value: 5.87e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2743330037  56 RTDGDTFFLDYLWTNPEFRGQGHAREMVDHFSAFVQTRGGR 96
Cdd:cd04301    20 GSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAK 60
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
53-96 2.42e-03

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 34.63  E-value: 2.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2743330037  53 IDFRTDGDTFFLDYLWTNPEFRGQGHAREMVDHFSAFVQTRGGR 96
Cdd:COG0456     5 LGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGAR 48
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
55-94 2.46e-03

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 35.41  E-value: 2.46e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2743330037  55 FRTDGDTFFLDYLWTNPEFRGQGHAREMVDHFSAFVQTRG 94
Cdd:COG0454    52 RRLDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERG 91
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
48-94 3.38e-03

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 35.06  E-value: 3.38e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2743330037  48 VVVSRIDFRTDGDTFFLDYLWTNPEFRGQGHAREMVDHFSAFVQTRG 94
Cdd:COG3153    54 VALSPVDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERG 100
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
49-97 6.72e-03

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 33.34  E-value: 6.72e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2743330037  49 VVSRIDFRTDGDTF-FLDYLWTNPEFRGQGHAREMVDHFSAFVQTRGGRI 97
Cdd:COG3393     2 LVAMAGVRAESPGVaEISGVYTHPEYRGRGLASALVAALAREALARGART 51
 
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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