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
- Functionsarylamine N-acetyltransferase activityProcessesmetabolic process / response to antibioticComponentsplasma 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
- Acetyltransf_2 (PF00797)
- 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
Resource Link UniProtKB ID P9WJI5 UniProtKB Entry Name NAT_MYCTU - General References
- 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]
- 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]
- 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]
- 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]
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- 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]
- 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]
- 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]