Hydroxymycolate synthase MmaA4
Details
- Name
- Hydroxymycolate synthase MmaA4
- Synonyms
- 2.1.1.-
- AdoMet-MT
- hma
- MA-MT
- mma4
- Mycolic acid methyltransferase
- S-adenosylmethionine-dependent methyltransferase
- SAM-MT
- Gene Name
- mmaA4
- Organism
- Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
- Amino acid sequence
>lcl|BSEQ0012694|Hydroxymycolate synthase MmaA4 MTRMAEKPISPTKTRTRFEDIQAHYDVSDDFFALFQDPTRTYSCAYFEPPELTLEEAQYA KVDLNLDKLDLKPGMTLLDIGCGWGTTMRRAVERFDVNVIGLTLSKNQHARCEQVLASID TNRSRQVLLQGWEDFAEPVDRIVSIEAFEHFGHENYDDFFKRCFNIMPADGRMTVQSSVS YHPYEMAARGKKLSFETARFIKFIVTEIFPGGRLPSTEMMVEHGEKAGFTVPEPLSLRPH YIKTLRIWGDTLQSNKDKAIEVTSEEVYNRYMKYLRGCEHYFTDEMLDCSLVTYLKPGAA A
- Number of residues
- 301
- Molecular Weight
- 34670.13
- Theoretical pI
- 5.44
- GO Classification
- Functionsmethyltransferase activity / S-adenosylmethionine-dependent methyltransferase activityProcessesmycolic acid biosynthetic processComponentscell wall / plasma membrane
- General Function
- S-adenosylmethionine-dependent methyltransferase activity
- Specific Function
- Involved in the biosynthesis of hydroxymycolate, a common precursor of oxygenated mycolic acids (methoxy-mycolate and keto-mycolate). Probably transfers a methyl group from the S-adenosylmethionine (SAM) cofactor and, subsequently or simultaneously, a water molecule onto the double bound of ethylene substrates, leading to the formation of the hydroxylated product at the distal position. Involved in the activation of the antitubercular drug thiacetazone (TAC).
- Pfam Domain Function
- CMAS (PF02353)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0012695|Hydroxymycolate synthase MmaA4 (mmaA4) ATGACGAGAATGGCCGAGAAACCGATTAGCCCAACCAAGACACGGACACGCTTCGAAGAC ATCCAAGCGCACTACGACGTCTCCGATGATTTCTTCGCCCTGTTCCAGGACCCGACCCGA ACTTACAGCTGTGCCTACTTCGAGCCACCGGAGCTCACGCTCGAAGAAGCCCAATACGCC AAGGTCGACCTCAACCTGGACAAGCTGGACCTCAAGCCGGGCATGACGCTGCTGGACATT GGGTGCGGTTGGGGCACCACCATGAGGCGCGCCGTCGAGCGGTTCGACGTTAACGTCATC GGCCTGACGTTGTCCAAGAACCAGCACGCCCGCTGCGAGCAAGTGCTGGCTTCGATCGAC ACCAACCGCTCACGTCAAGTGCTGCTGCAAGGCTGGGAGGATTTCGCCGAACCCGTCGAC CGGATTGTGTCGATCGAAGCCTTCGAGCACTTCGGGCACGAGAACTACGACGACTTCTTC AAGCGGTGTTTCAACATCATGCCCGCCGACGGCCGGATGACCGTCCAGAGCAGCGTCAGC TACCACCCCTACGAGATGGCGGCCCGCGGTAAGAAGCTGAGCTTCGAGACGGCGCGTTTC ATCAAGTTCATCGTCACCGAGATATTTCCCGGCGGCCGCCTGCCGTCCACCGAGATGATG GTCGAACACGGCGAGAAGGCCGGTTTCACCGTCCCGGAGCCGCTCTCGTTGCGCCCGCAT TACATCAAGACGCTGCGGATCTGGGGGGACACGCTGCAGTCCAATAAGGACAAGGCCATC GAGGTCACCTCCGAAGAGGTCTACAACCGCTACATGAAGTATTTGCGTGGCTGCGAGCAC TACTTCACCGACGAGATGCTCGACTGCAGCCTGGTGACCTACCTCAAGCCGGGTGCCGCG GCCTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q79FX8 UniProtKB Entry Name MMAA4_MYCTU GenBank Protein ID 2222772 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]
- Dubnau E, Chan J, Raynaud C, Mohan VP, Laneelle MA, Yu K, Quemard A, Smith I, Daffe M: Oxygenated mycolic acids are necessary for virulence of Mycobacterium tuberculosis in mice. Mol Microbiol. 2000 May;36(3):630-7. [Article]
- Dinadayala P, Laval F, Raynaud C, Lemassu A, Laneelle MA, Laneelle G, Daffe M: Tracking the putative biosynthetic precursors of oxygenated mycolates of Mycobacterium tuberculosis. Structural analysis of fatty acids of a mutant strain deviod of methoxy- and ketomycolates. J Biol Chem. 2003 Feb 28;278(9):7310-9. Epub 2002 Dec 6. [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]
- Dao DN, Sweeney K, Hsu T, Gurcha SS, Nascimento IP, Roshevsky D, Besra GS, Chan J, Porcelli SA, Jacobs WR: Mycolic acid modification by the mmaA4 gene of M. tuberculosis modulates IL-12 production. PLoS Pathog. 2008 Jun 6;4(6):e1000081. doi: 10.1371/journal.ppat.1000081. [Article]
- Alahari A, Alibaud L, Trivelli X, Gupta R, Lamichhane G, Reynolds RC, Bishai WR, Guerardel Y, Kremer L: Mycolic acid methyltransferase, MmaA4, is necessary for thiacetazone susceptibility in Mycobacterium tuberculosis. Mol Microbiol. 2009 Mar;71(5):1263-77. doi: 10.1111/j.1365-2958.2009.06604.x. Epub 2009 Jan 15. [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]
- Boissier F, Bardou F, Guillet V, Uttenweiler-Joseph S, Daffe M, Quemard A, Mourey L: Further insight into S-adenosylmethionine-dependent methyltransferases: structural characterization of Hma, an enzyme essential for the biosynthesis of oxygenated mycolic acids in Mycobacterium tuberculosis. J Biol Chem. 2006 Feb 17;281(7):4434-45. Epub 2005 Dec 15. [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]