Rv3281 - conserved hypothetical protein

Expression: Most Significant Conditions for Rv3281

Protein Domains

Gene Information
Locus	Rv3281
Symbol	accE5
Gene Name	conserved hypothetical protein
Location	3663689 - 3664222 (+)
Species	Mycobacterium tuberculosis H37Rv complete genome.
Length	Gene:534 bp Protein:178 aa
External Links	Tuberculist Target Gene Information String Protein-Protein Interactions STITCH Chemical-Protein Interactions Search Google Scholar
Orthologs
Orthogroup Number	6440
Related Genes	MAP3400 MAV_4251 Mkms_1310 ML0730 Mmcs_1293 MSMEG_1812 MT3380 MUL_2633 Mvan_1676
Transcriptional Regulation
Operons	View gene in operon browser
Regulatory Network	Search for regulators of Rv3281
Expression Correlation	Genes with Correlated Expression Scatterplot of Gene Expression

Sequence

Proteins

>Rv3281 Transcript 1
MGTCPCESSERNEPVSRVSGTNEVSDGNETNNPAEVSDGNETNNPAEVSDGNETNNPAPV
SRVSGTNEVSDGNETNNPAPVSRVSGTNEVSDGNETNNPAPVTEKPLHPHEPHIEILRGQ
PTDQELAALIAVLGSISGSTPPAQPEPTRWGLPVDQLRYPVFSWQRITLQEMTHMRR*

Genomic Sequence

>Rv3281
ATGGGAACGTGCCCCTGTGAGTCGAGTGAGCGGAACGAACCTGTGAGTCGAGTGAGCGGA
ACGAACGAAGTGAGTGACGGGAACGAGACGAACAATCCGGCAGAAGTGAGTGACGGGAAC
GAGACGAACAATCCGGCAGAAGTGAGTGACGGGAACGAGACGAACAATCCGGCCCCTGTG
AGTCGAGTGAGCGGAACGAACGAAGTGAGTGACGGGAACGAGACGAACAATCCGGCCCCT
GTGAGTCGAGTGAGCGGAACGAACGAAGTGAGTGACGGGAACGAGACGAACAATCCGGCC
CCTGTGACCGAGAAGCCGCTGCATCCGCACGAGCCCCACATCGAGATACTGCGGGGACAA
CCCACCGATCAGGAGCTGGCCGCGTTGATCGCGGTGCTGGGCAGTATCAGCGGTTCAACC
CCGCCCGCGCAACCCGAGCCCACCCGGTGGGGGCTGCCGGTCGACCAGTTGCGGTACCCC
GTCTTCAGTTGGCAGCGCATCACACTGCAAGAAATGACGCACATGCGCCGATGA

Community Annotations Pending Curatorial Review

Field	Value	Status	Creator	Date
Term	TBRXN:ACCOACr acetyl-CoA carboxylase, reversible reaction - ISS	active	njamshidi	2012-10-05
	PMID: 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
Term	EC:6.4.1.2 Acetyl-CoA carboxylase. - ISS	active	njamshidi	2012-10-05
	PMID: 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
Term	TBRXN:ACCOACr acetyl-CoA carboxylase, reversible reaction - IDA	active	njamshidi	2012-10-05
	PMID: 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
Term	EC:6.4.1.2 Acetyl-CoA carboxylase. - IDA	active	njamshidi	2012-10-05
	PMID: 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
Interaction	PhysicalInteraction Rv3799c	active	jgalag	2012-10-05
	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
Interaction	PhysicalInteraction Rv3799c	active	jgalag	2012-10-05
	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
Interaction	PhysicalInteraction Rv3280	active	priti.priety	2012-10-05
	Structural 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
Interaction	PhysicalInteraction Rv3280	active	priti.priety	2012-10-05
	Structural Analysis G. Gago, D. Kurth et al. Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. J. Bacteriol. 2006
Interaction	PhysicalInteraction Rv3280	active	priti.priety	2012-10-05
	Spectrophotometric 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
Interaction	PhysicalInteraction Rv3280	active	priti.priety	2012-10-05
	Spectrophotometric G. Gago, D. Kurth et al. Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. J. Bacteriol. 2006
Name	Biotin-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)	active	mjackson	2012-10-05
	Claisen-type condensation
Term	EC:6.4.1.3 Propionyl-CoA carboxylase. - NR	active	extern:JZUCKER	2012-03-06
	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
Term	EC:6.4.1.2 Acetyl-CoA carboxylase. - NR	active	extern:JZUCKER	2012-03-06
	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
Term	EC:6.4.1.3 Propionyl-CoA carboxylase. - NR	active	extern:JZUCKER	2012-03-06
	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
Term	EC:6.4.1.2 Acetyl-CoA carboxylase. - NR	active	extern:JZUCKER	2012-03-06
	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
Other	TBPWY:Methyl-malonyl-CoA synthesis	active	mjackson	2012-03-05
	Biotin-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
Other	TBPWY:Methyl-malonyl-CoA synthesis	active	mjackson	2012-03-05
	Biotin-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