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Conserved domains on  [gi|723588163|ref|WP_033567071|]
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MULTISPECIES: N-hydroxyarylamine O-acetyltransferase [Salmonella]

Protein Classification

N-hydroxyarylamine O-acetyltransferase( domain architecture ID 10014950)

N-hydroxyarylamine O-acetyltransferase catalyzes both the acetyl-CoA-dependent N-acetylation of aromatic amines and the O-acetylation of N-hydroxyarylamines

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK15047 PRK15047
N-hydroxyarylamine O-acetyltransferase; Provisional
1-281 0e+00

N-hydroxyarylamine O-acetyltransferase; Provisional


:

Pssm-ID: 185007  Cd Length: 281  Bit Score: 544.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723588163   1 MTSFLHAYFTRLHCQPLGVPTVEALRTLHLAHNCAIPFENLDVLLPREIQLDETALEEKLLYARRGGYCFELNGLFERAL 80
Cdd:PRK15047   1 MTPFLNAYFARINWSGAAAVNIDTLRALHLKHNCTIPFENLDVLLPREIQLDDQSLEEKLVIARRGGYCFEQNGLFERVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723588163  81 RDIGFNVRSLLGRVILSHPASLPPRTHRLLLVDVEDEQWIADVGFGGQTLTAPLRLQAEIAQQTPHCEYRLMQEGSTWIL 160
Cdd:PRK15047  81 RELGFNVRSLLGRVVLSNPPALPPRTHRLLLVELEGEKWIADVGFGGQTLTAPIRLVADIVQTTPHGEYRLLQEGDDWVL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723588163 161 QFRHHEHWQSMYCFDLGVQQQSDHVMGNFWSAHWPQSHFRHHLLMCRHLPDGGKLTLTNFHFTRYHQGHAVEQVNVPDVP 240
Cdd:PRK15047 161 QFNHHQHWQSMYRFDLCEQQQSDYVMGNFWSAHWPQSHFRHHLLMCRHLPDGGKLTLTNFHFTHYENGHAVEQRNLPDVA 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 723588163 241 SLYQLLQQQFGLGVNDVKHGFTEAELAAVMAAFDTHPEAGK 281
Cdd:PRK15047 241 SLYAVMQEQFGLGVDDAKHGFTVAELAAVMAAFDTHPEAGK 281
 
Name Accession Description Interval E-value
PRK15047 PRK15047
N-hydroxyarylamine O-acetyltransferase; Provisional
1-281 0e+00

N-hydroxyarylamine O-acetyltransferase; Provisional


Pssm-ID: 185007  Cd Length: 281  Bit Score: 544.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723588163   1 MTSFLHAYFTRLHCQPLGVPTVEALRTLHLAHNCAIPFENLDVLLPREIQLDETALEEKLLYARRGGYCFELNGLFERAL 80
Cdd:PRK15047   1 MTPFLNAYFARINWSGAAAVNIDTLRALHLKHNCTIPFENLDVLLPREIQLDDQSLEEKLVIARRGGYCFEQNGLFERVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723588163  81 RDIGFNVRSLLGRVILSHPASLPPRTHRLLLVDVEDEQWIADVGFGGQTLTAPLRLQAEIAQQTPHCEYRLMQEGSTWIL 160
Cdd:PRK15047  81 RELGFNVRSLLGRVVLSNPPALPPRTHRLLLVELEGEKWIADVGFGGQTLTAPIRLVADIVQTTPHGEYRLLQEGDDWVL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723588163 161 QFRHHEHWQSMYCFDLGVQQQSDHVMGNFWSAHWPQSHFRHHLLMCRHLPDGGKLTLTNFHFTRYHQGHAVEQVNVPDVP 240
Cdd:PRK15047 161 QFNHHQHWQSMYRFDLCEQQQSDYVMGNFWSAHWPQSHFRHHLLMCRHLPDGGKLTLTNFHFTHYENGHAVEQRNLPDVA 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 723588163 241 SLYQLLQQQFGLGVNDVKHGFTEAELAAVMAAFDTHPEAGK 281
Cdd:PRK15047 241 SLYAVMQEQFGLGVDDAKHGFTVAELAAVMAAFDTHPEAGK 281
Acetyltransf_2 pfam00797
N-acetyltransferase; Arylamine N-acetyltransferase (NAT) is a cytosolic enzyme of ...
21-255 7.20e-110

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: 317.30  E-value: 7.20e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723588163   21 TVEALRTLHLAHNCAIPFENLDVLLPREIQLDETALEEKLLYARRGGYCFELNGLFERALRDIGFNVRSLLGRVILSHP- 99
Cdd:pfam00797   1 DLETLRELHLHHLRAIPFENLDVHLGEPISLDLEALFDKLVHKRRGGYCYELNGLFYWVLTELGFDVTLLGGRVYWPRPg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723588163  100 ASLPPRTHRLLLVDVEDEQWIADVGFGGQTLTAPLRLQAEIAQQTPHCEYRLMQEGS-TWILQFRHHEHWQSMYCFDLGV 178
Cdd:pfam00797  81 AYSTPQTHLLLLVTIDGETYLVDVGFGGSTLWAPLELISGKDQPTPHGIFRLVEEGGgTWYLEKDGRDGWVPLYSFTLEP 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 723588163  179 QQQSDHVMGNFWSAHWPQSHFRHHLLMCRHLPDgGKLTLTNFHFTRYHQGHAVEQVNVPDVPSLYQLLQQQFGLGVN 255
Cdd:pfam00797 161 RQIEDFEVGNDYLQTSPDSHFTTHLLCSRQTPD-GRLTLTGRTLTLRYKDGALVEIRLLTDEEVEDVLKERFGIELD 236
NhoA COG2162
Arylamine N-acetyltransferase [Secondary metabolites biosynthesis, transport and catabolism];
2-256 3.03e-108

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


Pssm-ID: 441765  Cd Length: 256  Bit Score: 313.74  E-value: 3.03e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723588163   2 TSFLHAYFTRLHCQPLGVPTVEALRTLHLAHNCAIPFENLDVLLPREIQLDETALEEKLLYARRGGYCFELNGLFERALR 81
Cdd:COG2162    2 AFDLDAYLARIGYSGPPAPTLETLRALHRAHVRAIPFENLDVLLGRPISLDPDALFDKLVRRRRGGYCYELNGLFAALLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723588163  82 DIGFNVRSLLGRVILSHP-ASLPPRTHRLLLVDVEDEQWIADVGFGGQTLTAPLRLQAEIAQQTPHCEYRLMQE-GSTWI 159
Cdd:COG2162   82 ALGFDVTLLAARVRWGGPgGPGPPRTHMALLVTLDGERWLVDVGFGGGTPLEPLPLEDGTEQDQPGGTYRLVRSdDGEWV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723588163 160 LQFRHHEHWQSMYCFDLGVQQQSDHVMGNFWSAHWPQSHFRHHLLMCRHLPDgGKLTLTNFHFTRYHQGHAVEQVnVPDV 239
Cdd:COG2162  162 LQRRVDGGWRPLYRFDLEPQELADFEVANWYTSTHPDSPFVGNLLVARATPD-GRVTLRGRRLTRRRGGGEEERT-LLSA 239
                        250
                 ....*....|....*..
gi 723588163 240 PSLYQLLQQQFGLGVND 256
Cdd:COG2162  240 EELAAVLRERFGLDLDD 256
 
Name Accession Description Interval E-value
PRK15047 PRK15047
N-hydroxyarylamine O-acetyltransferase; Provisional
1-281 0e+00

N-hydroxyarylamine O-acetyltransferase; Provisional


Pssm-ID: 185007  Cd Length: 281  Bit Score: 544.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723588163   1 MTSFLHAYFTRLHCQPLGVPTVEALRTLHLAHNCAIPFENLDVLLPREIQLDETALEEKLLYARRGGYCFELNGLFERAL 80
Cdd:PRK15047   1 MTPFLNAYFARINWSGAAAVNIDTLRALHLKHNCTIPFENLDVLLPREIQLDDQSLEEKLVIARRGGYCFEQNGLFERVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723588163  81 RDIGFNVRSLLGRVILSHPASLPPRTHRLLLVDVEDEQWIADVGFGGQTLTAPLRLQAEIAQQTPHCEYRLMQEGSTWIL 160
Cdd:PRK15047  81 RELGFNVRSLLGRVVLSNPPALPPRTHRLLLVELEGEKWIADVGFGGQTLTAPIRLVADIVQTTPHGEYRLLQEGDDWVL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723588163 161 QFRHHEHWQSMYCFDLGVQQQSDHVMGNFWSAHWPQSHFRHHLLMCRHLPDGGKLTLTNFHFTRYHQGHAVEQVNVPDVP 240
Cdd:PRK15047 161 QFNHHQHWQSMYRFDLCEQQQSDYVMGNFWSAHWPQSHFRHHLLMCRHLPDGGKLTLTNFHFTHYENGHAVEQRNLPDVA 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 723588163 241 SLYQLLQQQFGLGVNDVKHGFTEAELAAVMAAFDTHPEAGK 281
Cdd:PRK15047 241 SLYAVMQEQFGLGVDDAKHGFTVAELAAVMAAFDTHPEAGK 281
Acetyltransf_2 pfam00797
N-acetyltransferase; Arylamine N-acetyltransferase (NAT) is a cytosolic enzyme of ...
21-255 7.20e-110

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: 317.30  E-value: 7.20e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723588163   21 TVEALRTLHLAHNCAIPFENLDVLLPREIQLDETALEEKLLYARRGGYCFELNGLFERALRDIGFNVRSLLGRVILSHP- 99
Cdd:pfam00797   1 DLETLRELHLHHLRAIPFENLDVHLGEPISLDLEALFDKLVHKRRGGYCYELNGLFYWVLTELGFDVTLLGGRVYWPRPg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723588163  100 ASLPPRTHRLLLVDVEDEQWIADVGFGGQTLTAPLRLQAEIAQQTPHCEYRLMQEGS-TWILQFRHHEHWQSMYCFDLGV 178
Cdd:pfam00797  81 AYSTPQTHLLLLVTIDGETYLVDVGFGGSTLWAPLELISGKDQPTPHGIFRLVEEGGgTWYLEKDGRDGWVPLYSFTLEP 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 723588163  179 QQQSDHVMGNFWSAHWPQSHFRHHLLMCRHLPDgGKLTLTNFHFTRYHQGHAVEQVNVPDVPSLYQLLQQQFGLGVN 255
Cdd:pfam00797 161 RQIEDFEVGNDYLQTSPDSHFTTHLLCSRQTPD-GRLTLTGRTLTLRYKDGALVEIRLLTDEEVEDVLKERFGIELD 236
NhoA COG2162
Arylamine N-acetyltransferase [Secondary metabolites biosynthesis, transport and catabolism];
2-256 3.03e-108

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


Pssm-ID: 441765  Cd Length: 256  Bit Score: 313.74  E-value: 3.03e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723588163   2 TSFLHAYFTRLHCQPLGVPTVEALRTLHLAHNCAIPFENLDVLLPREIQLDETALEEKLLYARRGGYCFELNGLFERALR 81
Cdd:COG2162    2 AFDLDAYLARIGYSGPPAPTLETLRALHRAHVRAIPFENLDVLLGRPISLDPDALFDKLVRRRRGGYCYELNGLFAALLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723588163  82 DIGFNVRSLLGRVILSHP-ASLPPRTHRLLLVDVEDEQWIADVGFGGQTLTAPLRLQAEIAQQTPHCEYRLMQE-GSTWI 159
Cdd:COG2162   82 ALGFDVTLLAARVRWGGPgGPGPPRTHMALLVTLDGERWLVDVGFGGGTPLEPLPLEDGTEQDQPGGTYRLVRSdDGEWV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723588163 160 LQFRHHEHWQSMYCFDLGVQQQSDHVMGNFWSAHWPQSHFRHHLLMCRHLPDgGKLTLTNFHFTRYHQGHAVEQVnVPDV 239
Cdd:COG2162  162 LQRRVDGGWRPLYRFDLEPQELADFEVANWYTSTHPDSPFVGNLLVARATPD-GRVTLRGRRLTRRRGGGEEERT-LLSA 239
                        250
                 ....*....|....*..
gi 723588163 240 PSLYQLLQQQFGLGVND 256
Cdd:COG2162  240 EELAAVLRERFGLDLDD 256
 
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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