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Search term: Rv1079

General annotation | Coordinates | Sequence | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography
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General annotation
Gene namemetB
Rv numberRv1079
FunctionInvolved in methionine biosynthesis: converts O-succinyl-L-homoserine to cystathionine [catalytic activity: O-succinyl-L-homoserine + L-cysteine = cystathionine + succinate (can also use hydrogen sulfide and methanethiol as substrates)].
ProductCystathionine gamma-synthase MetB (CGS) (O-succinylhomoserine [thiol]-lyase)
CommentsRv1079, (MTV017.32), len: 388 aa. metB, cystathionine gamma-synthase (see citation below). P46807|METB_MYCLE cystathionine gamma-synthase from Mycobacterium leprae (388 aa), FASTA scores: opt: 2220, E(): 0, (87.3% identity in 387 aa overlap). Also similar to other Mycobacterium tuberculosis enzymes involved in methionine synthesis e.g. Rv0391 and Rv3340. Contains PS00868 Cys/Met metabolism enzymes pyridoxal-phosphate attachment site. Belongs to the trans-sulfuration enzymes family.
Molecular mass (Da)40982.3
Isoelectric point5.0962
Gene length (bp)1167
Protein length388
Location (kb)1204.07

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). 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).
Mutationnon essential gene by Himar1-based transposon mutagenesis in H37Rv strain (see Sassetti et al., 2003). Required for survival in primary murine macrophages, by transposon site hybridization (TraSH) in H37Rv (See Rengarajan et al., 2005).
see TB knockouts/mutants availability


Protein sequence in FASTA format
>M. tuberculosis H37Rv|Rv1079|metB
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

Enzyme Classification2.5.1.48
Gene Ontologycystathionine gamma-synthase activity
methionine biosynthetic process
pyridoxal phosphate binding
M. bovisMb1108
M. lepraeML2394
M. marinumMMAR_4388
M. smegmatisMSMEG_5265
Multiple Sequences Alignment: between orthologs

Interacting Drugs/Compounds
TDR TargetsRv1079

Expression Data

Parish T, Gordhan BG, McAdam RA, Duncan K, Mizrahi V, Stoker NG,
Production of mutants in amino acid biosynthesis genes of Mycobacterium tuberculosis by homologous recombination
Microbiology (1999) 145(Pt 12):3497-503
Cited for: Mutant
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
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
Rengarajan J, Bloom BR, Rubin EJ,
Genome-wide requirements for Mycobacterium tuberculosis adaptation and survival in macrophages.
Proc Natl Acad Sci U S A (2005) 102(23):8327-32
Cited for: Mutant
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, 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