TB Genome Annotation Portal

Rv0645c (mmaA1)

Amino Acid Sequence

MAKLRPYYEESQSAYDISDDFFALFLDPTWVYTCAYFERDDMTLEEAQLAKVDLALDKLNLEPGMTLLDVGCGWGGALVRAVEKYDVNVIGLTLSRNHYE
RSKDRLAAIGTQRRAEARLQGWEEFEENVDRIVSFEAFDAFKKERYLTFFERSYDILPDDGRMLLHSLFTYDRRWLHEQGIALTMSDLRFLKFLRESIFP
GGELPSEPDIVDNAQAAGFTIEHVQLLQQHYARTLDAWAANLQAARERAIAVQSEEVYNNFMHYLTGCAERFRRGLINVAQFTMTK
(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 19 sites
Non-Essential Lignoceric Acid H37RvMA Gumbel Subhalaxmi Nambi Probability of Essentiality: 0.000000;
0 non-insertions in a row out of 19 sites
Non-Essential Phosphatidylcholine H37RvMA Gumbel Subhalaxmi Nambi Probability of Essentiality: 0.000000;
0 non-insertions in a row out of 19 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 20 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 20 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: 3.45
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

    RNA processing and modification
    Energy production and conversion
    Chromatin structure and dynamics
    Amino acid transport and metabolism
    Cell cycle control, cell division, chromosome partitioning
    Carbohydrate transport and metabolism
    Nucleotide transport and metabolism
    Lipid transport and metabolism
    Coenzyme transport and metabolism
    Transcription
    Translation, ribosomal structure and biogenesis
    Cell wall/membrane/envelope biogenesis
    Replication, recombination and repair
    Posttranslational modification, protein turnover, chaperones
    Cell motility
    Secondary metabolites biosynthesis, transport and catabolism
    Inorganic ion transport and metabolism
    Function unknown
    General function prediction only
    Intracellular trafficking, secretion, and vesicular transport
    Signal transduction mechanisms
    Extracellular structures
    Defense mechanisms
    Nuclear structure
    Cytoskeleton
  • BioCyc Co-regulated genes based on gene expression profiling (Systems Biology, Inferelator Network)
  • Differentially expressed as result of RNASeq in glycerol environment (Only top 20 genes shown sorted by log fold change with p_adj 0.05).
    Conditionally essential as result of TNSeq (Only top 20 genes shown sorted by log fold change with p_adj 0.05).
  • BioCyc Transcription factor binding based on ChIP-Seq (Systems Biology)
  • Interactions based on ChIPSeq data (Minch et al. 2014)

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



    TBCAP

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

    Rv0645c (mmaA1)

    PropertyValueCreatorEvidencePMIDComment
    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
    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
    NameMmaA1 METHOXY MYCOLIC ACID SYNTHASE; trans cyclopropanation of methoxy- and ketomycolatesmjacksonIMPS-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
    CitationMMAS-1, the branch point between cis- and trans-cyclopropane-containing oxygenated mycolates in Mycobacterium tuberculosis. authors,Y. Yuan,DC. Crane,JM. Musser,S. Sreevatsan,CE. Barry J. Biol. Chem. 1997extern:JZUCKER9092547Inferred from experiment
    TermEC:2.1.1.- Transferases. Transferring one-carbon groups. Methyltransferases. - NRextern:JZUCKERNRInferred from experiment
    authors,Y. Yuan,DC. Crane,JM. Musser,S. Sreevatsan,CE. Barry MMAS-1, the branch point between cis- and trans-cyclopropane-containing oxygenated mycolates in Mycobacterium tuberculosis. J. Biol. Chem. 1997
    TermEC:2.1.1.79 Cyclopropane-fatty-acyl-phospholipid synthase. - NRextern:JZUCKERNRInferred from experiment
    authors,Y. Yuan,DC. Crane,JM. Musser,S. Sreevatsan,CE. Barry MMAS-1, the branch point between cis- and trans-cyclopropane-containing oxygenated mycolates in Mycobacterium tuberculosis. J. Biol. Chem. 1997

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