NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|488981568|ref|WP_002892397|]
View 

MULTISPECIES: GNAT family N-acetyltransferase [Klebsiella]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10006981)

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
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
19-139 1.41e-13

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


:

Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 66.65  E-value: 1.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981568  19 FIDLAVKTFDLSFEEWYQQGYWTDAYIPYAFV--ERNKVIANASANIIDLRWQGEprrYIQIGTVMTEPDHRNKGLAGQL 96
Cdd:COG3153   12 IAALLRAAFGPGREAELVDRLREDPAAGLSLVaeDDGEIVGHVALSPVDIDGEGP---ALLLGPLAVDPEYRGQGIGRAL 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 488981568  97 IHHILQDWQQE-ADAFFLFANPTTVDFYPKFGFTRSEEYQYIMP 139
Cdd:COG3153   89 MRAALEAARERgARAVVLLGDPSLLPFYERFGFRPAGELGLTLG 132
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
19-139 1.41e-13

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 66.65  E-value: 1.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981568  19 FIDLAVKTFDLSFEEWYQQGYWTDAYIPYAFV--ERNKVIANASANIIDLRWQGEprrYIQIGTVMTEPDHRNKGLAGQL 96
Cdd:COG3153   12 IAALLRAAFGPGREAELVDRLREDPAAGLSLVaeDDGEIVGHVALSPVDIDGEGP---ALLLGPLAVDPEYRGQGIGRAL 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 488981568  97 IHHILQDWQQE-ADAFFLFANPTTVDFYPKFGFTRSEEYQYIMP 139
Cdd:COG3153   89 MRAALEAARERgARAVVLLGDPSLLPFYERFGFRPAGELGLTLG 132
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 14-128 1.67e-09

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 54.88  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981568   14 PLRKSFIDLAVKTFDLSFEEWYQQGYW------TDAYIPYAFVERNKVIANASANIIDLRWQGEPRRYIQIGTVMTEPDH 87
Cdd:pfam13527   3 PLTEDEFDEVLRLLEYAFQDEDSPELReyfrplLEEGRVLGAFDDGELVSTLALYPFELNVPGKTLPAAGITGVATYPEY 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 488981568   88 RNKGLAGQLIHHILQDWQQEADAF-FLFanPTTVDFYPKFGF 128
Cdd:pfam13527  83 RGRGVMSRLLRRSLEEMRERGVPLsFLY--PSSYPIYRRFGY 122
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 47-113 7.43e-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: 39.95  E-value: 7.43e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488981568  47 YAFVERNKVIAnasanIIDLRWQGEPRRYIQIGTVMTEPDHRNKGLAGQLIHHILQD-WQQEADAFFL 113
Cdd:cd04301    2 LVAEDDGEIVG-----FASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEaRERGAKRLRL 64
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
19-139 1.41e-13

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 66.65  E-value: 1.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981568  19 FIDLAVKTFDLSFEEWYQQGYWTDAYIPYAFV--ERNKVIANASANIIDLRWQGEprrYIQIGTVMTEPDHRNKGLAGQL 96
Cdd:COG3153   12 IAALLRAAFGPGREAELVDRLREDPAAGLSLVaeDDGEIVGHVALSPVDIDGEGP---ALLLGPLAVDPEYRGQGIGRAL 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 488981568  97 IHHILQDWQQE-ADAFFLFANPTTVDFYPKFGFTRSEEYQYIMP 139
Cdd:COG3153   89 MRAALEAARERgARAVVLLGDPSLLPFYERFGFRPAGELGLTLG 132
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
54-142 5.21e-12

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 60.69  E-value: 5.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981568  54 KVIANASANIidlrwqgEPRRYIQIGTVMTEPDHRNKGLAGQLIHHILQDWQQE-ADAFFLF---ANPTTVDFYPKFGFT 129
Cdd:COG3393    1 ELVAMAGVRA-------ESPGVAEISGVYTHPEYRGRGLASALVAALAREALARgARTPFLYvdaDNPAARRLYERLGFR 73

                         90
                 ....*....|...
gi 488981568 130 RSEEYQYIMPVSP 142
Cdd:COG3393   74 PVGEYATVLFRKP 86
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 14-128 1.67e-09

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 54.88  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981568   14 PLRKSFIDLAVKTFDLSFEEWYQQGYW------TDAYIPYAFVERNKVIANASANIIDLRWQGEPRRYIQIGTVMTEPDH 87
Cdd:pfam13527   3 PLTEDEFDEVLRLLEYAFQDEDSPELReyfrplLEEGRVLGAFDDGELVSTLALYPFELNVPGKTLPAAGITGVATYPEY 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 488981568   88 RNKGLAGQLIHHILQDWQQEADAF-FLFanPTTVDFYPKFGF 128
Cdd:pfam13527  83 RGRGVMSRLLRRSLEEMRERGVPLsFLY--PSSYPIYRRFGY 122
Eis COG4552
Predicted acetyltransferase [General function prediction only];
47-167 5.91e-09

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 56.45  E-value: 5.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981568  47 YAFVERNKVIANASANIIDLRWQGEPRRYIQIGTVMTEPDHRNKGLAGQLIHHILQDWQQEADAF-FLFanPTTVDFYPK 125
Cdd:COG4552   44 LGVFDDGELVGTLALYPFTLNVGGARVPMAGITGVAVAPEHRRRGVARALLREALAELRERGQPLsALY--PFEPGFYRR 121

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 488981568 126 FGFTR-SEEYQYIMPVS------PRAGDFRKLDmdsPDDVALLRHYYEK 167
Cdd:COG4552  122 FGYELaGDRRRYTIPPEslplrpDAPGRVRRVD---PDDAELLAALYER 167
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 78-146 7.77e-08

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: 50.38  E-value: 7.77e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981568  78 IGTVMTEPDHRNKGLAGQLIHHILQD-WQQEADAFFLFANPTTVDFYPKFGFTRSEEYQYIMPVSPRAGD 146
Cdd:COG1246   55 LRSLAVHPDYRGRGIGRRLLEALLAEaRELGLKRLFLLTTSAAIHFYEKLGFEEIDKEDLPYAKVWQRDS 124
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
66-134 1.55e-07

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 49.41  E-value: 1.55e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488981568  66 LRWQGEPRRYIQIGTVMTEPDHRNKGLAGQLIHHILQDWQQE-ADAFFLFANPTTVDFYPKFGFTR-SEEY 134
Cdd:COG2153   49 ARLLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERgARRIVLSAQAHAVGFYEKLGFVPvGEEF 119
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 50-134 1.68e-06

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 46.59  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981568  50 VERNKVIANASANIIDlRWQGEPRRyiqigtVMTEPDHRNKGLAGQLIHHiLQDWQQEAD--AFFLF---ANPTTVDFYP 124
Cdd:COG0454   40 DDKGEPIGFAGLRRLD-DKVLELKR------LYVLPEYRGKGIGKALLEA-LLEWARERGctALELDtldGNPAAIRFYE 111

                         90
                 ....*....|
gi 488981568 125 KFGFTRSEEY 134
Cdd:COG0454  112 RLGFKEIERY 121
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 68-133 3.65e-06

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 44.65  E-value: 3.65e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981568  68 WQGEPRRYIQIGTVMTEPDHRNKGLAGQLIHHILQD-WQQEADAFFLF---ANPTTVDFYPKFGFTRSEE 133
Cdd:COG0456    6 GLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERaRERGARRLRLEvreDNEAAIALYEKLGFEEVGE 75
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 51-130 7.85e-06

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 43.21  E-value: 7.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981568   51 ERNKVIANASANIIDlrwqgePRRYIQIGTVMTEPDHRNKGLAGQLIHHILQ-DWQQEADAFFLFANPTTVDFYPKFGFT 129
Cdd:pfam13508  10 DDGKIVGFAALLPLD------DEGALAELRLAVHPEYRGQGIGRALLEAAEAaAKEGGIKLLELETTNRAAAFYEKLGFE 83


                  .
gi 488981568  130 R 130
Cdd:pfam13508  84 E 84
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 32-128 1.42e-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: 43.28  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981568   32 EEWYQQGYWTDAYIPYAFVERN-KVIANASANIIDlrwqgEPRRYIQIGTVMTEPDHRNKGLAGQLIHHILQD-WQQEAD 109
Cdd:pfam00583  20 PLDLLEDWDEDASEGFFVAEEDgELVGFASLSIID-----DEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWaRERGCE 94

                          90       100
                  ....*....|....*....|..
gi 488981568  110 AFFLF---ANPTTVDFYPKFGF 128
Cdd:pfam00583  95 RIFLEvaaDNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 47-113 7.43e-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: 39.95  E-value: 7.43e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488981568  47 YAFVERNKVIAnasanIIDLRWQGEPRRYIQIGTVMTEPDHRNKGLAGQLIHHILQD-WQQEADAFFL 113
Cdd:cd04301    2 LVAEDDGEIVG-----FASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEaRERGAKRLRL 64
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 73-136 1.69e-04

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 40.72  E-value: 1.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488981568   73 RRYIQIGTVMTEPDHRNKGLAGQLIHHILQD---WQQEADAFFLFANPTTVDFYPKFGFTRSEEYQY 136
Cdd:pfam13673  49 RDRGHISLLFVDPDYQGQGIGKALLEAVEDYaekDGIKLSELTVNASPYAVPFYEKLGFRATGPEQE 115
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 78-137 1.06e-03

FR47-like protein; The members of this family are similar to the C-terminal region of the D. melanogaster hypothetical protein FR47. This protein has been found to consist of two N-acyltransferase-like domains swapped with the C-terminal strands.


Pssm-ID: 117022 [Multi-domain]  Cd Length: 86  Bit Score: 37.31  E-value: 1.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488981568   78 IGTVMTEPDHRNKGLAGQLIHHILQDWQQEADAFFLFANPT---TVDFYPKFGFTRSEEYQYI 137
Cdd:pfam08445  24 LGALQTLPEHRRRGLGSRLVAALARGIAERGITPFAVVVAGntpSRRLYEKLGFRKIDETYWV 86
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
31-134 2.93e-03

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 37.67  E-value: 2.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981568  31 FEEWYQQGYwtdayipYAFV--ERNKVIANASANIIDLRwqgEPRRYIQIGTVMTEPDHRNKGLAGQLIHHILQDWQQ-- 106
Cdd:COG1247   44 FAAILAPGR-------PVLVaeEDGEVVGFASLGPFRPR---PAYRGTAEESIYVDPDARGRGIGRALLEALIERARArg 113

                         90       100       110
                 ....*....|....*....|....*....|
gi 488981568 107 --EADAFFLFANPTTVDFYPKFGFTRSEEY 134
Cdd:COG1247  114 yrRLVAVVLADNEASIALYEKLGFEEVGTL 143
GNAT_acetyltran pfam12746
GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance ...
 76-135 8.77e-03

GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance proteins, whereas others are listed as being GNAT acetyltransferases. The family has similarities to the GNAT acetyltransferase family.


Pssm-ID: 403833  Cd Length: 239  Bit Score: 36.87  E-value: 8.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488981568   76 IQIGTvmtEPDHRNKGLA----GQLIHHILQ-----DWqqeaDAfflfANPTTVDFYPKFGFTRSEEYQ 135
Cdd:pfam12746 180 IEIDT---HPDYRGKGLAticaAALILECLKrglypSW----DA----HNEASVALAEKLGYEFVKEYT 237
 
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