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Conserved domains on  [gi|544938557|ref|WP_021346905|]
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MULTISPECIES: GNAT family N-acetyltransferase [Elizabethkingia]

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

CATH:  3.40.630.30
EC:  2.3.1.-|2.3.-.-
Gene Ontology:  GO:0008080|GO:0016746
PubMed:  10940244|9175471|15581578|27367672|26818562
SCOP:  3000403

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];
1-91 2.64e-32

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


:

Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 107.55  E-value: 2.64e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544938557  1 MEIKHrrEGSKGVFEAIEYDRVVGLMTYSVAGeDKIIIDHTEVDEAFGGRGIGKQLVNAGVDYARENNIKIIPLCPYANR 80
Cdd:COG2388   1 MEITH--NEEKGRFELEVDGELAGELTYRLEG-GVIIITHTEVPPALRGQGIASALVEAALDDARERGLKVVPLCPFVAA 77

                        90
                ....*....|.
gi 544938557 81 VLHSSDEYKDI 91
Cdd:COG2388  78 YFERHPEYADL 88
 
Name Accession Description Interval E-value
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
1-91 2.64e-32

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 107.55  E-value: 2.64e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544938557  1 MEIKHrrEGSKGVFEAIEYDRVVGLMTYSVAGeDKIIIDHTEVDEAFGGRGIGKQLVNAGVDYARENNIKIIPLCPYANR 80
Cdd:COG2388   1 MEITH--NEEKGRFELEVDGELAGELTYRLEG-GVIIITHTEVPPALRGQGIASALVEAALDDARERGLKVVPLCPFVAA 77

                        90
                ....*....|.
gi 544938557 81 VLHSSDEYKDI 91
Cdd:COG2388  78 YFERHPEYADL 88
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
 14-91 1.31e-28

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: 97.98  E-value: 1.31e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544938557  14 FEA-IEYDRVVGLMTYSVaGEDKIIIDHTEVDEAFGGRGIGKQLVNAGVDYARENNIKIIPLCPYANRVLHSSDEYKDI 91
Cdd:pfam14542  2 FEIrVDGGAEVAFLTYRR-GDGVLIITHTEVPPALRGQGIASKLVKAALDDAREEGLKIVPLCSYVAAYLEKHPEYADL 79
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 13-72 1.53e-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: 1.53e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544938557 13 VFEAIEYDRVVGLMTYSVAG--EDKIIIDHTEVDEAFGGRGIGKQLVNAGVDYARENNIKII 72
Cdd:cd04301   1 FLVAEDDGEIVGFASLSPDGsgGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
PRK07757 PRK07757
N-acetyltransferase;
43-70 3.18e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 34.40  E-value: 3.18e-03
                         10        20
                 ....*....|....*....|....*...
gi 544938557  43 VDEAFGGRGIGKQLVNAGVDYARENNIK 70
Cdd:PRK07757  73 VSEDYRGQGIGRMLVEACLEEARELGVK 100
 
Name Accession Description Interval E-value
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
1-91 2.64e-32

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 107.55  E-value: 2.64e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544938557  1 MEIKHrrEGSKGVFEAIEYDRVVGLMTYSVAGeDKIIIDHTEVDEAFGGRGIGKQLVNAGVDYARENNIKIIPLCPYANR 80
Cdd:COG2388   1 MEITH--NEEKGRFELEVDGELAGELTYRLEG-GVIIITHTEVPPALRGQGIASALVEAALDDARERGLKVVPLCPFVAA 77

                        90
                ....*....|.
gi 544938557 81 VLHSSDEYKDI 91
Cdd:COG2388  78 YFERHPEYADL 88
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
 14-91 1.31e-28

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: 97.98  E-value: 1.31e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544938557  14 FEA-IEYDRVVGLMTYSVaGEDKIIIDHTEVDEAFGGRGIGKQLVNAGVDYARENNIKIIPLCPYANRVLHSSDEYKDI 91
Cdd:pfam14542  2 FEIrVDGGAEVAFLTYRR-GDGVLIITHTEVPPALRGQGIASKLVKAALDDAREEGLKIVPLCSYVAAYLEKHPEYADL 79
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 20-75 1.57e-06

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 43.12  E-value: 1.57e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 544938557  20 DRVVGLMTYSVAGEDKIIIDHTEVDEAFGGRGIGKQLVNAGVDYARENNIKIIPLC 75
Cdd:COG0454   43 GEPIGFAGLRRLDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELD 98
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 13-72 1.53e-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: 1.53e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544938557 13 VFEAIEYDRVVGLMTYSVAG--EDKIIIDHTEVDEAFGGRGIGKQLVNAGVDYARENNIKII 72
Cdd:cd04301   1 FLVAEDDGEIVGFASLSPDGsgGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 7-72 3.95e-05

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: 39.04  E-value: 3.95e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544938557    7 REGSKGVFEAIEYDRVVGLMTYSVAGE--DKIIIDHTEVDEAFGGRGIGKQLVNAGVDYARENNIKII 72
Cdd:pfam00583  29 EDASEGFFVAEEDGELVGFASLSIIDDepPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERI 96
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
16-72 7.04e-05

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 38.91  E-value: 7.04e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544938557  16 AIEYDRVVG---LMTYSVAGEDKII-IDHTEVDEAFGGRGIGKQLVNAGVDYARENNIKII 72
Cdd:COG3153   44 AEDDGEIVGhvaLSPVDIDGEGPALlLGPLAVDPEYRGQGIGRALMRAALEAARERGARAV 104
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 25-72 3.43e-04

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 36.17  E-value: 3.43e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 544938557 25 LMTYSVAGEDKIIIDHTEVDEAFGGRGIGKQLVNAGVDYARENNIKII 72
Cdd:COG0456   3 ALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRL 50
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
20-70 1.20e-03

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 35.74  E-value: 1.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 544938557  20 DRVVGLMT---------YSVAGEDKIIidhteVDEAFGGRGIGKQLVNAGVDYARENNIK 70
Cdd:COG1247   61 GEVVGFASlgpfrprpaYRGTAEESIY-----VDPDARGRGIGRALLEALIERARARGYR 115
PRK07757 PRK07757
N-acetyltransferase;
43-70 3.18e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 34.40  E-value: 3.18e-03
                         10        20
                 ....*....|....*....|....*...
gi 544938557  43 VDEAFGGRGIGKQLVNAGVDYARENNIK 70
Cdd:PRK07757  73 VSEDYRGQGIGRMLVEACLEEARELGVK 100
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
43-72 7.79e-03

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 33.23  E-value: 7.79e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 544938557  43 VDEAFGGRGIGKQLVNAGVDYARENNIKII 72
Cdd:COG2153   66 VLPEYRGQGLGRALMEAAIEEARERGARRI 95
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 43-70 7.89e-03

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: 33.04  E-value: 7.89e-03
                         10        20
                 ....*....|....*....|....*...
gi 544938557  43 VDEAFGGRGIGKQLVNAGVDYARENNIK 70
Cdd:COG1246   60 VHPDYRGRGIGRRLLEALLAEARELGLK 87
 
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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