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Search term: Rv2243

General annotation | Coordinates | Sequence | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography
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General annotation
Gene namefabD
Rv numberRv2243
Synonym(s)mtFabD
TypeCDS
FunctionCatalyzes malonyl-CoA-ACP transacylase (MCAT) activity using holo-ACPM as substrate for transacylation [catalytic activity: malonyl-CoA + [acyl-carrier protein] = CoA + malonyl-[acyl-carrier protein]].
ProductMalonyl CoA-acyl carrier protein transacylase FabD (malonyl CoA:ACPM acyltransferase) (MCT)
CommentsRv2243, (MTCY427.24), len: 302 aa. FabD (alternate gene name: mtFabD), malonyl CoA-acyl carrier protein transacylase (see citations below), highly similar to e.g. A57356 acyl-CoA carrier protein malonyltransferase from Streptomyces coelicolor (316 aa), FASTA score: opt: 955, E(): 0, (52.6% identity in 304 aa overlap); FABD_HAEIN|P43712 malonyl CoA-acyl carrier protein transacylase from Haemophilus influenzae, FASTA score: (30.5% identity in 308 aa overlap); and FABD_ECOLI|P25715 from Escherichia coli, FASTA score: (31.4% identity in 309 aa overlap). Identified as a substrate for proteasomal degradation (See Pearce et al., 2006).
Molecular mass (Da)30756.1
Isoelectric point4.5962
Gene length (bp)909
Protein length302
Location (kb)2516.79


Functional categorylipid metabolism


ProteomicsIdentified by mass spectrometry in M. tuberculosis H37Rv-infected guinea pig lungs at 30 days but not 90 days (See Kruh et al., 2010).
TranscriptomemRNA identified by DNA microarray analysis (gene induced by isoniazid (INH) or ethionamide treatment) (see Wilson et al., 1999). mRNA also identified by other microarray analysis and real-time RT-PCR; transcription up-repressed at low pH in vitro conditions, which may mimic an environmental signal encountered by phagocytosed bacteria (see Fisher et al., 2002). DNA microarrays show increased expression in M. tuberculosis H37Rv in BALB/c mice compared to SCID mice, after 21 days of infection (See Talaat et al., 2004).
Mutation Check for mutants available at TARGET website


Coordinates
TypeStartEndOrientation
CDS25167872517695+


Protein sequence in FASTA format
>M. tuberculosis H37Rv|Rv2243|fabD
VIALLAPGQGSQTEGMLSPWLQLPGAADQIAAWSKAADLDLARLGTTASTEEITDTAVAQ
PLIVAATLLAHQELARRCVLAGKDVIVAGHSVGEIAAYAIAGVIAADDAVALAATRGAEM
AKACATEPTGMSAVLGGDETEVLSRLEQLDLVPANRNAAGQIVAAGRLTALEKLAEDPPA
KARVRALGVAGAFHTEFMAPALDGFAAAAANIATADPTATLLSNRDGKPVTSAAAAMDTL
VSQLTQPVRWDLCTATLREHTVTAIVEFPPAGTLSGIAKRELRGVPARAVKSPADLDELA
NL
Blastp: Pre-computed results
TransMembrane prediction using Hidden Markov Models: TMHMM
Genomic sequence

Add extra bases upstream (5') and downstream (3')



Structural information
PFAMP63458
Protein Data Bank2QC3 2QJ3


Orthologs/Cross-references
CDC1551MT2303
Enzyme Classification2.3.1.39
Gene Ontology[acyl-carrier-protein] S-malonyltransferase activity
fatty acid biosynthetic process
M. bovisMb2267
M. lepraeML1653
M. marinumMMAR_3336
M. smegmatisMSMEG_4325
UniProtP63458
Multiple Sequences Alignment: between orthologs


Interacting Drugs/Compounds
TDR TargetsRv2243
Drug Resistance MutationsIsoniazid


Expression Data
TBDBRv2243


Bibliography
Wilson M, DeRisi J, Kristensen HH, Imboden P, Rane S, Brown PO, Schoolnik GK,
Exploring drug-induced alterations in gene expression in Mycobacterium tuberculosis by microarray hybridization
Proc Natl Acad Sci U S A (1999) 96(22):12833-8
Cited for: Regulation
Kremer L, Nampoothiri KM, Lesjean S, Dover LG, Graham S, Betts J, Brennan PJ, Minnikin DE, Locht C, Besra GS,
Biochemical characterization of acyl carrier protein (AcpM) and malonyl-CoA:AcpM transacylase (mtFabD), two major components of Mycobacterium tuberculosis fatty acid synthase II
J Biol Chem (2001) 276(30):27967-74
Cited for: Product/Mutant/Biochemistry/Function
Fisher MA, Plikaytis BB, Shinnick TM,
Microarray analysis of the Mycobacterium tuberculosis transcriptional response to the acidic conditions found in phagosomes
J Bacteriol (2002) 184(14):4025-32
Cited for: Transcriptome/Regulation
Talaat AM, Lyons R, Howard ST, Johnston SA,
The temporal expression profile of Mycobacterium tuberculosis infection in mice.
Proc Natl Acad Sci U S A (2004) 101(13):4602-7
Cited for: Transcriptome
Pearce MJ, Arora P, Festa RA, Butler-Wu SM, Gokhale RS, Darwin KH,
Identification of substrates of the Mycobacterium tuberculosis proteasome.
EMBO J (2006) 25(22):5423-32
Cited for: Biochemistry
Li Z, Huang Y, Ge J, Fan H, Zhou X, Li S, Bartlam M, Wang H, Rao Z,
The crystal structure of MCAT from Mycobacterium tuberculosis reveals three new catalytic models.
J Mol Biol (2007) 371(4):1075-83
Cited for: Structure
Ghadbane H, Brown AK, Kremer L, Besra GS, Futterer K,
Structure of Mycobacterium tuberculosis mtFabD, a malonyl-CoA:acyl carrier protein transacylase (MCAT).
Acta Crystallogr Sect F Struct Biol Cryst Commun (2007) 63(Pt 10):831-5
Cited for: Structure
Pearce MJ, Mintseris J, Ferreyra J, Gygi SP, Darwin KH,
Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis.
Science (2008) 322(5904):1104-7
Cited for: Biochemistry
Kruh NA, Troudt J, Izzo A, Prenni J, Dobos KM,
Portrait of a pathogen: the Mycobacterium tuberculosis proteome in vivo.
PLoS One (2010) 5(11):e13938
Cited for: Proteomics
Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Barrell BG, et al,
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
Nature (1998) 393(6685):537-44
Cited for: Sequence/Secondary
Kremer L, Baulard AR, Besra GS,
Molecular Genetics of Mycobacteria; Eleventh chapter: Genetics of Mycolic Acid Biosynthesis
ASM Press (2000) 1-55581-191-4:173-190
Cited for: Review