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
- Functionscyclopropane-fatty-acyl-phospholipid synthase activity / methyltransferase activityProcessesmycolic acid biosynthetic processComponentscell 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
- CMAS (PF02353)
- 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
Resource Link UniProtKB ID Q79FX6 UniProtKB Entry Name MMAA2_MYCTU GenBank Gene ID BX842574 - 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]
- 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. [Article]
- 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. [Article]
- 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]
- 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. [Article]
- 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. [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]