Mycothiol acetyltransferase

Details

Name
Mycothiol acetyltransferase
Synonyms
  • 2.3.1.189
  • MSH acetyltransferase
  • Mycothiol synthase
Gene Name
mshD
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Amino acid sequence
>lcl|BSEQ0051157|Mycothiol acetyltransferase
MTALDWRSALTADEQRSVRALVTATTAVDGVAPVGEQVLRELGQQRTEHLLVAGSRPGGP
IIGYLNLSPPRGAGGAMAELVVHPQSRRRGIGTAMARAALAKTAGRNQFWAHGTLDPARA
TASALGLVGVRELIQMRRPLRDIPEPTIPDGVVIRTYAGTSDDAELLRVNNAAFAGHPEQ
GGWTAVQLAERRGEAWFDPDGLILAFGDSPRERPGRLLGFHWTKVHPDHPGLGEVYVLGV
DPAAQRRGLGQMLTSIGIVSLARRLGGRKTLDPAVEPAVLLYVESDNVAAVRTYQSLGFT
TYSVDTAYALAGTDN
Number of residues
315
Molecular Weight
33598.82
Theoretical pI
Not Available
GO Classification
Functions
mycothiol synthase activity / N-acetyltransferase activity
Processes
growth of symbiont in host cell / mycothiol biosynthetic process / response to stress
Components
cytosol
General Function
Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Specific Function
Mycothiol synthase activity
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0051158|Mycothiol acetyltransferase (mshD)
GTGACGGCGCTTGACTGGCGCTCCGCTCTGACCGCCGACGAGCAGCGCAGCGTGCGTGCA
CTGGTCACGGCGACAACAGCAGTCGATGGGGTAGCACCCGTGGGTGAACAGGTGCTGCGG
GAACTGGGCCAGCAACGCACCGAGCATCTGCTGGTGGCCGGTTCGCGACCGGGCGGCCCG
ATCATCGGCTACCTCAACCTCAGCCCACCCCGGGGCGCGGGTGGTGCGATGGCGGAGTTG
GTGGTGCATCCGCAGTCTCGACGGCGCGGTATCGGCACCGCCATGGCCCGCGCGGCATTG
GCCAAGACCGCCGGCCGCAACCAGTTCTGGGCGCACGGCACGCTGGATCCCGCTCGGGCG
ACCGCGTCCGCGCTGGGTCTGGTCGGCGTCCGCGAACTGATCCAGATGCGACGCCCGCTG
CGTGATATCCCCGAACCGACGATCCCCGACGGGGTGGTGATCCGCACCTACGCGGGCACG
TCCGACGACGCTGAGCTACTCCGGGTCAACAACGCCGCGTTCGCCGGACACCCGGAACAG
GGTGGGTGGACCGCGGTCCAGCTTGCCGAGCGGCGTGGCGAGGCGTGGTTCGATCCAGAC
GGCCTGATCTTGGCCTTCGGTGATTCGCCACGTGAACGGCCTGGCCGGTTGCTGGGTTTC
CATTGGACCAAAGTGCATCCCGATCACCCGGGATTGGGCGAGGTGTACGTGCTGGGCGTC
GATCCGGCGGCGCAGCGCCGCGGTCTCGGCCAGATGTTGACGTCGATCGGTATCGTCTCG
CTGGCCCGTCGGCTGGGCGGTCGGAAGACCCTCGACCCTGCGGTCGAACCCGCCGTGCTG
CTCTACGTGGAGTCGGACAATGTGGCGGCCGTGCGAACCTACCAGAGCCTGGGCTTCACC
ACCTACAGCGTCGATACCGCCTACGCGCTGGCTGGCACGGATAACTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP9WJM7
UniProtKB Entry NameMSHD_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. Koledin T, Newton GL, Fahey RC: Identification of the mycothiol synthase gene (mshD) encoding the acetyltransferase producing mycothiol in actinomycetes. Arch Microbiol. 2002 Nov;178(5):331-7. Epub 2002 Aug 15. [Article]
  3. 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]
  4. 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]
  5. Vetting MW, Roderick SL, Yu M, Blanchard JS: Crystal structure of mycothiol synthase (Rv0819) from Mycobacterium tuberculosis shows structural homology to the GNAT family of N-acetyltransferases. Protein Sci. 2003 Sep;12(9):1954-9. [Article]
  6. Vetting MW, Yu M, Rendle PM, Blanchard JS: The substrate-induced conformational change of Mycobacterium tuberculosis mycothiol synthase. J Biol Chem. 2006 Feb 3;281(5):2795-802. Epub 2005 Dec 2. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01992Coenzyme Ainvestigational, nutraceuticalunknownDetails