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Conserved domains on  [gi|16131953|ref|NP_418551|]
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putative N-acetyltransferase YjdJ [Escherichia coli str. K-12 substr. MG1655]

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];
1-88 7.96e-28

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


:

Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 95.99  E-value: 7.96e-28
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131953  1 MEIR--EGHNKFYINDkQGKQIAEIVFVPTGENLaIIEHTDVDESLKGQGIGKQLVAKVVEKMRREKRKIIPLCPFAKHE 78
Cdd:COG2388  1 MEIThnEEKGRFELEV-DGELAGELTYRLEGGVI-IITHTEVPPALRGQGIASALVEAALDDARERGLKVVPLCPFVAAY 78

                       90
               ....*....|
gi 16131953 79 FDKTREYDDI 88
Cdd:COG2388 79 FERHPEYADL 88
 
Name Accession Description Interval E-value
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
1-88 7.96e-28

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 95.99  E-value: 7.96e-28
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131953  1 MEIR--EGHNKFYINDkQGKQIAEIVFVPTGENLaIIEHTDVDESLKGQGIGKQLVAKVVEKMRREKRKIIPLCPFAKHE 78
Cdd:COG2388  1 MEIThnEEKGRFELEV-DGELAGELTYRLEGGVI-IITHTEVPPALRGQGIASALVEAALDDARERGLKVVPLCPFVAAY 78

                       90
               ....*....|
gi 16131953 79 FDKTREYDDI 88
Cdd:COG2388 79 FERHPEYADL 88
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
 9-88 9.53e-27

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: 93.35  E-value: 9.53e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131953    9 KFYINDKQGKQIAEIVFVpTGENLAIIEHTDVDESLKGQGIGKQLVAKVVEKMRREKRKIIPLCPFAKHEFDKTREYDDI 88
Cdd:pfam14542  1 RFEIRVDGGAEVAFLTYR-RGDGVLIITHTEVPPALRGQGIASKLVKAALDDAREEGLKIVPLCSYVAAYLEKHPEYADL 79
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 10-69 1.16e-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: 34.17  E-value: 1.16e-03
                       10        20        30        40        50        60
               ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131953 10 FYINDKQGKQI--AEIVFVPTGENLAIIEHTDVDESLKGQGIGKQLVAKVVEKMRREKRKII 69
Cdd:cd04301  1 FLVAEDDGEIVgfASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
 
Name Accession Description Interval E-value
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
1-88 7.96e-28

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 95.99  E-value: 7.96e-28
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131953  1 MEIR--EGHNKFYINDkQGKQIAEIVFVPTGENLaIIEHTDVDESLKGQGIGKQLVAKVVEKMRREKRKIIPLCPFAKHE 78
Cdd:COG2388  1 MEIThnEEKGRFELEV-DGELAGELTYRLEGGVI-IITHTEVPPALRGQGIASALVEAALDDARERGLKVVPLCPFVAAY 78

                       90
               ....*....|
gi 16131953 79 FDKTREYDDI 88
Cdd:COG2388 79 FERHPEYADL 88
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
 9-88 9.53e-27

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: 93.35  E-value: 9.53e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131953    9 KFYINDKQGKQIAEIVFVpTGENLAIIEHTDVDESLKGQGIGKQLVAKVVEKMRREKRKIIPLCPFAKHEFDKTREYDDI 88
Cdd:pfam14542  1 RFEIRVDGGAEVAFLTYR-RGDGVLIITHTEVPPALRGQGIASKLVKAALDDAREEGLKIVPLCSYVAAYLEKHPEYADL 79
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 3-63 8.19e-05

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: 38.43  E-value: 8.19e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131953   3 IREGHNKFYINDKQGKQIAEIVFVPTGENLAIIEHTDVDESLKGQGIGKQLVAKVVEKMRR 63
Cdd:COG1246  23 LEEEIGEFWVAEEDGEIVGCAALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARE 83
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 21-64 2.23e-04

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: 37.11  E-value: 2.23e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 16131953    21 AEIVFVPTGENLAIIEHTDVDESLKGQGIGKQLVAKVVEKMRRE 64
Cdd:pfam00583  48 ASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARER 91
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 10-69 1.16e-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: 34.17  E-value: 1.16e-03
                       10        20        30        40        50        60
               ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131953 10 FYINDKQGKQI--AEIVFVPTGENLAIIEHTDVDESLKGQGIGKQLVAKVVEKMRREKRKII 69
Cdd:cd04301  1 FLVAEDDGEIVgfASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 7-71 2.58e-03

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 33.58  E-value: 2.58e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131953    7 HNKFYINDKQGKQIAEIVFVPTGENLAIIEHT-DVDESLKGQGIGKQLVAKVVEKMRREKRKIIPL 71
Cdd:pfam13508  2 GGRFFVAEDDGKIVGFAALLPLDDEGALAELRlAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLEL 67
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
24-87 2.78e-03

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 34.29  E-value: 2.78e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131953  24 VFVPTGENLAIIEHTDVDESLKGQGIGKQLVAKVVEKMRREKRKII------PLCPF-AKHEFDKTREYDD 87
Cdd:COG3153  59 VDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVvllgdpSLLPFyERFGFRPAGELGL 129
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 23-69 4.45e-03

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 33.09  E-value: 4.45e-03
                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*..
gi 16131953 23 IVFVPTGENLAIIEHTDVDESLKGQGIGKQLVAKVVEKMRREKRKII 69
Cdd:COG0456  4 LLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRL 50
 
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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