Rv3280 - propionyl-CoA carboxylase beta chain 5 accD5

Expression: Most Significant Conditions for Rv3280

Protein Domains

Gene Information
Locus	Rv3280
Symbol	accD5
Gene Name	propionyl-CoA carboxylase beta chain 5 accD5
Location	3662062 - 3663708 (+)
Species	Mycobacterium tuberculosis H37Rv complete genome.
Length	Gene:1647 bp Protein:549 aa
External Links	Tuberculist Target Gene Information String Protein-Protein Interactions STITCH Chemical-Protein Interactions Search Google Scholar
Orthologs
Orthogroup Number	35146
Related Genes	jk1662 MAP3399 MAV_4250 Mkms_1311 ML0731 Mmcs_1294 MSMEG_1813 MUL_2632 Mvan_1677 nfa9940 PPA1707
Transcriptional Regulation
Operons	View gene in operon browser
Regulatory Network	Search for regulators of Rv3280
Expression Correlation	Genes with Correlated Expression Scatterplot of Gene Expression

Sequence

Proteins

>Rv3280 Transcript 1
MTSVTDRSAHSAERSTEHTIDIHTTAGKLAELHKRREESLHPVGEDAVEKVHAKGKLTAR
ERIYALLDEDSFVELDALAKHRSTNFNLGEKRPLGDGVVTGYGTIDGRDVCIFSQDATVF
GGSLGEVYGEKIVKVQELAIKTGRPLIGINDGAGARIQEGVVSLGLYSRIFRNNILASGV
IPQISLIMGAAAGGHVYSPALTDFVIMVDQTSQMFITGPDVIKTVTGEEVTMEELGGAHT
HMAKSGTAHYAASGEQDAFDYVRELLSYLPPNNSTDAPRYQAAAPTGPIEENLTDEDLEL
DTLIPDSPNQPYDMHEVITRLLDDEFLEIQAGYAQNIVVGFGRIDGRPVGIVANQPTHFA
GCLDINASEKAARFVRTCDCFNIPIVMLVDVPGFLPGTDQEYNGIIRRGAKLLYAYGEAT
VPKITVITRKAYGGAYCVMGSKDMGCDVNLAWPTAQIAVMGASGAVGFVYRQQLAEAAAN
GEDIDKLRLRLQQEYEDTLVNPYVAAERGYVDAVIPPSHTRGYIGTALRLLERKIAQLPP
KKHGNVPL*

Genomic Sequence

>Rv3280
ATGACAAGCGTTACCGACCGCTCGGCTCATTCCGCAGAGCGGTCCACCGAGCACACCATC
GACATCCACACCACCGCGGGCAAGCTGGCGGAGCTGCACAAACGCAGGGAAGAGTCGCTG
CACCCCGTCGGTGAGGATGCCGTCGAAAAAGTACACGCCAAGGGCAAGCTGACGGCTCGC
GAGCGTATCTACGCGTTGCTGGATGAGGATTCGTTCGTCGAGCTGGACGCGCTGGCCAAA
CACCGCAGCACCAACTTCAATCTCGGTGAAAAACGCCCGCTCGGCGACGGCGTGGTCACC
GGCTACGGCACCATCGACGGGCGCGACGTGTGCATCTTCAGCCAGGACGCCACGGTGTTT
GGCGGCAGCCTTGGCGAGGTGTACGGCGAGAAAATCGTCAAGGTCCAGGAACTGGCGATC
AAGACCGGCCGTCCGCTCATCGGCATCAACGACGGTGCTGGCGCGCGCATCCAGGAAGGT
GTCGTCTCGCTGGGCCTGTACAGCCGTATCTTTCGCAACAACATCCTGGCCTCCGGCGTC
ATCCCGCAAATCTCGTTGATCATGGGAGCCGCCGCCGGTGGGCACGTCTACTCCCCCGCC
CTGACCGACTTCGTGATCATGGTCGATCAGACCAGCCAGATGTTCATCACCGGGCCCGAC
GTCATCAAGACCGTCACCGGCGAGGAAGTCACCATGGAAGAACTCGGCGGCGCCCACACC
CACATGGCCAAGTCGGGTACGGCACACTACGCCGCATCGGGCGAACAGGACGCCTTCGAC
TACGTTCGCGAGCTGCTGAGCTACCTGCCGCCCAACAACTCCACCGACGCGCCCCGATAC
CAAGCCGCAGCCCCGACAGGGCCCATCGAGGAGAACCTCACCGACGAGGACCTCGAATTG
GATACGCTGATCCCGGACTCGCCCAACCAGCCCTATGACATGCACGAGGTGATCACCCGG
CTCCTCGACGACGAATTCCTGGAGATACAGGCCGGTTACGCCCAAAACATCGTGGTGGGG
TTCGGGCGCATCGACGGCCGGCCAGTCGGCATTGTCGCCAACCAGCCGACACACTTCGCC
GGCTGCCTGGATATCAACGCCTCGGAGAAAGCGGCCCGGTTTGTGCGGACCTGCGACTGC
TTCAATATCCCCATCGTCATGCTGGTGGACGTCCCGGGCTTCCTGCCGGGCACCGACCAG
GAATACAACGGCATCATCCGGCGCGGCGCCAAGCTGCTCTACGCCTACGGCGAGGCCACC
GTGCCAAAGATCACGGTCATCACCCGCAAGGCCTACGGCGGTGCGTACTGCGTTATGGGC
TCCAAAGACATGGGCTGCGACGTCAACCTGGCGTGGCCGACCGCGCAGATCGCGGTGATG
GGCGCCTCCGGCGCAGTGGGCTTCGTGTACCGCCAGCAGCTGGCCGAGGCCGCCGCCAAC
GGCGAGGACATCGACAAGCTGCGGCTGCGGCTCCAGCAGGAGTACGAGGACACACTGGTC
AACCCGTACGTGGCCGCCGAACGCGGATACGTCGACGCGGTGATCCCGCCGTCGCATACT
CGCGGCTACATCGGGACCGCGCTGCGGCTGCTGGAACGCAAGATCGCGCAGCTGCCGCCC
AAAAAGCATGGGAACGTGCCCCTGTGA

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
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 Rv3801c	active	sourish10	2012-10-05
	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
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 Rv3281	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 Rv3281	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 Rv3281	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 Rv3281	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
Interaction	RegulatedBy Rv1221	active	yamir.moreno	2012-10-05
	Microarrays. mRNA levels of regulated element measured and compared between wild-type and trans-element mutation (knockout, over expression etc.) performed by using microarray (or macroarray) experiments.. R. Manganelli, MI. Voskuil et al. The Mycobacterium tuberculosis ECF sigma factor sigmaE: role in global gene expression and survival in macrophages. Mol. Microbiol. 2001
Name	Biotin-dependent propionyl-CoA carboxylase beta-5 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
Term	EC:6.4.1.3 Propionyl-CoA carboxylase. - NR	active	extern:JZUCKER	2012-03-06
	Human inference of function from sequence authors,ST. Cole,R. Brosch,J. Parkhill,T. Garnier,C. Churcher,D. Harris,SV. Gordon,K. Eiglmeier,S. Gas,CE. Barry,F. Tekaia,K. Badcock,D. Basham,D. Brown,T. Chillingworth,R. Connor,R. Davies,K. Devlin,T. Feltwell,S. Gentles,N. Hamlin,S. Holroyd,T. Hornsby,K. Jagels,A. Krogh,J. McLean,S. Moule,L. Murphy,K. Oliver,J. Osborne,MA. Quail,MA. Rajandream,J. Rogers,S. Rutter,K. Seeger,J. Skelton,R. Squares,S. Squares,JE. Sulston,K. Taylor,S. Whitehead,BG. Barrell Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 1998
Term	EC:6.4.1.2 Acetyl-CoA carboxylase. - NR	active	extern:JZUCKER	2012-03-06
	Human inference of function from sequence authors,ST. Cole,R. Brosch,J. Parkhill,T. Garnier,C. Churcher,D. Harris,SV. Gordon,K. Eiglmeier,S. Gas,CE. Barry,F. Tekaia,K. Badcock,D. Basham,D. Brown,T. Chillingworth,R. Connor,R. Davies,K. Devlin,T. Feltwell,S. Gentles,N. Hamlin,S. Holroyd,T. Hornsby,K. Jagels,A. Krogh,J. McLean,S. Moule,L. Murphy,K. Oliver,J. Osborne,MA. Quail,MA. Rajandream,J. Rogers,S. Rutter,K. Seeger,J. Skelton,R. Squares,S. Squares,JE. Sulston,K. Taylor,S. Whitehead,BG. Barrell Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 1998
Other	TBPWY:Methyl-malonyl-CoA synthesis	active	mjackson	2012-03-05
	Biotin-dependent propionyl-CoA carboxylase beta-5 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) 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
Other	TBPWY:Methyl-malonyl-CoA synthesis	active	mjackson	2012-03-05
	Biotin-dependent propionyl-CoA carboxylase beta-5 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 beta-5 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
Term	EC:6.4.1.3 Propionyl-CoA carboxylase. - NR	active	jjmcfadden	2012-03-05
	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
Term	EC:6.4.1.2 Acetyl-CoA carboxylase. - NR	active	jjmcfadden	2012-03-05
	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
Term	EC:6.4.1.4 Methylcrotonoyl-CoA carboxylase. - NR	active	jjmcfadden	2012-03-05
	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
Term	EC:4.1.1.41 Methylmalonyl-CoA decarboxylase. - NR	active	jjmcfadden	2012-03-05
	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