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Conserved domains on  [gi|491111268|ref|WP_004969793|]
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MULTISPECIES: GNAT family N-acetyltransferase [Acinetobacter]

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];
1-91 4.61e-26

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


:

Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 91.75  E-value: 4.61e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491111268  1 MQIQHQETQrgGEFFIERDGRHIAEITYQYQDDhTILADHTWVDLTLRGQGVARQLLDILVAFAREKQLKIVPVCSYIET 80
Cdd:COG2388   1 MEITHNEEK--GRFELEVDGELAGELTYRLEGG-VIIITHTEVPPALRGQGIASALVEAALDDARERGLKVVPLCPFVAA 77
                        90
                ....*....|.
gi 491111268 81 AFETDTQYADV 91
Cdd:COG2388  78 YFERHPEYADL 88
 
Name Accession Description Interval E-value
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
1-91 4.61e-26

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 91.75  E-value: 4.61e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491111268  1 MQIQHQETQrgGEFFIERDGRHIAEITYQYQDDhTILADHTWVDLTLRGQGVARQLLDILVAFAREKQLKIVPVCSYIET 80
Cdd:COG2388   1 MEITHNEEK--GRFELEVDGELAGELTYRLEGG-VIIITHTEVPPALRGQGIASALVEAALDDARERGLKVVPLCPFVAA 77
                        90
                ....*....|.
gi 491111268 81 AFETDTQYADV 91
Cdd:COG2388  78 YFERHPEYADL 88
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
13-91 8.97e-21

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: 78.33  E-value: 8.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491111268  13 EFFIERDG-RHIAEITYQYQDDHTILaDHTWVDLTLRGQGVARQLLDILVAFAREKQLKIVPVCSYIETAFETDTQYADV 91
Cdd:pfam14542  1 RFEIRVDGgAEVAFLTYRRGDGVLII-THTEVPPALRGQGIASKLVKAALDDAREEGLKIVPLCSYVAAYLEKHPEYADL 79
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
14-72 9.98e-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: 34.17  E-value: 9.98e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491111268 14 FFIERDGRHI--AEITYQYQDDHTILADHTWVDLTLRGQGVARQLLDILVAFAREKQLKIV 72
Cdd:cd04301   2 LVAEDDGEIVgfASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
 
Name Accession Description Interval E-value
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
1-91 4.61e-26

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 91.75  E-value: 4.61e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491111268  1 MQIQHQETQrgGEFFIERDGRHIAEITYQYQDDhTILADHTWVDLTLRGQGVARQLLDILVAFAREKQLKIVPVCSYIET 80
Cdd:COG2388   1 MEITHNEEK--GRFELEVDGELAGELTYRLEGG-VIIITHTEVPPALRGQGIASALVEAALDDARERGLKVVPLCPFVAA 77
                        90
                ....*....|.
gi 491111268 81 AFETDTQYADV 91
Cdd:COG2388  78 YFERHPEYADL 88
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
13-91 8.97e-21

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: 78.33  E-value: 8.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491111268  13 EFFIERDG-RHIAEITYQYQDDHTILaDHTWVDLTLRGQGVARQLLDILVAFAREKQLKIVPVCSYIETAFETDTQYADV 91
Cdd:pfam14542  1 RFEIRVDGgAEVAFLTYRRGDGVLII-THTEVPPALRGQGIASKLVKAALDDAREEGLKIVPLCSYVAAYLEKHPEYADL 79
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
9-70 4.47e-04

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: 36.51  E-value: 4.47e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491111268   9 QRGGEFFI-ERDGRHIAEITYQYQDDHTILADHTWVDLTLRGQGVARQLLDILVAFAREKQLK 70
Cdd:COG1246   25 EEIGEFWVaEEDGEIVGCAALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLK 87
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
10-81 4.75e-04

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 35.51  E-value: 4.75e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491111268  10 RGGEFFI-ERDGRHIAEITYQYQDDHTILADHT-WVDLTLRGQGVARQLLDILVAFAREKQLKIVPVCSYIETA 81
Cdd:pfam13508  1 PGGRFFVaEDDGKIVGFAALLPLDDEGALAELRlAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAA 74
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
2-72 9.35e-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: 35.57  E-value: 9.35e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491111268    2 QIQHQETQRGGEFFIERDGRHI--AEITYQYQDDHTILADHTWVDLTLRGQGVARQLLDILVAFAREKQLKIV 72
Cdd:pfam00583  24 LEDWDEDASEGFFVAEEDGELVgfASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERI 96
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
14-72 9.98e-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: 34.17  E-value: 9.98e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491111268 14 FFIERDGRHI--AEITYQYQDDHTILADHTWVDLTLRGQGVARQLLDILVAFAREKQLKIV 72
Cdd:cd04301   2 LVAEDDGEIVgfASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
9-79 3.39e-03

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 34.26  E-value: 3.39e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491111268   9 QRGGEFFI-ERDGRHIAEITYQYQDDHTILADHTWVDLTLRGQGVARQLLDILVAFAREKQLKIVPVCSYIE 79
Cdd:COG0454   31 LAGAEFIAvDDKGEPIGFAGLRRLDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDG 102
 
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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