TB Genome Annotation Portal

Rv3281 (accE5)

Amino Acid Sequence

MGTCPCESSERNEPVSRVSGTNEVSDGNETNNPAEVSDGNETNNPAEVSDGNETNNPAPVSRVSGTNEVSDGNETNNPAPVSRVSGTNEVSDGNETNNPA
PVTEKPLHPHEPHIEILRGQPTDQELAALIAVLGSISGSTPPAQPEPTRWGLPVDQLRYPVFSWQRITLQEMTHMRR
(Nucleotide sequence available on KEGG)

Additional Information

Oh, T. J., J. Daniel, H. J. Kim, T. D. Sirakova, and
P. E. Kolattukudy. 2006. Identification and characterization of Rv3281
as a novel subunit of a biotin-dependent acyl-CoA carboxylase in
Mycobacterium tuberculosis H37Rv. J. Biol. Chem. 281:3899-3908.

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
Too-Short Sodium Oleate H37RvMA Gumbel Subhalaxmi Nambi Probability of Essentiality: -1.000000;
3 non-insertions in a row out of 3 sites
Too-Short Lignoceric Acid H37RvMA Gumbel Subhalaxmi Nambi Probability of Essentiality: -1.000000;
3 non-insertions in a row out of 3 sites
Too-Short Phosphatidylcholine H37RvMA Gumbel Subhalaxmi Nambi Probability of Essentiality: -1.000000;
3 non-insertions in a row out of 3 sites
Too-Short minimal media + 0.1% glycerol H37RvMA Gumbel Griffin et al. (2011) Probability of Essentiality: -1.000000;
3 non-insertions in a row out of 3 sites
Too-Short minimal media + 0.01% cholesterol H37RvMA Gumbel Griffin et al. (2011) Probability of Essentiality: -1.000000;
3 non-insertions in a row out of 3 sites
Essential 7H10-glycerol H37RvMA TraSH Sassetti et al. (2003a)
Essential C57BL/6J mice (8 weeks) H37RvMA TraSH Sassetti et al. (2003b) Hybridization Ratio: 0.03
Essential 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)

    Rv3281 (accE5)

    PropertyValueCreatorEvidencePMIDComment
    CitationBiochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. G. Gago, D. Kurth et al. J. Bacteriol. 2006njamshidiIDA16385038PMID: 16385038 AccE5 neede for max catalytic activity
    TermEC:6.4.1.2 Acetyl-CoA carboxylase. - IDAnjamshidiIDA16385038PMID: 16385038 AccE5 neede for max catalytic activity
    G. Gago, D. Kurth et al. Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. J. Bacteriol. 2006
    TermTBRXN:ACCOACr acetyl-CoA carboxylase, reversible reaction - IDAnjamshidiIDA16385038PMID: 16385038 AccE5 neede for max catalytic activity
    G. Gago, D. Kurth et al. Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. J. Bacteriol. 2006
    CitationBiochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. G. Gago, D. Kurth et al. J. Bacteriol. 2006njamshidiISS16385038PMID: 16385038 AccE5 neede for max catalytic activity
    TermEC:6.4.1.2 Acetyl-CoA carboxylase. - ISSnjamshidiISS16385038PMID: 16385038 AccE5 neede for max catalytic activity
    G. Gago, D. Kurth et al. Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. J. Bacteriol. 2006
    TermTBRXN:ACCOACr acetyl-CoA carboxylase, reversible reaction - ISSnjamshidiISS16385038PMID: 16385038 AccE5 neede for max catalytic activity
    G. Gago, D. Kurth et al. Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. J. Bacteriol. 2006
    CitationBiochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. G. Gago, D. Kurth et al. J. Bacteriol. 2006priti.prietyIDA16385038Spectrophotometric
    InteractionPhysicalInteraction Rv3280priti.prietyIDASpectrophotometric
    G. Gago, D. Kurth et al. Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. J. Bacteriol. 2006
    CitationStructure-based inhibitor design of AccD5, an essential acyl-CoA carboxylase carboxyltransferase domain of Mycobacterium tuberculosis. TW. Lin, MM. Melgar et al. Proc. Natl. Acad. Sci. U.S.A. 2006priti.prietyIDA16492739Spectrophotometric
    InteractionPhysicalInteraction Rv3280priti.prietyIDASpectrophotometric
    TW. Lin, MM. Melgar et al. Structure-based inhibitor design of AccD5, an essential acyl-CoA carboxylase carboxyltransferase domain of Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U.S.A. 2006
    CitationBiochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. G. Gago, D. Kurth et al. J. Bacteriol. 2006priti.prietyIDA16385038Structural Analysis
    InteractionPhysicalInteraction Rv3280priti.prietyIDAStructural Analysis
    G. Gago, D. Kurth et al. Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. J. Bacteriol. 2006
    CitationStructure-based inhibitor design of AccD5, an essential acyl-CoA carboxylase carboxyltransferase domain of Mycobacterium tuberculosis. TW. Lin, MM. Melgar et al. Proc. Natl. Acad. Sci. U.S.A. 2006priti.prietyIDA16492739Structural Analysis
    InteractionPhysicalInteraction Rv3280priti.prietyIDAStructural Analysis
    TW. Lin, MM. Melgar et al. Structure-based inhibitor design of AccD5, an essential acyl-CoA carboxylase carboxyltransferase domain of Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U.S.A. 2006
    NameBiotin-dependent propionyl-CoA carboxylase epsilon subunit involved in the synthesis of methyl-malonyl-CoA required for the biosynthesis of multiple methyl-branched fatty acids; the enzyme complex made of AccA3-AccD5-AccE5 shows a clear substrate preference for propionyl-CoA compared with acetyl-CoA (used in the generation of malonyl-CoA)mjacksonIDAClaisen-type condensation
    OtherTBPWY:Methyl-malonyl-CoA synthesismjacksonBiotin-dependent propionyl-CoA carboxylase epsilon subunit involved in the synthesis of methyl-malonyl-CoA required for the biosynthesis of multiple methyl-branched fatty acids (enzymatic); the enzyme complex made of AccA3-AccD5-AccE5 shows a clear substrate preference for propionyl-CoA compared with acetyl-CoA (used in the generation of malonyl-CoA)
    TJ. Oh, J. Daniel et al. Identification and characterization of Rv3281 as a novel subunit of a biotin-dependent acyl-CoA Carboxylase in Mycobacterium tuberculosis H37Rv. J. Biol. Chem. 2006
    CitationBiochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. G. Gago, D. Kurth et al. J. Bacteriol. 2006mjackson16385038Biotin-dependent propionyl-CoA carboxylase epsilon subunit involved in the synthesis of methyl-malonyl-CoA required for the biosynthesis of multiple methyl-branched fatty acids (enzymatic); the enzyme complex made of AccA3-AccD5-AccE5 shows a clear substrate preference for propionyl-CoA compared with acetyl-CoA (used in the generation of malonyl-CoA)
    OtherTBPWY:Methyl-malonyl-CoA synthesismjacksonBiotin-dependent propionyl-CoA carboxylase epsilon subunit involved in the synthesis of methyl-malonyl-CoA required for the biosynthesis of multiple methyl-branched fatty acids (enzymatic); the enzyme complex made of AccA3-AccD5-AccE5 shows a clear substrate preference for propionyl-CoA compared with acetyl-CoA (used in the generation of malonyl-CoA)
    G. Gago, D. Kurth et al. Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. J. Bacteriol. 2006
    CitationIdentification and characterization of Rv3281 as a novel subunit of a biotin-dependent acyl-CoA Carboxylase in Mycobacterium tuberculosis H37Rv. TJ. Oh, J. Daniel et al. J. Biol. Chem. 2006mjackson16354663Biotin-dependent propionyl-CoA carboxylase epsilon subunit involved in the synthesis of methyl-malonyl-CoA required for the biosynthesis of multiple methyl-branched fatty acids (enzymatic); the enzyme complex made of AccA3-AccD5-AccE5 shows a clear substrate preference for propionyl-CoA compared with acetyl-CoA (used in the generation of malonyl-CoA)
    CitationCentral carbon metabolism in Mycobacterium tuberculosis: an unexpected frontier. authors,KY. Rhee,LP. de Carvalho,R. Bryk,S. Ehrt,J. Marrero,SW. Park,D. Schnappinger,A. Venugopal,C. Nathan Trends Microbiol. 2011extern:JZUCKER21561773Traceable author statement to experimental support
    TermEC:6.4.1.2 Acetyl-CoA carboxylase. - NRextern:JZUCKERNRTraceable author statement to experimental support
    authors,KY. Rhee,LP. de Carvalho,R. Bryk,S. Ehrt,J. Marrero,SW. Park,D. Schnappinger,A. Venugopal,C. Nathan Central carbon metabolism in Mycobacterium tuberculosis: an unexpected frontier. Trends Microbiol. 2011
    TermEC:6.4.1.3 Propionyl-CoA carboxylase. - NRextern:JZUCKERNRTraceable author statement to experimental support
    authors,KY. Rhee,LP. de Carvalho,R. Bryk,S. Ehrt,J. Marrero,SW. Park,D. Schnappinger,A. Venugopal,C. Nathan Central carbon metabolism in Mycobacterium tuberculosis: an unexpected frontier. Trends Microbiol. 2011
    CitationBiochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. G. Gago, D. Kurth et al. J. Bacteriol. 2006extern:JZUCKER16385038Inferred from mutant phenotype
    TermEC:6.4.1.2 Acetyl-CoA carboxylase. - NRextern:JZUCKERNRInferred from mutant phenotype
    G. Gago, D. Kurth et al. Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. J. Bacteriol. 2006
    TermEC:6.4.1.3 Propionyl-CoA carboxylase. - NRextern:JZUCKERNRInferred from mutant phenotype
    G. Gago, D. Kurth et al. Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. J. Bacteriol. 2006

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