TB Genome Annotation Portal

Rv0644c (mmaA2)

Amino Acid Sequence

MVNDLTPHFEDVQAHYDLSDDFFRLFLDPTQTYSCAHFEREDMTLEEAQIAKIDLALGKLGLQPGMTLLDIGCGWGATMRRAIAQYDVNVVGLTLSKNQA
AHVQKSFDEMDTPRDRRVLLAGWEQFNEPVDRIVSIGAFEHFGHDRHADFFARAHKILPPDGVLLLHTITGLTRQQMVDHGLPLTLWLARFLKFIATEIF
PGGQPPTIEMVEEQSAKTGFTLTRRQSLQPHYARTLDLWAEALQEHKSEAIAIQSEEVYERYMKYLTGCAKLFRVGYIDVNQFTLAK
(Nucleotide sequence available on KEGG)

Additional Information



ESSENTIALITY

MtbTnDB - interactive tool for exploring a database of published TnSeq datasets for Mtb

TnSeqCorr - genes with correlated TnSeq profiles across >100 conditions *new*

Classification Condition Strain Method Reference Notes
Non-Essential Sodium Oleate H37RvMA Gumbel Subhalaxmi Nambi Probability of Essentiality: 0.000000;
1 non-insertions in a row out of 11 sites
Non-Essential Lignoceric Acid H37RvMA Gumbel Subhalaxmi Nambi Probability of Essentiality: 0.000000;
1 non-insertions in a row out of 11 sites
Non-Essential Phosphatidylcholine H37RvMA Gumbel Subhalaxmi Nambi Probability of Essentiality: 0.000000;
1 non-insertions in a row out of 11 sites
Non-Essential minimal media + 0.1% glycerol H37RvMA Gumbel Griffin et al. (2011) Probability of Essentiality: 0.000000;
1 non-insertions in a row out of 12 sites
Non-Essential minimal media + 0.01% cholesterol H37RvMA Gumbel Griffin et al. (2011) Probability of Essentiality: 0.000000;
1 non-insertions in a row out of 12 sites
Non-Essential 7H10-glycerol H37RvMA TraSH Sassetti et al. (2003a)
Non-Essential C57BL/6J mice (8 weeks) H37RvMA TraSH Sassetti et al. (2003b) Hybridization Ratio: 1.36
Growth-Advantage 7H09/7H10 + rich media H37RvMA MotifHMM DeJesus et al. (2017) Fully saturated (14 reps).

TnSeq Data No data currently available.
  • No TnSeq data currently available for this Target.
RNASeq Data No data currently available.
  • No RNA-Seq data currently available for this Target.
Metabolomic Profiles No data currently available.
  • No Metabolomic data currently available for this Target.
Proteomic Data No data currently available.
  • No Proteomic data currently available for this Target.

Regulatory Relationships from Systems Biology
  • BioCyc

    Gene interactions based on ChIPSeq and Transcription Factor Over-Expression (TFOE) (Systems Biology)

    NOTE: Green edges represent the connected genes being classified as differentially essential as a result of the middle gene being knocked out. These interactions are inferred based on RNASeq.

    Interactions based on ChIPSeq data

    • Binds To:

      • No bindings to other targets were found.
    • Bound By:

    Interactions based on ChIPSeq data (Minch et al. 2014)

    • Binds To:

      • No bindings to other targets were found.
    • Bound By:

      • No bindings to other targets were found.

    Interactions based on TFOE data (Rustad et al. 2014)

    • Upregulates:

      • Does not upregulate other genes.
    • Upregulated by:

    • Downregulates:

      • Does not downregulate other genes.
    • Downregulated by:

      • Not downregulated by other genes.


    TBCAP

    Tubculosis Community Annotation Project (
    Slayden et al., 2013)

    Rv0644c (mmaA2)

    PropertyValueCreatorEvidencePMIDComment
    CitationFurther insight into S-adenosylmethionine-dependent methyltransferases: structural characterization of Hma, an enzyme essential for the biosynthesis of oxygenated mycolic acids in Mycobacterium tuberculosis. F. Boissier, F. Bardou et al. J. Biol. Chem. 2006njamshidiIDA16356931PMID: 16356931
    TermTBRXN:MYC1M2 Mycolic Acid Methyl Hydroxyl Addition - IDAnjamshidiIDA16356931PMID: 16356931
    F. Boissier, F. Bardou et al. 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
    CitationFurther insight into S-adenosylmethionine-dependent methyltransferases: structural characterization of Hma, an enzyme essential for the biosynthesis of oxygenated mycolic acids in Mycobacterium tuberculosis. F. Boissier, F. Bardou et al. J. Biol. Chem. 2006njamshidiISS16356931PMID: 16356931
    TermTBRXN:MYC1M2 Mycolic Acid Methyl Hydroxyl Addition - ISSnjamshidiISS16356931PMID: 16356931
    F. Boissier, F. Bardou et al. 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
    CitationFurther insight into S-adenosylmethionine-dependent methyltransferases: structural characterization of Hma, an enzyme essential for the biosynthesis of oxygenated mycolic acids in Mycobacterium tuberculosis. F. Boissier, F. Bardou et al. J. Biol. Chem. 2006njamshidiIDA16356931PMID: 16356931
    TermTBRXN:MYC1M1 Mycolic Acid Methyl Hydroxyl Addition - IDAnjamshidiIDA16356931PMID: 16356931
    F. Boissier, F. Bardou et al. 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
    CitationFurther insight into S-adenosylmethionine-dependent methyltransferases: structural characterization of Hma, an enzyme essential for the biosynthesis of oxygenated mycolic acids in Mycobacterium tuberculosis. F. Boissier, F. Bardou et al. J. Biol. Chem. 2006njamshidiISS16356931PMID: 16356931
    TermTBRXN:MYC1M1 Mycolic Acid Methyl Hydroxyl Addition - ISSnjamshidiISS16356931PMID: 16356931
    F. Boissier, F. Bardou et al. 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
    CitationFurther insight into S-adenosylmethionine-dependent methyltransferases: structural characterization of Hma, an enzyme essential for the biosynthesis of oxygenated mycolic acids in Mycobacterium tuberculosis. F. Boissier, F. Bardou et al. J. Biol. Chem. 2006njamshidiIDA16356931PMID: 16356931
    TermTBRXN:MYC1CYC5 Mycolic Acid Cyclopropanation - IDAnjamshidiIDA16356931PMID: 16356931
    F. Boissier, F. Bardou et al. 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
    CitationFurther insight into S-adenosylmethionine-dependent methyltransferases: structural characterization of Hma, an enzyme essential for the biosynthesis of oxygenated mycolic acids in Mycobacterium tuberculosis. F. Boissier, F. Bardou et al. J. Biol. Chem. 2006njamshidiISS16356931PMID: 16356931
    TermTBRXN:MYC1CYC5 Mycolic Acid Cyclopropanation - ISSnjamshidiISS16356931PMID: 16356931
    F. Boissier, F. Bardou et al. 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
    CitationFurther insight into S-adenosylmethionine-dependent methyltransferases: structural characterization of Hma, an enzyme essential for the biosynthesis of oxygenated mycolic acids in Mycobacterium tuberculosis. F. Boissier, F. Bardou et al. J. Biol. Chem. 2006njamshidiIDA16356931PMID: 16356931
    TermTBRXN:MYC1CYC4 Mycolic Acid Cyclopropanation - IDAnjamshidiIDA16356931PMID: 16356931
    F. Boissier, F. Bardou et al. 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
    CitationFurther insight into S-adenosylmethionine-dependent methyltransferases: structural characterization of Hma, an enzyme essential for the biosynthesis of oxygenated mycolic acids in Mycobacterium tuberculosis. F. Boissier, F. Bardou et al. J. Biol. Chem. 2006njamshidiISS16356931PMID: 16356931
    TermTBRXN:MYC1CYC4 Mycolic Acid Cyclopropanation - ISSnjamshidiISS16356931PMID: 16356931
    F. Boissier, F. Bardou et al. 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
    NameMmaA2 METHOXY MYCOLIC ACID SYNTHASE, adds the cyclopropane rings to the distal positions of the alpha mycolatemjacksonIMPS-adenosyl-methionine-dependent mycolic acid methyltransferases
    CitationPathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis. K. Takayama, C. Wang et al. Clin. Microbiol. Rev. 2005jjmcfadden15653820Inferred from direct assay
    TermEC:2.1.1.- Transferases. Transferring one-carbon groups. Methyltransferases. - NRjjmcfaddenNRInferred from direct assay
    K. Takayama, C. Wang et al. Pathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis. Clin. Microbiol. Rev. 2005
    CitationThe mmaA2 gene of Mycobacterium tuberculosis encodes the distal cyclopropane synthase of the alpha-mycolic acid. MS. Glickman J. Biol. Chem. 2003extern:JZUCKER12502719Reaction blocked in mutant
    TermEC:2.1.1.- Transferases. Transferring one-carbon groups. Methyltransferases. - NRextern:JZUCKERNRReaction blocked in mutant
    MS. Glickman The mmaA2 gene of Mycobacterium tuberculosis encodes the distal cyclopropane synthase of the alpha-mycolic acid. J. Biol. Chem. 2003
    TermEC:2.1.1.79 Cyclopropane-fatty-acyl-phospholipid synthase. - NRextern:JZUCKERNRReaction blocked in mutant
    MS. Glickman The mmaA2 gene of Mycobacterium tuberculosis encodes the distal cyclopropane synthase of the alpha-mycolic acid. J. Biol. Chem. 2003

    Comments