Rv3280 (accD5)

Current annotations:
- TBCAP: (community-based annotations - see table at bottom of page)
- TBDB: propionyl-CoA carboxylase beta chain
- REFSEQ: propionyl-CoA carboxylase beta chain
- PATRIC: Methylcrotonyl-CoA carboxylase carboxyl transferase subunit (EC 6.4.1.4)
- TUBERCULIST: Probable propionyl-CoA carboxylase beta chain 5 AccD5 (pccase) (propanoyl-CoA:carbon dioxide ligase)
- NCBI: Probable propionyl-CoA carboxylase beta chain 5 AccD5 (pccase) (propanoyl-CoA:carbon dioxide ligase)
- updated information (H37Rv4):
  - gene name: accD5
  - function:
  - reference:
Type: Essential
Start: 3662062
End: 3663708
Operon:

Trans-membrane region:
Role: I.H.1 - Synthesis of fatty and mycolic acids
GO terms:
- GO:0042802 - identical protein binding (Uniprot)
- GO:0032991 - protein-containing complex (Uniprot)
- GO:0016874 - ligase activity (Uniprot)
- GO:0015977 - carbon fixation (Uniprot)
- GO:0009317 - acetyl-CoA carboxylase complex (Uniprot)
- GO:0009062 - fatty acid catabolic process (Uniprot)
- GO:0005886 - plasma membrane (Uniprot)
- GO:0005618 - cell wall (Uniprot)
- GO:0005524 - ATP binding (Uniprot)
- GO:0005515 - protein binding (Uniprot)
- GO:0004658 - propionyl-CoA carboxylase activity (Uniprot)
- GO:0003989 - acetyl-CoA carboxylase activity (Uniprot)
- GO:0000166 - nucleotide binding (Uniprot)
Reaction(s) (based on iSM810 metabolic model):
Gene Expression Profile (Transcriptional Responses to Drugs; Boshoff et al, 2004)
Gene Modules extracted from cluster analysis of 249 transcriptomic datasets using ICA
Orthologs among selected mycobacteria
Protein structure: 2bzr, 2a7s
Search for Homologs in PDB

Top 10 Homologs in PDB (as of Nov 2020):

PDB	aa ident	species	PDB title
2A7S	100%	Mycobacterium tuberculosis	Crystal Structure of the Acyl-CoA Carboxylase, AccD5, from Mycobacterium tuberculosis
2BZR	99%	MYCOBACTERIUM TUBERCULOSIS	Crystal structure of accD5 (Rv3280), an acyl-CoA carboxylase beta- subunit from Mycobacterium tuberculosis
3MFM	68%	Streptomyces coelicolor	Crystal Structures and Mutational Analyses of Acyl-CoA Carboxylase Subunit of Streptomyces coelicolor
3IBB	68%	Streptomyces coelicolor	Propionyl-CoA Carboxylase Beta Subunit, D422A
3IB9	68%	Streptomyces coelicolor	Propionyl-CoA Carboxylase Beta Subunit, D422L
3IAV	68%	Streptomyces coelicolor	Propionyl-CoA Carboxylase Beta Subunit, D422V
1XO6	68%	Streptomyces coelicolor	Acyl-CoA Carboxylase Beta Subunit from S. coelicolor (PccB), apo form #3
1XNY	68%	Streptomyces coelicolor	Biotin and propionyl-CoA bound to Acyl-CoA Carboxylase Beta Subunit from S. coelicolor (PccB)
1XNW	68%	Streptomyces coelicolor	Acyl-CoA Carboxylase Beta Subunit from S. coelicolor (PccB), apo form #2, mutant D422I
1XNV	68%	Streptomyces coelicolor	Acyl-CoA Carboxylase Beta Subunit from S. coelicolor (PccB), apo form #1

Links to additional information on accD5:
- TBDB (updated)
- Phyre2 structure prediction, model: final.casp.pdb (from Mao et al, 2013)
- UniProt
- AlphaFold model
- Vulnerability = -11.013 (from Jeremy Rock's lab)
- KEGG - nucleotide and amino acid sequences of gene
- Mycobrowser
- PATRIC
- BioCyc
- Systems Biology

Amino Acid Sequence

MTSVTDRSAHSAERSTEHTIDIHTTAGKLAELHKRREESLHPVGEDAVEKVHAKGKLTARERIYALLDEDSFVELDALAKHRSTNFNLGEKRPLGDGVVT
GYGTIDGRDVCIFSQDATVFGGSLGEVYGEKIVKVQELAIKTGRPLIGINDGAGARIQEGVVSLGLYSRIFRNNILASGVIPQISLIMGAAAGGHVYSPA
LTDFVIMVDQTSQMFITGPDVIKTVTGEEVTMEELGGAHTHMAKSGTAHYAASGEQDAFDYVRELLSYLPPNNSTDAPRYQAAAPTGPIEENLTDEDLEL
DTLIPDSPNQPYDMHEVITRLLDDEFLEIQAGYAQNIVVGFGRIDGRPVGIVANQPTHFAGCLDINASEKAARFVRTCDCFNIPIVMLVDVPGFLPGTDQ
EYNGIIRRGAKLLYAYGEATVPKITVITRKAYGGAYCVMGSKDMGCDVNLAWPTAQIAVMGASGAVGFVYRQQLAEAAANGEDIDKLRLRLQQEYEDTLV
NPYVAAERGYVDAVIPPSHTRGYIGTALRLLERKIAQLPPKKHGNVPL

(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
Essential	Sodium Oleate	H37RvMA	Gumbel	Subhalaxmi Nambi	Probability of Essentiality: 1.000000; 32 non-insertions in a row out of 32 sites
Essential	Lignoceric Acid	H37RvMA	Gumbel	Subhalaxmi Nambi	Probability of Essentiality: 1.000000; 32 non-insertions in a row out of 32 sites
Essential	Phosphatidylcholine	H37RvMA	Gumbel	Subhalaxmi Nambi	Probability of Essentiality: 1.000000; 32 non-insertions in a row out of 32 sites
Essential	minimal media + 0.1% glycerol	H37RvMA	Gumbel	Griffin et al. (2011)	Probability of Essentiality: 1.000000; 32 non-insertions in a row out of 32 sites
Essential	minimal media + 0.01% cholesterol	H37RvMA	Gumbel	Griffin et al. (2011)	Probability of Essentiality: 1.000000; 32 non-insertions in a row out of 32 sites
No-Data	7H10-glycerol	H37RvMA	TraSH	Sassetti et al. (2003a)
Too-Short	C57BL/6J mice (8 weeks)	H37RvMA	TraSH	Sassetti et al. (2003b)	Hybridization Ratio: -1
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

accD5 KO Metabolomic Profile

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)

Binds To:
- No bindings to other targets were found.
Bound By:
- No bindings from other targets were found.

Interactions based on ChIPSeq data (Minch et al. 2014)

Binds To:
- No bindings to other targets were found.
Bound By:
- No bindings to other targets were found.

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

Upregulates:
- Does not upregulate other genes.
Upregulated by:
- Not upregulated by other genes.
Downregulates:
- Does not downregulate other genes.
Downregulated by:
- Not downregulated by other genes.

TBCAP

Tubculosis Community Annotation Project (

Slayden et al., 2013

Rv3280 (accD5)

Property	Value	Creator	Evidence	PMID	Comment
Citation	Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. G. Gago, D. Kurth et al. J. Bacteriol. 2006	njamshidi	IDA	16385038	PMID: 16385038 AccE5 neede for max catalytic activity
Term	EC:6.4.1.2 Acetyl-CoA carboxylase. - IDA	njamshidi	IDA	16385038	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	njamshidi	IDA	16385038	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
Citation	Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. G. Gago, D. Kurth et al. J. Bacteriol. 2006	njamshidi	ISS	16385038	PMID: 16385038 AccE5 neede for max catalytic activity
Term	EC:6.4.1.2 Acetyl-CoA carboxylase. - ISS	njamshidi	ISS	16385038	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	njamshidi	ISS	16385038	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
Citation	Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. G. Gago, D. Kurth et al. J. Bacteriol. 2006	njamshidi	IDA	16385038	PMID: 16385038 AccE5 neede for max catalytic activity
Term	EC:6.4.1.2 Acetyl-CoA carboxylase. - IDA	njamshidi	IDA	16385038	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	njamshidi	IDA	16385038	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
Citation	Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. G. Gago, D. Kurth et al. J. Bacteriol. 2006	njamshidi	ISS	16385038	PMID: 16385038 AccE5 neede for max catalytic activity
Term	EC:6.4.1.2 Acetyl-CoA carboxylase. - ISS	njamshidi	ISS	16385038	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	njamshidi	ISS	16385038	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	sourish10	TAS		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 Rv3281	priti.priety	IDA		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	PhysicalInteraction Rv3281	priti.priety	IDA		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	priti.priety	IDA		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	priti.priety	IDA		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	RegulatedBy Rv1221	yamir.moreno	IEP		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)	mjackson	IDA		Claisen-type condensation
Citation	Identification 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. 2006	mjackson		16354663	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)
Other	TBPWY:Methyl-malonyl-CoA synthesis	mjackson			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
Citation	Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. G. Gago, D. Kurth et al. J. Bacteriol. 2006	mjackson		16385038	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)
Other	TBPWY:Methyl-malonyl-CoA synthesis	mjackson			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
Citation	Structure-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. 2006	mjackson		16492739	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)
Other	TBPWY:Methyl-malonyl-CoA synthesis	mjackson			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
Term	EC:6.4.1.3 Propionyl-CoA carboxylase. - NR	jjmcfadden	NR		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
Citation	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. D. Portevin, C. de Sousa-D'Auria et al. J. Biol. Chem. 2005	jjmcfadden		15632194	Inferred from direct assay
Term	EC:4.1.1.41 Methylmalonyl-CoA decarboxylase. - NR	jjmcfadden	NR		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	jjmcfadden	NR		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	jjmcfadden	NR		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
Citation	Deciphering the biology of Mycobacterium tuberculosis from the complete genome 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 Nature 1998	extern:JZUCKER		9634230	Human inference of function from sequence
Term	EC:6.4.1.2 Acetyl-CoA carboxylase. - NR	extern:JZUCKER	NR		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:6.4.1.3 Propionyl-CoA carboxylase. - NR	extern:JZUCKER	NR		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
Citation	Central 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. 2011	extern:JZUCKER		21561773	Traceable author statement to experimental support
Term	EC:6.4.1.2 Acetyl-CoA carboxylase. - NR	extern:JZUCKER	NR		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	extern:JZUCKER	NR		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
Citation	Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. G. Gago, D. Kurth et al. J. Bacteriol. 2006	extern:JZUCKER		16385038	Inferred from mutant phenotype
Term	EC:6.4.1.2 Acetyl-CoA carboxylase. - NR	extern:JZUCKER	NR		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	extern:JZUCKER	NR		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

Property

Value

Creator

Evidence

PMID

Comment

Citation

Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. G. Gago, D. Kurth et al. J. Bacteriol. 2006

njamshidi

IDA

16385038

PMID: 16385038 AccE5 neede for max catalytic activity

Term

EC:6.4.1.2 Acetyl-CoA carboxylase. - IDA

njamshidi

IDA

16385038

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

njamshidi

IDA

16385038

Citation

Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. G. Gago, D. Kurth et al. J. Bacteriol. 2006

njamshidi

ISS

16385038

PMID: 16385038 AccE5 neede for max catalytic activity

Term

EC:6.4.1.2 Acetyl-CoA carboxylase. - ISS

njamshidi

ISS

16385038

Term

TBRXN:ACCOACr acetyl-CoA carboxylase, reversible reaction - ISS

njamshidi

ISS

16385038

Citation

Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. G. Gago, D. Kurth et al. J. Bacteriol. 2006

njamshidi

IDA

16385038

PMID: 16385038 AccE5 neede for max catalytic activity

Term

EC:6.4.1.2 Acetyl-CoA carboxylase. - IDA

njamshidi

IDA

16385038

Term

TBRXN:ACCOACr acetyl-CoA carboxylase, reversible reaction - IDA

njamshidi

IDA

16385038

Citation

Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. G. Gago, D. Kurth et al. J. Bacteriol. 2006

njamshidi

ISS

16385038

PMID: 16385038 AccE5 neede for max catalytic activity

Term

EC:6.4.1.2 Acetyl-CoA carboxylase. - ISS

njamshidi

ISS

16385038

Term

TBRXN:ACCOACr acetyl-CoA carboxylase, reversible reaction - ISS

njamshidi

ISS

16385038

Interaction

PhysicalInteraction Rv3801c

sourish10

TAS

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 Rv3281

priti.priety

IDA

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

PhysicalInteraction Rv3281

priti.priety

IDA

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

priti.priety

IDA

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

priti.priety

IDA

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

RegulatedBy Rv1221

yamir.moreno

IEP

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

mjackson

IDA

Claisen-type condensation

Citation

Identification 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. 2006

mjackson

16354663

Other

TBPWY:Methyl-malonyl-CoA synthesis

mjackson

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

Citation

Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. G. Gago, D. Kurth et al. J. Bacteriol. 2006

mjackson

16385038

Other

TBPWY:Methyl-malonyl-CoA synthesis

mjackson

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

Citation

Structure-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. 2006

mjackson

16492739

Other

TBPWY:Methyl-malonyl-CoA synthesis

mjackson

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

Term

EC:6.4.1.3 Propionyl-CoA carboxylase. - NR

jjmcfadden

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

Citation

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. D. Portevin, C. de Sousa-D'Auria et al. J. Biol. Chem. 2005

jjmcfadden

15632194

Inferred from direct assay

Term

EC:4.1.1.41 Methylmalonyl-CoA decarboxylase. - NR

jjmcfadden

Term

EC:6.4.1.4 Methylcrotonoyl-CoA carboxylase. - NR

jjmcfadden

Term

EC:6.4.1.2 Acetyl-CoA carboxylase. - NR

jjmcfadden

Citation

Deciphering the biology of Mycobacterium tuberculosis from the complete genome 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 Nature 1998

extern:JZUCKER

9634230

Human inference of function from sequence

Term

EC:6.4.1.2 Acetyl-CoA carboxylase. - NR

extern:JZUCKER

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:6.4.1.3 Propionyl-CoA carboxylase. - NR

extern:JZUCKER

Citation

Central 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. 2011

extern:JZUCKER

21561773

Traceable author statement to experimental support

Term

EC:6.4.1.2 Acetyl-CoA carboxylase. - NR

extern:JZUCKER

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

extern:JZUCKER

Citation

Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. G. Gago, D. Kurth et al. J. Bacteriol. 2006

extern:JZUCKER

16385038

Inferred from mutant phenotype

Term

EC:6.4.1.2 Acetyl-CoA carboxylase. - NR

extern:JZUCKER

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

extern:JZUCKER

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

Comments