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Search term: Rv0363c

General annotation | Coordinates | Sequence | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography
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General annotation
Gene namefba
Rv numberRv0363c
FunctionInvolved in glycolysis (at the sixth step) [catalytic activity: D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate].
ProductProbable fructose-bisphosphate aldolase Fba
CommentsRv0363c, (MTCY13E10.25c), len: 344 aa. Probable fba (alternate gene name: fda), fructose bisphosphate aldolase , equivalent to AL023514|MLCB4_18|O69600|ALF_MYCLE fructose-bisphosphate aldolase from Mycobacterium leprae (345 aa), FASTA scores: opt: 1995, E(): 0, (87.7% identity in 342 aa overlap). Also highly similar to others. Belongs to class II fructose-bisphosphate aldolase family. Cofactor: zinc.
Molecular mass (Da)36544.5
Isoelectric point5.5853
Gene length (bp)1035
Protein length344
Location (kb)441.265

Functional categoryintermediary metabolism and respiration

ProteomicsIdentified by proteomics at the Max Planck Institute for Infection Biology, Berlin, Germany, and at the Statens Serum Institute (Denmark) under aerobic and low oxygen conditions (see citations below). Identified in the membrane fraction of M. tuberculosis H37Rv using 1D-SDS-PAGE and uLC-MS/MS (See Gu et al., 2003). Identified in the culture supernatant of M. tuberculosis H37Rv using mass spectrometry (See Mattow et al., 2003). Identified in culture filtrates of M. tuberculosis H37Rv (See Malen et al., 2007). Identified by mass spectrometry in Triton X-114 extracts of M. tuberculosis H37Rv (See Malen et al., 2010). Identified by mass spectrometry in the culture filtrate, membrane protein fraction, and whole cell lysates of M. tuberculosis H37Rv (See de Souza et al., 2011). Translational start site supported by proteomics data (See de Souza et al., 2011) (See Kelkar et al., 2011).
MutationEssential 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


Protein sequence in FASTA format
>M. tuberculosis H37Rv|Rv0363c|fba
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 Bank3EKL 3EKZ 3ELF 4A21 4A22

Enzyme Classification4.1.2.13
Gene Ontologyfructose-bisphosphate aldolase activity
zinc ion binding
M. bovisMb0370c
M. lepraeML0286
M. marinumMMAR_0669
M. smegmatisMSMEG_0752
Multiple Sequences Alignment: between orthologs

Interacting Drugs/Compounds
TDR TargetsRv0363c

Expression Data

Jungblut PR, Schaible UE, Mollenkopf HJ, Zimny-Arndt U, Zimny -Arndt U, Raupach B, Mattow J, Halada P, Lamer S, Hagens K, Kaufmann SH,
Comparative proteome analysis of Mycobacterium tuberculosis and Mycobacterium bovis BCG strains: towards functional genomics of microbial pathogens
Mol Microbiol (1999) 33(6):1103-17
Cited for: Proteomics
Rosenkrands I, King A, Weldingh K, Moniatte M, Moertz E, Andersen P,
Towards the proteome of Mycobacterium tuberculosis
Electrophoresis (2000) 21(17):3740-56
Cited for: Proteomics
Rosenkrands I, Slayden RA, Crawford J, Aagaard C, Barry III CE, Andersen P,
Hypoxic response of Mycobacterium tuberculosis studied by metabolic labeling and proteome analysis of cellular and extracellular proteins
J Bacteriol (2002) 184(13):3485-91
Cited for: Proteomics/Regulation
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
Mattow J, Schaible UE, Schmidt F, Hagens K, Siejak F, Brestrich G, Haeselbarth G, Muller EC, Jungblut PR, Kaufmann SH,
Comparative proteome analysis of culture supernatant proteins from virulent Mycobacterium tuberculosis H37Rv and attenuated M. bovis BCG Copenhagen.
Electrophoresis (2003) 24(19-20):3405-20
Cited for: Proteomics
Malen H, Berven FS, Fladmark KE, Wiker HG,
Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv.
Proteomics (2007) 7(10):1702-18
Cited for: Proteomics
Pegan SD, Rukseree K, Franzblau SG, Mesecar AD,
Structural basis for catalysis of a tetrameric class IIa fructose 1,6-bisphosphate aldolase from Mycobacterium tuberculosis.
J Mol Biol (2009) 386(4):1038-53
Cited for: Structure
Malen H, Pathak S, Softeland T, de Souza GA, Wiker HG,
Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv.
BMC Microbiol (2010) 10:132
Cited for: Proteomics
de Souza GA, Arntzen MO, Fortuin S, Schurch AC, Malen H, McEvoy CR, van Soolingen D, Thiede B, Warren RM, Wiker HG,
Proteogenomic analysis of polymorphisms and gene annotation divergences in prokaryotes using a clustered mass spectrometry-friendly database.
Mol Cell Proteomics (2011) 10(1):M110.002527
Cited for: Proteomics/Sequence
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