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Gene: Rv0241c

General annotation | Coordinates | Sequence | Genome Browser | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography


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General annotation
Gene namehtdX
Rv numberRv0241c
TypeCDS
FunctionINVOLVED IN FATTY ACID SYNTHESIS TYPE II (FAS-II)
ProductPROBABLE 3-HYDROXYACYL-THIOESTER DEHYDRATASE HTDX
Evidenceexperimental
CommentsRv0241c, (MTV034.07c), len: 280 aa. Probable htdX, 3-hydroxyacyl-thioester dehydratase (See Gurvitz et al., 2009), highly similar to MLCB1883.17c|T44876063881|CAA18566.1|AL022486 hypothetical protein from Mycobacterium leprae (280 aa), FASTA scores: opt: 1564, E(): 0, (81.8% identity in 280 aa overlap); and CAC32097.1|AL583926 conserved hypothetical protein from Mycobacterium leprae (300 aa). Shows structural similarity to six others in Mycobacterium tuberculosis (see Castell et al (2005) below). Also similar to proteins from other organisms e.g. CAB77291.1|AL160312 putative dehydratase from Streptomyces coelicolor (291 aa); part of BAA92930.1|AB032743 fatty acid synthetase beta subunit from Pichia angusta (2060 aa).
Molecular mass (Da)30162.8
Isoelectric point10.5111
Gene length (bp)843
Protein length280
Location (kb)290.654


Functional categoryintermediary metabolism and respiration


ProteomicsIdentified in the membrane fraction of M. tuberculosis H37Rv using 1D-SDS-PAGE and uLC-MS/MS (See Gu et al., 2003).
TranscriptomemRNA identified by microarray analysis and down-regulated after 24h of starvation (see citation below).
Mutationnon essential gene by Himar1-based transposon mutagenesis in H37Rv and CDC1551 strains (see Sassetti et al., 2003 and Lamichhane et al., 2003). Found to be deleted (partially or completely) in one or more clinical isolates (See Tsolaki et al., 2004). mutants available at TARGET website


Coordinates
TypeStartEndOrientation
CDS289812290654-
RBS290663290666-


Protein sequence in FASTA format
>M. tuberculosis H37Rv | htdX
MTQPSGLKNLLRAAAGALPVVPRTDQLPNRTVTVEELPIDPANVAAYAAVTGLRYGNQVPLTYPFALTFPSVMSLVTGFD
FPFAAMGAIHTENHITQYRPIAVTDAVGVRVRAENLREHRRGLLVDLVTNVSVGNDVAWHQVTTFLHQQRTSLSGEPKPP
PQKKPKLPPPAAVLRITPAKIRRYAAVGGDHNPIHTNPIAAKLFGFPTVIAHGMFTAAAVLANIEARFPDAVRYSVRFAK
PVLLPATAGLYVAEGDGGWDLTLRNMAKGYPHLTATVRGL
Blastp: results
TransMembrane prediction using Hidden Markov Models: tmhmm
Microbe Genome Browser
Genomic sequence

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



Structural information
Protein Data BankNo structure available
PFAMProtein Family Domains


Orthologs/Cross-references
CDC1551MT0255
Gene Ontologyfatty-acid synthase activity
fatty acid synthase complex
fatty acid biosynthetic process
oxidoreductase activity
oxidation reduction
MbovisMb0247c
MlepraeML2566
MmarinumMMAR_0502
MsmegmatisMSMEG_0371
UniProtO53664


Interacting Drugs/Compounds
TDR TargetsRv0241c


Expression Data
TBDBRv0241c


Bibliography
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 :717
Sassetti CM, Boyd DH, Rubin EJ,
Genes required for mycobacterial growth defined by high density mutagenesis.
Mol Microbiol (2003) 48(1):77-84
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 :7213
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
Tsolaki AG, Hirsh AE, DeRiemer K, Enciso JA, Wong MZ, Hannan M, Goguet de la Salmoniere YO, Aman K, Kato-Maeda M, Small PM,
Functional and evolutionary genomics of Mycobacterium tuberculosis: insights from genomic deletions in 100 strains.
Proc Natl Acad Sci U S A (2004) 101(14):4865-70
Castell A, Johansson P, Unge T, Jones TA, Backbro K,
Rv0216, a conserved hypothetical protein from Mycobacterium tuberculosis that is essential for bacterial survival during infection, has a double hotdog fold
Protein Sci (2005) 14(7):1850
Gurvitz A, Hiltunen JK, Kastaniotis AJ,
Heterologous expression of mycobacterial proteins in Saccharomyces cerevisiae reveals two physiologically functional 3-hydroxyacyl-thioester dehydratases HtdX and HtdY, in addition to HadABC and HtdZ.
J Bacteriol (2009) 191(8):2683-90