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Search term: Rv3318

General annotation | Coordinates | Sequence | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography
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General annotation
Gene namesdhA
Rv numberRv3318
FunctionInvolved in tricarboxylic acid cycle. Membrane-bound FAD-containing enzyme which is responsible for succinate interconversion [catalytic activity: succinate + acceptor = fumarate + reduced acceptor].
ProductProbable succinate dehydrogenase (flavoprotein subunit) SdhA (succinic dehydrogenase) (fumarate reductase) (fumarate dehydrogenase) (fumaric hydrogenase)
CommentsRv3318, (MTV016.18), len: 590 aa. Probable sdhA, flavoprotein of succinate dehydrogenase SdhA subunit, equivalent to Q9CCM1|SDHA|ML0697 succinate dehydrogenase flavoprotein subunit from Mycobacterium leprae (584 aa), FASTA scores: opt: 3657, E(): 1.2e-217, (92.55% identity in 590 aa overlap). Also highly similar to others e.g. Q9KZ90|DHSA from Streptomyces coelicolor (584 aa), FASTA scores: opt: 2813, E(): 1.1e-165, (70.5% identity in 586 aa overlap); Q9RVS0|DR0952 from Deinococcus radiodurans (583 aa), FASTA scores: opt: 2203, E(): 4.1e-128, (57.35% identity in 593 aa overlap); P31038|DHSA_RICPR|SDHA|RP128 from Rickettsia prowazekii (596 aa), FASTA scores: opt: 1892, E(): 5.8e-109, (50.0% identity in 588 aa overlap); P10444|DHSA_ECOLI|SDHA|B0723|Z0877|ECS0748 from Escherichia coli strains K12 and O157:H7 (588 aa), FASTA scores: opt: 1844, E(): 5.2e-106, (48.75% identity in 591 aa overlap); etc. Contains PS00504 Fumarate reductase / succinate dehydrogenase FAD-binding site. Cofactor: FAD. Similar to the flavoprotein subunits of other species succinate dehydrogenase and of fumarate reductase. Part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur, cytochrome B-556, and an hydrophobic anchor protein.
Molecular mass (Da)64807.5
Isoelectric point5.9775
Gene length (bp)1773
Protein length590
Location (kb)3705

Functional categoryintermediary metabolism and respiration

ProteomicsIdentified in the cytosol and cell membrane fraction of M. tuberculosis H37Rv using 2DLC/MS (See Mawuenyega et al., 2005). Identified by mass spectrometry in Triton X-114 extracts of M. tuberculosis H37Rv (See Malen et al., 2010). Identified by mass spectrometry in M. tuberculosis H37Rv-infected guinea pig lungs at 30 and 90 days (See Kruh 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 and CDC1551 strains (see Sassetti et al., 2003 and Lamichhane et al., 2003). Check for mutants available at TARGET website


Protein sequence in FASTA format
>M. tuberculosis H37Rv|Rv3318|sdhA
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 Classification1.3.99.1
Gene Ontologysuccinate dehydrogenase activity
tricarboxylic acid cycle
electron carrier activity
electron transport chain
FAD binding
M. bovisMb3347
M. lepraeML0697
M. marinumMMAR_1201
M. smegmatisMSMEG_1670
Multiple Sequences Alignment: between orthologs

Interacting Drugs/Compounds
TDR TargetsRv3318

Expression Data

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
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
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
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