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Conserved domains on  [gi|219416|dbj|BAA14096|]
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arylamine N-acetyltransferase [Homo sapiens]

Protein Classification

arylamine N-acetyltransferase( domain architecture ID 10466656)

arylamine N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl coenzyme A (CoA) to the nitrogen or oxygen atom of a wide variety of aromatic amines (arylamines) and hydrazines

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Acetyltransf_2 pfam00797
N-acetyltransferase; Arylamine N-acetyltransferase (NAT) is a cytosolic enzyme of ...
20-280 2.06e-111

N-acetyltransferase; Arylamine N-acetyltransferase (NAT) is a cytosolic enzyme of approximately 30kDa. It facilitates the transfer of an acetyl group from Acetyl Coenzyme A on to a wide range of arylamine, N-hydroxyarylamines and hydrazines. Acetylation of these compounds generally results in inactivation. NAT is found in many species from Mycobacteria (M. tuberculosis, M. smegmatis etc) to man. It was the first enzyme to be observed to have polymorphic activity amongst human individuals. NAT is responsible for the inactivation of Isoniazid (a drug used to treat Tuberculosis) in humans. The NAT protein has also been shown to be involved in the breakdown of folic acid.


:

Pssm-ID: 395644  Cd Length: 240  Bit Score: 321.53  E-value: 2.06e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219416      20 DLETLTDILEHQIRAVPFENLNMHCGQAMELGLEAIFDHIVRRNRGGWCLQVNQLLYWALTTIGFQTTMLGGYFYIPPVN 99
Cdd:pfam00797   1 DLETLRELHLHHLRAIPFENLDVHLGEPISLDLEALFDKLVHKRRGGYCYELNGLFYWVLTELGFDVTLLGGRVYWPRPG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219416     100 KYSTGMVHLLLQVTIDGRNYIVDAGSGSSSqMWQPLELISGKDQPQVPCIFCLTEER-GIWYLDQIRREQYitnkeflns 178
Cdd:pfam00797  81 AYSTPQTHLLLLVTIDGETYLVDVGFGGST-LWAPLELISGKDQPTPHGIFRLVEEGgGTWYLEKDGRDGW--------- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219416     179 hllpkkkhQKIYLFTLEPRTIEDFESMNTYLQTSPTSSFITTSFCSLQTPEGVYCLVGFILTYRkfnYKDNTdLVEFKTL 258
Cdd:pfam00797 151 --------VPLYSFTLEPRQIEDFEVGNDYLQTSPDSHFTTHLLCSRQTPDGRLTLTGRTLTLR---YKDGA-LVEIRLL 218
                         250       260
                  ....*....|....*....|..
gi 219416     259 TEEEVEEVLKNIFKISLGRNLV 280
Cdd:pfam00797 219 TDEEVEDVLKERFGIELDAKLV 240
 
Name Accession Description Interval E-value
Acetyltransf_2 pfam00797
N-acetyltransferase; Arylamine N-acetyltransferase (NAT) is a cytosolic enzyme of ...
20-280 2.06e-111

N-acetyltransferase; Arylamine N-acetyltransferase (NAT) is a cytosolic enzyme of approximately 30kDa. It facilitates the transfer of an acetyl group from Acetyl Coenzyme A on to a wide range of arylamine, N-hydroxyarylamines and hydrazines. Acetylation of these compounds generally results in inactivation. NAT is found in many species from Mycobacteria (M. tuberculosis, M. smegmatis etc) to man. It was the first enzyme to be observed to have polymorphic activity amongst human individuals. NAT is responsible for the inactivation of Isoniazid (a drug used to treat Tuberculosis) in humans. The NAT protein has also been shown to be involved in the breakdown of folic acid.


Pssm-ID: 395644  Cd Length: 240  Bit Score: 321.53  E-value: 2.06e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219416      20 DLETLTDILEHQIRAVPFENLNMHCGQAMELGLEAIFDHIVRRNRGGWCLQVNQLLYWALTTIGFQTTMLGGYFYIPPVN 99
Cdd:pfam00797   1 DLETLRELHLHHLRAIPFENLDVHLGEPISLDLEALFDKLVHKRRGGYCYELNGLFYWVLTELGFDVTLLGGRVYWPRPG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219416     100 KYSTGMVHLLLQVTIDGRNYIVDAGSGSSSqMWQPLELISGKDQPQVPCIFCLTEER-GIWYLDQIRREQYitnkeflns 178
Cdd:pfam00797  81 AYSTPQTHLLLLVTIDGETYLVDVGFGGST-LWAPLELISGKDQPTPHGIFRLVEEGgGTWYLEKDGRDGW--------- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219416     179 hllpkkkhQKIYLFTLEPRTIEDFESMNTYLQTSPTSSFITTSFCSLQTPEGVYCLVGFILTYRkfnYKDNTdLVEFKTL 258
Cdd:pfam00797 151 --------VPLYSFTLEPRQIEDFEVGNDYLQTSPDSHFTTHLLCSRQTPDGRLTLTGRTLTLR---YKDGA-LVEIRLL 218
                         250       260
                  ....*....|....*....|..
gi 219416     259 TEEEVEEVLKNIFKISLGRNLV 280
Cdd:pfam00797 219 TDEEVEDVLKERFGIELDAKLV 240
NhoA COG2162
Arylamine N-acetyltransferase [Secondary metabolites biosynthesis, transport and catabolism];
1-242 1.01e-66

Arylamine N-acetyltransferase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441765  Cd Length: 256  Bit Score: 208.58  E-value: 1.01e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219416     1 MDIEAYFERIGYKNSRnKLDLETLTDILEHQIRAVPFENLNMHCGQAMELGLEAIFDHIVRRNRGGWCLQVNQLLYWALT 80
Cdd:COG2162   3 FDLDAYLARIGYSGPP-APTLETLRALHRAHVRAIPFENLDVLLGRPISLDPDALFDKLVRRRRGGYCYELNGLFAALLE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219416    81 TIGFQTTMLGGYFYIPPVNKYSTGMVHLLLQVTIDGRNYIVDAGSGSSSqMWQPLELISGKDQPQVPCIFCLTEER-GIW 159
Cdd:COG2162  82 ALGFDVTLLAARVRWGGPGGPGPPRTHMALLVTLDGERWLVDVGFGGGT-PLEPLPLEDGTEQDQPGGTYRLVRSDdGEW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219416   160 YLDQIRREQYITnkeflnshllpkkkhqkIYLFTLEPRTIEDFESMNTYLQTSPTSSFITTSFCSLQTPEGVYCLVGFIL 239
Cdd:COG2162 161 VLQRRVDGGWRP-----------------LYRFDLEPQELADFEVANWYTSTHPDSPFVGNLLVARATPDGRVTLRGRRL 223

                ...
gi 219416   240 TYR 242
Cdd:COG2162 224 TRR 226
PRK15047 PRK15047
N-hydroxyarylamine O-acetyltransferase; Provisional
3-169 3.59e-12

N-hydroxyarylamine O-acetyltransferase; Provisional


Pssm-ID: 185007  Cd Length: 281  Bit Score: 65.25  E-value: 3.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219416      3 IEAYFERIGYKNSrNKLDLETLTDILEHQIRAVPFENLNMHCGQAMELGLEAIFDHIVRRNRGGWCLQVNQLLYWALTTI 82
Cdd:PRK15047   5 LNAYFARINWSGA-AAVNIDTLRALHLKHNCTIPFENLDVLLPREIQLDDQSLEEKLVIARRGGYCFEQNGLFERVLREL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219416     83 GFQTTMLGGYFYI--PPVNKYSTgmvHLLLQVTIDGRNYIVDAGSGSSSqMWQPLELISGKDQPQVPCIFCLTEERGIWY 160
Cdd:PRK15047  84 GFNVRSLLGRVVLsnPPALPPRT---HRLLLVELEGEKWIADVGFGGQT-LTAPIRLVADIVQTTPHGEYRLLQEGDDWV 159

                 ....*....
gi 219416    161 LdQIRREQY 169
Cdd:PRK15047 160 L-QFNHHQH 167
 
Name Accession Description Interval E-value
Acetyltransf_2 pfam00797
N-acetyltransferase; Arylamine N-acetyltransferase (NAT) is a cytosolic enzyme of ...
20-280 2.06e-111

N-acetyltransferase; Arylamine N-acetyltransferase (NAT) is a cytosolic enzyme of approximately 30kDa. It facilitates the transfer of an acetyl group from Acetyl Coenzyme A on to a wide range of arylamine, N-hydroxyarylamines and hydrazines. Acetylation of these compounds generally results in inactivation. NAT is found in many species from Mycobacteria (M. tuberculosis, M. smegmatis etc) to man. It was the first enzyme to be observed to have polymorphic activity amongst human individuals. NAT is responsible for the inactivation of Isoniazid (a drug used to treat Tuberculosis) in humans. The NAT protein has also been shown to be involved in the breakdown of folic acid.


Pssm-ID: 395644  Cd Length: 240  Bit Score: 321.53  E-value: 2.06e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219416      20 DLETLTDILEHQIRAVPFENLNMHCGQAMELGLEAIFDHIVRRNRGGWCLQVNQLLYWALTTIGFQTTMLGGYFYIPPVN 99
Cdd:pfam00797   1 DLETLRELHLHHLRAIPFENLDVHLGEPISLDLEALFDKLVHKRRGGYCYELNGLFYWVLTELGFDVTLLGGRVYWPRPG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219416     100 KYSTGMVHLLLQVTIDGRNYIVDAGSGSSSqMWQPLELISGKDQPQVPCIFCLTEER-GIWYLDQIRREQYitnkeflns 178
Cdd:pfam00797  81 AYSTPQTHLLLLVTIDGETYLVDVGFGGST-LWAPLELISGKDQPTPHGIFRLVEEGgGTWYLEKDGRDGW--------- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219416     179 hllpkkkhQKIYLFTLEPRTIEDFESMNTYLQTSPTSSFITTSFCSLQTPEGVYCLVGFILTYRkfnYKDNTdLVEFKTL 258
Cdd:pfam00797 151 --------VPLYSFTLEPRQIEDFEVGNDYLQTSPDSHFTTHLLCSRQTPDGRLTLTGRTLTLR---YKDGA-LVEIRLL 218
                         250       260
                  ....*....|....*....|..
gi 219416     259 TEEEVEEVLKNIFKISLGRNLV 280
Cdd:pfam00797 219 TDEEVEDVLKERFGIELDAKLV 240
NhoA COG2162
Arylamine N-acetyltransferase [Secondary metabolites biosynthesis, transport and catabolism];
1-242 1.01e-66

Arylamine N-acetyltransferase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441765  Cd Length: 256  Bit Score: 208.58  E-value: 1.01e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219416     1 MDIEAYFERIGYKNSRnKLDLETLTDILEHQIRAVPFENLNMHCGQAMELGLEAIFDHIVRRNRGGWCLQVNQLLYWALT 80
Cdd:COG2162   3 FDLDAYLARIGYSGPP-APTLETLRALHRAHVRAIPFENLDVLLGRPISLDPDALFDKLVRRRRGGYCYELNGLFAALLE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219416    81 TIGFQTTMLGGYFYIPPVNKYSTGMVHLLLQVTIDGRNYIVDAGSGSSSqMWQPLELISGKDQPQVPCIFCLTEER-GIW 159
Cdd:COG2162  82 ALGFDVTLLAARVRWGGPGGPGPPRTHMALLVTLDGERWLVDVGFGGGT-PLEPLPLEDGTEQDQPGGTYRLVRSDdGEW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219416   160 YLDQIRREQYITnkeflnshllpkkkhqkIYLFTLEPRTIEDFESMNTYLQTSPTSSFITTSFCSLQTPEGVYCLVGFIL 239
Cdd:COG2162 161 VLQRRVDGGWRP-----------------LYRFDLEPQELADFEVANWYTSTHPDSPFVGNLLVARATPDGRVTLRGRRL 223

                ...
gi 219416   240 TYR 242
Cdd:COG2162 224 TRR 226
PRK15047 PRK15047
N-hydroxyarylamine O-acetyltransferase; Provisional
3-169 3.59e-12

N-hydroxyarylamine O-acetyltransferase; Provisional


Pssm-ID: 185007  Cd Length: 281  Bit Score: 65.25  E-value: 3.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219416      3 IEAYFERIGYKNSrNKLDLETLTDILEHQIRAVPFENLNMHCGQAMELGLEAIFDHIVRRNRGGWCLQVNQLLYWALTTI 82
Cdd:PRK15047   5 LNAYFARINWSGA-AAVNIDTLRALHLKHNCTIPFENLDVLLPREIQLDDQSLEEKLVIARRGGYCFEQNGLFERVLREL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219416     83 GFQTTMLGGYFYI--PPVNKYSTgmvHLLLQVTIDGRNYIVDAGSGSSSqMWQPLELISGKDQPQVPCIFCLTEERGIWY 160
Cdd:PRK15047  84 GFNVRSLLGRVVLsnPPALPPRT---HRLLLVELEGEKWIADVGFGGQT-LTAPIRLVADIVQTTPHGEYRLLQEGDDWV 159

                 ....*....
gi 219416    161 LdQIRREQY 169
Cdd:PRK15047 160 L-QFNHHQH 167
 
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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