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Search term: Rv2524c

General annotation | Coordinates | Sequence | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography
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General annotation
Gene namefas
Rv numberRv2524c
TypeCDS
FunctionInvolved in lipid metabolism. Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH.
ProductProbable fatty acid synthase Fas (fatty acid synthetase)
CommentsRv2524c, (MTCY159.32, MTV009.09c), len: 3069 aa. Probable fas, Fatty Acid Synthase, equivalent to Q9X7E2|fas|ML1191 putative type I fatty acid synthase from Mycobacterium leprae (3076 aa), FASTA scores: opt: 17484, E(): 0, (85.8% identity in 3081 aa overlap). Also similar to others e.g. Q04846|fas|Q59497 from Corynebacterium ammoniagenes (Brevibacterium ammoniagenes) (3104 aa), FASTA scores: opt: 3981, E(): 5.5e-203, (49.8% identity in 3099 aa overlap); Q48926|fas from Mycobacterium bovis (2796 aa), FASTA scores: opt: 2098, E(): 3.9e-103, (59.7% identity in 2862 aa overlap) (see Fernandes et al., 1996); P34731|FAS1_CANAL fatty acid synthase subunit beta from Candida albicans (Yeast) (2037 aa), FASTA scores: opt: 955, E(): 1.3e-42, (27.4% identity in 1926 aa overlap); etc. Contains PS00017 ATP/GTP-binding site motif A (P-loop), and PS00606 Beta-ketoacyl synthases active site.
Molecular mass (Da)326222
Isoelectric point4.7804
Gene length (bp)9210
Protein length3069
Location (kb)2840.12


Functional categorylipid metabolism


ProteomicsIdentified in the membrane fraction of M. tuberculosis H37Rv using 1D-SDS-PAGE and uLC-MS/MS (See Gu et al., 2003). Identified in the cytosol, cell wall, and cell membrane fractions of M. tuberculosis H37Rv using 2DLC/MS (See Mawuenyega et al., 2005). Identified by mass spectrometry in M. tuberculosis H37Rv-infected guinea pig lungs at 30 days but not 90 days (See Kruh et al., 2010). Identified by mass spectrometry in whole cell lysates of M. tuberculosis H37Rv but not the culture filtrate or membrane protein fraction (See de Souza et al., 2011). Translational start site supported by proteomics data (See Kelkar et al., 2011).
TranscriptomemRNA identified by microarray analysis and down-regulated after 4h, 24h and 96h of starvation (see Betts et al., 2002).
Mutationessential gene by Himar1-based transposon mutagenesis in H37Rv and CDC1551 strains (see Sassetti et al., 2003 and Lamichhane et al., 2003). Essential gene for in vitro growth of H37Rv, by sequencing of Himar1-based transposon mutagenesis (See Griffin et al., 2011). Check for mutants available at TARGET website


Coordinates
TypeStartEndOrientation
CDS28401232849332-
RBS28493422849345-


Protein sequence in FASTA format
>M. tuberculosis H37Rv|Rv2524c|fas
VTIHEHDRVSADRGGDSPHTTHALVDRLMAGEPYAVAFGGQGSAWLETLEELVSATGIET
ELATLVGEAELLLDPVTDELIVVRPIGFEPLQWVRALAAEDPVPSDKHLTSAAVSVPGVL
LTQIAATRALARQGMDLVATPPVAMAGHSQGVLAVEALKAGGARDVELFALAQLIGAAGT
LVARRRGISVLGDRPPMVSVTNADPERIGRLLDEFAQDVRTVLPPVLSIRNGRRAVVITG
TPEQLSRFELYCRQISEKEEADRKNKVRGGDVFSPVFEPVQVEVGFHTPRLSDGIDIVAG
WAEKAGLDVALARELADAILIRKVDWVDEITRVHAAGARWILDLGPGDILTRLTAPVIRG
LGIGIVPAATRGGQRNLFTVGATPEVARAWSSYAPTVVRLPDGRVKLSTKFTRLTGRSPI
LLAGMTPTTVDAKIVAAAANAGHWAELAGGGQVTEEIFGNRIEQMAGLLEPGRTYQFNAL
FLDPYLWKLQVGGKRLVQKARQSGAAIDGVVISAGIPDLDEAVELIDELGDIGISHVVFK
PGTIEQIRSVIRIATEVPTKPVIMHVEGGRAGGHHSWEDLDDLLLATYSELRSRANITVC
VGGGIGTPRRAAEYLSGRWAQAYGFPLMPIDGILVGTAAMATKESTTSPSVKRMLVDTQG
TDQWISAGKAQGGMASSRSQLGADIHEIDNSASRCGRLLDEVAGDAEAVAERRDEIIAAM
AKTAKPYFGDVADMTYLQWLRRYVELAIGEGNSTADTASVGSPWLADTWRDRFEQMLQRA
EARLHPQDFGPIQTLFTDAGLLDNPQQAIAALLARYPDAETVQLHPADVPFFVTLCKTLG
KPVNFVPVIDQDVRRWWRSDSLWQAHDARYDADAVCIIPGTASVAGITRMDEPVGELLDR
FEQAAIDEVLGAGVEPKDVASRRLGRADVAGPLAVVLDAPDVRWAGRTVTNPVHRIADPA
EWQVHDGPENPRATHSSTGARLQTHGDDVALSVPVSGTWVDIRFTLPANTVDGGTPVIAT
EDATSAMRTVLAIAAGVDSPEFLPAVANGTATLTVDWHPERVADHTGVTATFGEPLAPSL
TNVPDALVGPCWPAVFAAIGSAVTDTGEPVVEGLLSLVHLDHAARVVGQLPTVPAQLTVT
ATAANATDTDMGRVVPVSVVVTGADGAVIATLEERFAILGRTGSAELADPARAGGAVSAN
ATDTPRRRRRDVTITAPVDMRPFAVVSGDHNPIHTDRAAALLAGLESPIVHGMWLSAAAQ
HAVTATDGQARPPARLVGWTARFLGMVRPGDEVDFRVERVGIDQGAEIVDVAARVGSDLV
MSASARLAAPKTVYAFPGQGIQHKGMGMEVRARSKAARKVWDTADKFTRDTLGFSVLHVV
RDNPTSIIASGVHYHHPDGVLYLTQFTQVAMATVAAAQVAEMREQGAFVEGAIACGHSVG
EYTALACVTGIYQLEALLEMVFHRGSKMHDIVPRDELGRSNYRLAAIRPSQIDLDDADVP
AFVAGIAESTGEFLEIVNFNLRGSQYAIAGTVRGLEALEAEVERRRELTGGRRSFILVPG
IDVPFHSRVLRVGVAEFRRSLDRVMPRDADPDLIIGRYIPNLVPRLFTLDRDFIQEIRDL
VPAEPLDEILADYDTWLRERPREMARTVFIELLAWQFASPVRWIETQDLLFIEEAAGGLG
VERFVEIGVKSSPTVAGLATNTLKLPEYAHSTVEVLNAERDAAVLFATDTDPEPEPEEDE
PVAESPAPDVVSEAAPVAPAASSAGPRPDDLVFDAADATLALIALSAKMRIDQIEELDSI
ESITDGASSRRNQLLVDLGSELNLGAIDGAAESDLAGLRSQVTKLARTYKPYGPVLSDAI
NDQLRTVLGPSGKRPGAIAERVKKTWELGEGWAKHVTVEVALGTREGSSVRGGAMGHLHE
GALADAASVDKVIDAAVASVAARQGVSVALPSAGSGGGATIDAAALSEFTDQITGREGVL
ASAARLVLGQLGLDDPVNALPAAPDSELIDLVTAELGADWPRLVAPVFDPKKAVVFDDRW
ASAREDLVKLWLTDEGDIDADWPRLAERFEGAGHVVATQATWWQGKSLAAGRQIHASLYG
RIAAGAENPEPGRYGGEVAVVTGASKGSIAASVVARLLDGGATVIATTSKLDEERLAFYR
TLYRDHARYGAALWLVAANMASYSDVDALVEWIGTEQTESLGPQSIHIKDAQTPTLLFPF
AAPRVVGDLSEAGSRAEMEMKVLLWAVQRLIGGLSTIGAERDIASRLHVVLPGSPNRGMF
GGDGAYGEAKSALDAVVSRWHAESSWAARVSLAHALIGWTRGTGLMGHNDAIVAAVEEAG
VTTYSTDEMAALLLDLCDAESKVAAARSPIKADLTGGLAEANLDMAELAAKAREQMSAAA
AVDEDAEAPGAIAALPSPPRGFTPAPPPQWDDLDVDPADLVVIVGGAEIGPYGSSRTRFE
MEVENELSAAGVLELAWTTGLIRWEDDPQPGWYDTESGEMVDESELVQRYHDAVVQRVGI
REFVDDGAIDPDHASPLLVSVFLEKDFAFVVSSEADARAFVEFDPEHTVIRPVPDSTDWQ
VIRKAGTEIRVPRKTKLSRVVGGQIPTGFDPTVWGISADMAGSIDRLAVWNMVATVDAFL
SSGFSPAEVMRYVHPSLVANTQGTGMGGGTSMQTMYHGNLLGRNKPNDIFQEVLPNIIAA
HVVQSYVGSYGAMIHPVAACATAAVSVEEGVDKIRLGKAQLVVAGGLDDLTLEGIIGFGD
MAATADTSMMCGRGIHDSKFSRPNDRRRLGFVEAQGGGTILLARGDLALRMGLPVLAVVA
FAQSFGDGVHTSIPAPGLGALGAGRGGKDSPLARALAKLGVAADDVAVISKHDTSTLAND
PNETELHERLADALGRSEGAPLFVVSQKSLTGHAKGGAAVFQMMGLCQILRDGVIPPNRS
LDCVDDELAGSAHFVWVRDTLRLGGKFPLKAGMLTSLGFGHVSGLVALVHPQAFIASLDP
AQRADYQRRADARLLAGQRRLASAIAGGAPMYQRPGDRRFDHHAPERPQEASMLLNPAAR
LGDGEAYIG
Blastp: Pre-computed results
TransMembrane prediction using Hidden Markov Models: TMHMM
Genomic sequence

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



Structural information
Protein Data BankNo structure available
PFAMP95029


Orthologs/Cross-references
CDC1551MT2600
Enzyme Classification2.3.1.-
Gene Ontologyfatty acid synthase activity
fatty acid synthase complex
fatty acid biosynthetic process
oxidoreductase activity
oxidation reduction
M. bovisMb2553c
M. lepraeML1191
M. marinumMMAR_3962
M. smegmatisMSMEG_4757
UniProtP95029
Multiple Sequences Alignment: between orthologs


Interacting Drugs/Compounds
TDR TargetsRv2524c


Expression Data
TBDBRv2524c


Bibliography
Zimhony O, Cox JS, Welch JT, Vilcheze C, Jacobs WR,
Pyrazinamide inhibits the eukaryotic-like fatty acid synthetase I (FASI) of Mycobacterium tuberculosis.
Nat Med (2000) 6(9):1043-7
Cited for: Biochemistry
Boshoff HI, Mizrahi V, Barry CE,
Effects of pyrazinamide on fatty acid synthesis by whole mycobacterial cells and purified fatty acid synthase I.
J Bacteriol (2002) 184(8):2167-72
Cited for: Biochemistry
Betts JC, Lukey PT, Robb LC, McAdam RA, Duncan K,
Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling
Mol Microbiol (2002) 43(3):717-31
Cited for: Transcriptome
Sassetti CM, Boyd DH, Rubin EJ,
Genes required for mycobacterial growth defined by high density mutagenesis.
Mol Microbiol (2003) 48(1):77-84
Cited for: Mutant
Lamichhane G, Zignol M, Blades NJ, Geiman DE, Dougherty A, Grosset J, Broman KW, Bishai WR,
A postgenomic method for predicting essential genes at subsaturation levels of mutagenesis: application to Mycobacterium tuberculosis.
Proc Natl Acad Sci U S A (2003) 100(12):7213-8
Cited for: Mutant
Gu S, Chen J, Dobos KM, Bradbury EM, Belisle JT, Chen X,
Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain.
Mol Cell Proteomics (2003) 2(12):1284-96
Cited for: Proteomics
Zimhony O, Vilcheze C, Jacobs WR,
Characterization of Mycobacterium smegmatis expressing the Mycobacterium tuberculosis fatty acid synthase I (fas1) gene.
J Bacteriol (2004) 186(13):4051-5
Cited for: Function
Mawuenyega KG, Forst CV, Dobos KM, Belisle JT, Chen J, Bradbury EM, Bradbury AR, Chen X,
Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling.
Mol Biol Cell (2005) 16(1):396-404
Cited for: Proteomics
Ngo SC, Zimhony O, Chung WJ, Sayahi H, Jacobs WR, Welch JT,
Inhibition of isolated Mycobacterium tuberculosis fatty acid synthase I by pyrazinamide analogs.
Antimicrob Agents Chemother (2007) 51(7):2430-5
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
de Souza GA, Leversen NA, Malen H, Wiker HG,
Bacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathway.
J Proteomics (2011) 75(2):502-10
Cited for: Proteomics
Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A,
Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry.
Mol Cell Proteomics (2011) 10(12):M111.011627
Cited for: Proteomics/Sequence
Griffin JE, Gawronski JD, Dejesus MA, Ioerger TR, Akerley BJ, Sassetti CM,
High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism.
PLoS Pathog (2011) 7(9):e1002251
Cited for: Mutant
Fernandes ND, Kolattukudy PE,
Cloning, sequencing and characterization of a fatty acid synthase-encoding gene from Mycobacterium tuberculosis var. bovis BCG
Gene (1996) 170(1):95-9
Cited for: Homolog/Sequence