Cyclopropane mycolic acid synthase MmaA2

Details

Name
Cyclopropane mycolic acid synthase MmaA2
Synonyms
  • 2.1.1.79
  • AdoMet-MT
  • CFA synthase
  • CMAS
  • Cyclopropane-fatty-acyl-phospholipid synthase
  • MA-MT
  • mma2
  • Mycolic acid methyltransferase
  • S-adenosylmethionine-dependent methyltransferase
  • SAM-MT
Gene Name
mmaA2
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Amino acid sequence
>lcl|BSEQ0011791|Cyclopropane mycolic acid synthase MmaA2
MVNDLTPHFEDVQAHYDLSDDFFRLFLDPTQTYSCAHFEREDMTLEEAQIAKIDLALGKL
GLQPGMTLLDIGCGWGATMRRAIAQYDVNVVGLTLSKNQAAHVQKSFDEMDTPRDRRVLL
AGWEQFNEPVDRIVSIGAFEHFGHDRHADFFARAHKILPPDGVLLLHTITGLTRQQMVDH
GLPLTLWLARFLKFIATEIFPGGQPPTIEMVEEQSAKTGFTLTRRQSLQPHYARTLDLWA
EALQEHKSEAIAIQSEEVYERYMKYLTGCAKLFRVGYIDVNQFTLAK
Number of residues
287
Molecular Weight
32724.06
Theoretical pI
5.73
GO Classification
Functions
cyclopropane-fatty-acyl-phospholipid synthase activity / methyltransferase activity
Processes
mycolic acid biosynthetic process
Components
cell wall / plasma membrane
General Function
Methyltransferase activity
Specific Function
Catalyzes the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. MmaA2 also catalyzes the biosynthesis of the cis-cyclopropanated methoxymycolates. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0011792|Cyclopropane mycolic acid synthase MmaA2 (mmaA2)
ATGGTCAACGACCTAACGCCGCACTTCGAGGACGTGCAGGCACACTACGACCTGTCCGAC
GACTTCTTCCGGCTGTTCCTGGATCCGACCCAGACCTACAGCTGCGCGCATTTCGAACGC
GAGGACATGACGCTGGAAGAGGCCCAGATCGCCAAGATCGACCTGGCGCTGGGCAAGCTA
GGTCTGCAGCCCGGCATGACGCTGCTCGATATCGGTTGCGGCTGGGGCGCCACCATGCGG
CGCGCGATCGCGCAGTATGACGTCAACGTCGTCGGCCTGACATTGTCGAAGAACCAGGCC
GCCCATGTGCAGAAGTCGTTCGACGAGATGGACACCCCGCGCGACAGGCGAGTGTTGCTG
GCGGGATGGGAGCAGTTCAACGAGCCCGTCGACCGCATCGTGTCGATCGGCGCGTTCGAG
CACTTCGGCCACGATCGTCACGCCGACTTCTTCGCCCGGGCCCACAAAATCCTGCCGCCC
GATGGCGTGTTGCTGCTGCACACGATCACCGGCCTGACCAGGCAGCAGATGGTCGACCAC
GGCTTGCCGCTCACGTTGTGGCTGGCCCGCTTTCTCAAGTTCATCGCGACCGAAATCTTC
CCGGGGGGCCAACCTCCGACGATTGAAATGGTTGAGGAACAGTCGGCGAAGACGGGTTTC
ACGCTGACTCGCCGCCAGTCGCTGCAGCCGCATTACGCCAGGACCCTCGACCTGTGGGCC
GAGGCGCTGCAGGAACACAAAAGCGAGGCCATCGCGATCCAGTCCGAAGAGGTCTACGAG
CGGTACATGAAATACCTGACCGGCTGCGCCAAGCTGTTCCGGGTCGGCTACATCGACGTC
AACCAGTTCACGCTGGCGAAGTAG
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDQ79FX6
UniProtKB Entry NameMMAA2_MYCTU
GenBank Gene IDBX842574
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. [PubMed:9634230]
  2. Glickman MS: The mmaA2 gene of Mycobacterium tuberculosis encodes the distal cyclopropane synthase of the alpha-mycolic acid. J Biol Chem. 2003 Mar 7;278(10):7844-9. Epub 2002 Dec 26. [PubMed:12502719]
  3. Alahari A, Trivelli X, Guerardel Y, Dover LG, Besra GS, Sacchettini JC, Reynolds RC, Coxon GD, Kremer L: Thiacetazone, an antitubercular drug that inhibits cyclopropanation of cell wall mycolic acids in mycobacteria. PLoS One. 2007 Dec 19;2(12):e1343. [PubMed:18094751]
  4. 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. [PubMed:19099550]
  5. Vaubourgeix J, Bardou F, Boissier F, Julien S, Constant P, Ploux O, Daffe M, Quemard A, Mourey L: S-adenosyl-N-decyl-aminoethyl, a potent bisubstrate inhibitor of mycobacterium tuberculosis mycolic acid methyltransferases. J Biol Chem. 2009 Jul 17;284(29):19321-30. doi: 10.1074/jbc.M809599200. Epub 2009 May 13. [PubMed:19439410]
  6. Barkan D, Rao V, Sukenick GD, Glickman MS: Redundant function of cmaA2 and mmaA2 in Mycobacterium tuberculosis cis cyclopropanation of oxygenated mycolates. J Bacteriol. 2010 Jul;192(14):3661-8. doi: 10.1128/JB.00312-10. Epub 2010 May 14. [PubMed:20472794]
  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. [PubMed:21969609]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01718CetrimoniumapprovedunknownDetails
DB01752S-adenosyl-L-homocysteineexperimentalunknownDetails