TB Genome Annotation Portal

Rv3318 (sdhA)

• Current annotations:
  • TBCAP: (community-based annotations - see table at bottom of page)
  • TBDB: succinate dehydrogenase flavoprotein subunit
  • REFSEQ: succinate dehydrogenase flavoprotein subunit
  • PATRIC: Succinate dehydrogenase flavoprotein subunit (EC 1.3.99.1)
  • TUBERCULIST: Probable succinate dehydrogenase (flavoprotein subunit) SdhA (succinic dehydrogenase) (fumarate reductase) (fumarate dehydrogenase) (fumaric hydrogenase)
  • NCBI: Probable succinate dehydrogenase (flavoprotein subunit) SdhA (succinic dehydrogenase) (fumarate reductase) (fumarate dehydrogenase) (fumaric hydrogenase)
  • updated information (H37Rv4):
    • gene name: sdhA
    • function:
    • reference:
• Type: Not Target
• Start: 3705000
• End: 3706772
• Operon:


• Trans-membrane region:
  
• Role: I.B.3 - TCA cycle
• GO terms:
  • GO:0055114 - oxidation-reduction process (Uniprot)
  • GO:0050660 - flavin adenine dinucleotide binding (Uniprot)
  • GO:0022900 - electron transport chain (Uniprot)
  • GO:0016627 - oxidoreductase activity, acting on the CH-CH group of donors (Uniprot)
  • GO:0016491 - oxidoreductase activity (Uniprot)
  • GO:0016020 - membrane (Uniprot)
  • GO:0008177 - succinate dehydrogenase (ubiquinone) activity (Uniprot)
  • GO:0006099 - tricarboxylic acid cycle (Uniprot)
  • GO:0005886 - plasma membrane (Uniprot)
  • GO:0005829 - cytosol (Uniprot)
• Reaction(s) (based on iSM810 metabolic model):
  • SUCC[c] + FAD[c] <=> FUM[c] + FADH2[c]
  • MK[c] + SUCC[c] <=> MKH2[c] + FUM[c]
• Gene Expression Profile (Transcriptional Responses to Drugs; Boshoff et al, 2004)
• Gene Modules extracted from cluster analysis of 249 transcriptomic datasets using ICA
• Orthologs among selected mycobacteria
• Protein structure:
• Search for Homologs in PDB
• Top 10 Homologs in PDB (as of Nov 2020):
  

  PDB	aa ident	species	PDB title
  6LUM	93%	Mycolicibacterium smegmatis MC2 51	Structure of Mycobacterium smegmatis succinate dehydrogenase 2
  6C12	48%	Escherichia coli (strain K12)	SDHA-SDHE complex
  2WU5	48%	ESCHERICHIA COLI	Crystal structure of the E. coli succinate:quinone oxidoreductase (SQR) SdhD His71Met mutant
  2WU2	48%	ESCHERICHIA COLI	Crystal structure of the E. coli succinate:quinone oxidoreductase (SQR) SdhC His84Met mutant
  2WS3	48%	ESCHERICHIA COLI	Crystal structure of the E. coli succinate:quinone oxidoreductase (SQR) SdhD Tyr83Phe mutant
  2WP9	48%	ESCHERICHIA COLI	Crystal structure of the E. coli succinate:quinone oxidoreductase (SQR) SdhB His207Thr mutant
  2WDV	48%	ESCHERICHIA COLI	E. coli succinate:quinone oxidoreductase (SQR) with an empty quinone- binding pocket
  2WDR	48%	ESCHERICHIA COLI	E. coli succinate:quinone oxidoreductase (SQR) with pentachlorophenol bound
  2WDQ	48%	ESCHERICHIA COLI	E. coli succinate:quinone oxidoreductase (SQR) with carboxin bound
  2ACZ	48%	Escherichia coli	Complex II (Succinate Dehydrogenase) From E. Coli with Atpenin A5 inhibitor co-crystallized at the ubiquinone binding site

• Links to additional information on sdhA:
  • TBDB (updated)
  • Phyre2 structure prediction, model: final.casp.pdb (from Mao et al, 2013)
  • UniProt
  • AlphaFold model
  • Vulnerability = 1.32 (from Jeremy Rock's lab)
  • KEGG - nucleotide and amino acid sequences of gene
  • Mycobrowser
  • PATRIC
  • BioCyc
  • Systems Biology

Amino Acid Sequence

LICQHRYDVVIVGAGGAGMRAAVEAGPRVRTAVLTKLYPTRSHTGAAQGGMCAALANVEDDNWEWHTFDTVKGGDYLADQDAVEIMCKEAIDAVLDLEKM
GMPFNRTPEGRIDQRRFGGHTRDHGKAPVRRACYAADRTGHMILQTLYQNCVKHDVEFFNEFYALDLALTQTPSGPVATGVIAYELATGDIHVFHAKAVV
IATGGSGRMYKTTSNAHTLTGDGIGIVFRKGLPLEDMEFHQFHPTGLAGLGILISEAVRGEGGRLLNGEGERFMERYAPTIVDLAPRDIVARSMVLEVLE
GRGAGPLKDYVYIDVRHLGEEVLEAKLPDITEFARTYLGVDPVTELVPVYPTCHYLMGGIPTTVTGQVLRDNTSVVPGLYAAGECACVSVHGANRLGTNS
LLDINVFGRRAGIAAASYAQGHDFVDMPPNPEAMVVGWVSDILSEHGNERVADIRGALQQSMDNNAAVFRTEETLKQALTDIHALKERYSRITVHDKGKR
FNTDLLEAIELGFLLELAEVTVVGALNRKESRGGHAREDYPNRDDVNYMRHTMAYKEIGADKEGPELRSDVRLDFKPVVQTRYEPKERKY

Additional Information