Rv3285 - bifunctional acetyl-/propionyl-coenzyme A carboxylase alpha chain accA3
Protein Domains

Gene Information
LocusRv3285
SymbolaccA3
Gene Namebifunctional acetyl-/propionyl-coenzyme A carboxylase alpha chain accA3
Location3666357 - 3668159 (+)
SpeciesMycobacterium tuberculosis H37Rv complete genome.
LengthGene:1803 bp
Protein:601 aa
External LinksTuberculist
Target Gene Information
String Protein-Protein Interactions
STITCH Chemical-Protein Interactions
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Orthologs
Orthogroup Number34685
Related GenesCE0709 CE0713 CE0719 cg0791 cg0802 DIP0646 DIP0649 jk1669 MAP3404 MAV_4255 Mkms_1306 ML0726 Mmcs_1289 MSMEG_1807 MT3384 MUL_2637 Mvan_1664 nfa9890 PPA1719 SAV3337
Transcriptional Regulation
Operons View gene in operon browser
Regulatory Network
Search for regulators of Rv3285
Expression Correlation Genes with Correlated Expression
Scatterplot of Gene Expression

Sequence
Proteins
Genomic Sequence
Community Annotations Pending Curatorial Review
FieldValueStatusCreatorDate
InteractionPhysicalInteraction Rv3801cactivesourish102012-10-05
Affinity purification (Physical interaction)
SK. Parker, RM. Barkley et al. Mycobacterium tuberculosis Rv3802c encodes a phospholipase/thioesterase and is inhibited by the antimycobacterial agent tetrahydrolipstatin. PLoS ONE 2009
InteractionPhysicalInteraction Rv3799cactivejgalag2012-10-05
Affinity purification (Physical interaction)
D. Portevin, C. de Sousa-D'Auria et al. The acyl-AMP ligase FadD32 and AccD4-containing acyl-CoA carboxylase are required for the synthesis of mycolic acids and essential for mycobacterial growth: identification of the carboxylation product and determination of the acyl-CoA carboxylase components. J. Biol. Chem. 2005
InteractionPhysicalInteraction Rv3799cactivejgalag2012-10-05
Affinity purification (Physical interaction)
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
NameBiotin-dependent propionyl-CoA carboxylase alpha-3 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)activemjackson2012-10-05
Claisen-type condensation
TermEC:6.4.1.3 Propionyl-CoA carboxylase. - NRactiveextern:JZUCKER2012-03-06
Inferred 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:6.4.1.2 Acetyl-CoA carboxylase. - NRactiveextern:JZUCKER2012-03-06
Inferred 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:6.3.4.14 Biotin carboxylase. - NRactiveextern:JZUCKER2012-03-06
Inferred 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. - NRactiveextern:JZUCKER2012-03-06
Traceable 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:6.4.1.2 Acetyl-CoA carboxylase. - NRactiveextern:JZUCKER2012-03-06
Traceable 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:6.3.4.14 Biotin carboxylase. - NRactiveextern:JZUCKER2012-03-06
Traceable 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
OtherTBPWY:Methyl-malonyl-CoA synthesisactivemjackson2012-03-05
Biotin-dependent propionyl-CoA carboxylase alpha-3 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
OtherTBPWY:Methyl-malonyl-CoA synthesisactivemjackson2012-03-05
Biotin-dependent propionyl-CoA carboxylase alpha-3 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
TermEC:6.3.4.14 Biotin carboxylase. - NRactivejjmcfadden2012-03-05
Inferred from direct assay
D. Portevin, C. de Sousa-D'Auria et al. The acyl-AMP ligase FadD32 and AccD4-containing acyl-CoA carboxylase are required for the synthesis of mycolic acids and essential for mycobacterial growth: identification of the carboxylation product and determination of the acyl-CoA carboxylase components. J. Biol. Chem. 2005
TermEC:6.4.1.2 Acetyl-CoA carboxylase. - NRactivejjmcfadden2012-03-05
Inferred from direct assay
D. Portevin, C. de Sousa-D'Auria et al. The acyl-AMP ligase FadD32 and AccD4-containing acyl-CoA carboxylase are required for the synthesis of mycolic acids and essential for mycobacterial growth: identification of the carboxylation product and determination of the acyl-CoA carboxylase components. J. Biol. Chem. 2005