NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446139540|ref|WP_000217395|]
View 

MULTISPECIES: GNAT family N-acetyltransferase [Enterobacterales]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11447364)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 13-149 7.42e-06

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: 43.83  E-value: 7.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139540  13 TKQDVPFIIAVIRDGmRDGYFNFDDDDGLSQFESQISEAIARRERGENcadFLFVFDAQHNGAAIGFALLTGKNGANGla 92
Cdd:COG1670   14 RPEDAEALAELLNDP-EVARYLPGPPYSLEEARAWLERLLADWADGGA---LPFAIEDKEDGELIGVVGLYDIDRANR-- 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446139540  93 sHLEIRmFGVTRSQRQKGFGRSMLQSILD---ATPG-HKVEASCLPASVVMARMLTNAGFH 149
Cdd:COG1670   88 -SAEIG-YWLAPAYWGKGYATEALRALLDyafEELGlHRVEAEVDPDNTASIRVLEKLGFR 146
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 13-149 7.42e-06

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: 43.83  E-value: 7.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139540  13 TKQDVPFIIAVIRDGmRDGYFNFDDDDGLSQFESQISEAIARRERGENcadFLFVFDAQHNGAAIGFALLTGKNGANGla 92
Cdd:COG1670   14 RPEDAEALAELLNDP-EVARYLPGPPYSLEEARAWLERLLADWADGGA---LPFAIEDKEDGELIGVVGLYDIDRANR-- 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446139540  93 sHLEIRmFGVTRSQRQKGFGRSMLQSILD---ATPG-HKVEASCLPASVVMARMLTNAGFH 149
Cdd:COG1670   88 -SAEIG-YWLAPAYWGKGYATEALRALLDyafEELGlHRVEAEVDPDNTASIRVLEKLGFR 146
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 70-121 6.92e-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: 33.40  E-value: 6.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446139540  70 AQHNGAAIGFALLTGKNGANGlasHLEIRMFGVTRSQRQKGFGRSMLQSILD 121
Cdd:cd04301    4 AEDDGEIVGFASLSPDGSGGD---TAYIGDLAVLPEYRGKGIGSALLEAAEE 52
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 13-149 7.42e-06

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: 43.83  E-value: 7.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139540  13 TKQDVPFIIAVIRDGmRDGYFNFDDDDGLSQFESQISEAIARRERGENcadFLFVFDAQHNGAAIGFALLTGKNGANGla 92
Cdd:COG1670   14 RPEDAEALAELLNDP-EVARYLPGPPYSLEEARAWLERLLADWADGGA---LPFAIEDKEDGELIGVVGLYDIDRANR-- 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446139540  93 sHLEIRmFGVTRSQRQKGFGRSMLQSILD---ATPG-HKVEASCLPASVVMARMLTNAGFH 149
Cdd:COG1670   88 -SAEIG-YWLAPAYWGKGYATEALRALLDyafEELGlHRVEAEVDPDNTASIRVLEKLGFR 146
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 70-121 6.92e-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: 33.40  E-value: 6.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446139540  70 AQHNGAAIGFALLTGKNGANGlasHLEIRMFGVTRSQRQKGFGRSMLQSILD 121
Cdd:cd04301    4 AEDDGEIVGFASLSPDGSGGD---TAYIGDLAVLPEYRGKGIGSALLEAAEE 52
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH