Arylamine N-acetyltransferase

Details

Name
Arylamine N-acetyltransferase
Synonyms
  • 2.3.1.5
  • NAT
  • nhoA
  • tbnat
Gene Name
nat
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Amino acid sequence
>lcl|BSEQ0051280|Arylamine N-acetyltransferase
MALDLTAYFDRINYRGATDPTLDVLQDLVTVHSRTIPFENLDPLLGVPVDDLSPQALADK
LVLRRRGGYCFEHNGLMGYVLAELGYRVRRFAARVVWKLAPDAPLPPQTHTLLGVTFPGS
GGCYLVDVGFGGQTPTSPLRLETGAVQPTTHEPYRLEDRVDGFVLQAMVRDTWQTLYEFT
TQTRPQIDLKVASWYASTHPASKFVTGLTAAVITDDARWNLSGRDLAVHRAGGTEKIRLA
DAAAVVDTLSERFGINVADIGERGALETRIDELLARQPGADAP
Number of residues
283
Molecular Weight
31028.88
Theoretical pI
Not Available
GO Classification
Functions
arylamine N-acetyltransferase activity
Processes
metabolic process / response to antibiotic
Components
plasma membrane
General Function
Catalyzes the transfer of the acetyl group from acetyl coenzyme A to the free amino group of arylamines and hydrazines (PubMed:18795795). Is able to utilize not only acetyl-CoA, but also n-propionyl-CoA and acetoacetyl-CoA as acyl donors, although at a lower rate (PubMed:19014350). As acetyl-CoA and propionyl-CoA are products of cholesterol catabolism and the nat gene is likely present in the same operon than genes involved in cholesterol degradation, this enzyme could have a role in the utilization and regulation of these CoA species (PubMed:19014350).
Specific Function
Arylamine n-acetyltransferase activity
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0051281|Arylamine N-acetyltransferase (nat)
ATGGCACTGGATCTGACCGCGTACTTCGATCGCATCAACTATCGCGGCGCTACCGATCCA
ACCCTGGATGTTCTGCAGGATCTGGTGACCGTGCACAGTCGAACGATTCCGTTCGAGAAC
CTCGACCCGCTGCTGGGGGTGCCGGTCGACGACCTCAGTCCACAGGCGCTGGCCGACAAG
CTGGTACTTCGGCGCCGAGGCGGGTACTGCTTTGAGCACAACGGGCTGATGGGTTATGTG
CTGGCCGAACTCGGCTATCGGGTGCGCCGATTCGCCGCCCGCGTCGTCTGGAAGCTCGCG
CCGGACGCGCCCCTGCCGCCGCAGACGCACACCCTGCTGGGGGTCACGTTCCCCGGCTCG
GGCGGATGCTATCTCGTCGACGTCGGATTCGGCGGCCAAACACCGACCTCACCGCTTCGC
CTCGAAACCGGCGCCGTCCAGCCGACAACGCACGAACCTTATCGGCTCGAGGACCGCGTC
GACGGCTTTGTCTTGCAGGCGATGGTCCGGGACACATGGCAGACACTGTACGAATTCACC
ACCCAGACCCGCCCGCAGATCGATCTGAAAGTGGCCAGCTGGTACGCCTCAACACACCCG
GCATCGAAGTTCGTCACGGGACTGACCGCCGCGGTGATCACCGACGACGCCCGGTGGAAC
CTATCTGGCCGCGACCTTGCCGTTCACCGTGCCGGTGGTACCGAGAAGATCCGCCTTGCC
GATGCGGCAGCGGTTGTCGACACCCTGAGCGAACGGTTCGGGATCAACGTGGCAGATATC
GGCGAGCGCGGCGCGCTCGAGACGCGCATCGACGAGCTATTGGCTCGGCAGCCAGGAGCC
GATGCGCCGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP9WJI5
UniProtKB Entry NameNAT_MYCTU
General References
  1. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [Article]
  2. Camus JC, Pryor MJ, Medigue C, Cole ST: Re-annotation of the genome sequence of Mycobacterium tuberculosis H37Rv. Microbiology. 2002 Oct;148(Pt 10):2967-73. [Article]
  3. Payton M, Auty R, Delgoda R, Everett M, Sim E: Cloning and characterization of arylamine N-acetyltransferase genes from Mycobacterium smegmatis and Mycobacterium tuberculosis: increased expression results in isoniazid resistance. J Bacteriol. 1999 Feb;181(4):1343-7. [Article]
  4. Sikora AL, Frankel BA, Blanchard JS: Kinetic and chemical mechanism of arylamine N-acetyltransferase from Mycobacterium tuberculosis. Biochemistry. 2008 Oct 7;47(40):10781-9. doi: 10.1021/bi800398c. Epub 2008 Sep 17. [Article]
  5. Lack NA, Kawamura A, Fullam E, Laurieri N, Beard S, Russell AJ, Evangelopoulos D, Westwood I, Sim E: Temperature stability of proteins essential for the intracellular survival of Mycobacterium tuberculosis. Biochem J. 2009 Mar 1;418(2):369-78. doi: 10.1042/BJ20082011. [Article]
  6. Raman K, Yeturu K, Chandra N: targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis. BMC Syst Biol. 2008 Dec 19;2:109. doi: 10.1186/1752-0509-2-109. [Article]
  7. Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A: Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3. [Article]
  8. Coelho MB, Costa ER, Vasconcellos SE, Linck N, Ramos RM, Amorim HL, Suffys PN, Santos AR, Silva PE, Ramos DF, Silva MS, Rossetti ML: Sequence and structural characterization of tbnat gene in isoniazid-resistant Mycobacterium tuberculosis: identification of new mutations. Mutat Res. 2011 Jul 1;712(1-2):33-9. doi: 10.1016/j.mrfmmm.2011.03.017. Epub 2011 Apr 14. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00951Isoniazidapproved, investigationalunknowninhibitorDetails
DB00515CisplatinapprovedunknowninhibitorDetails
DB01582Sulfamethazineapproved, investigational, vet_approvedunknownsubstrateDetails