TB Genome Annotation Portal

Rv2215 (dlaT)

• Current annotations:
  • TBCAP: (community-based annotations - see table at bottom of page)
  • TBDB: 2-oxoglutarate dehydrogenase E2 component dihydrolipoamide succinyltransferase
  • REFSEQ: dihydrolipoamide acetyltransferase
  • PATRIC: Dihydrolipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex (EC 2.3.1.168)
  • TUBERCULIST: DlaT dihydrolipoamide acyltransferase E2 component of pyruvate dehydrogenase
  • NCBI: DlaT, dihydrolipoamide acyltransferase, E2 component of pyruvate dehydrogenase
  • updated information (H37Rv4):
    • gene name: dlaT
    • function:
    • reference:
• Type: Not Target
• Start: 2481965
• End: 2483626
• Operon:


• Trans-membrane region:
  
• Role: I.B.3 - TCA cycle
• GO terms:
  • GO:0098869 - cellular oxidant detoxification (Uniprot)
  • GO:0055114 - oxidation-reduction process (Uniprot)
  • GO:0045454 - cell redox homeostasis (Uniprot)
  • GO:0045254 - pyruvate dehydrogenase complex (Uniprot)
  • GO:0040007 - growth (Uniprot)
  • GO:0031405 - lipoic acid binding (Uniprot)
  • GO:0016746 - transferase activity, transferring acyl groups (Uniprot)
  • GO:0016740 - transferase activity (Uniprot)
  • GO:0016209 - antioxidant activity (Uniprot)
  • GO:0015036 - disulfide oxidoreductase activity (Uniprot)
  • GO:0009405 - pathogenesis (Uniprot)
  • GO:0008152 - metabolic process (Uniprot)
  • GO:0006096 - glycolytic process (Uniprot)
  • GO:0005886 - plasma membrane (Uniprot)
  • GO:0005829 - cytosol (Uniprot)
  • GO:0005618 - cell wall (Uniprot)
  • GO:0005515 - protein binding (Uniprot)
  • GO:0004742 - dihydrolipoyllysine-residue acetyltransferase activity (Uniprot)
  • GO:0004148 - dihydrolipoyl dehydrogenase activity (Uniprot)
• Reaction(s) (based on iSM810 metabolic model):
  • ADLIPO[c] + COA[c] <=> DLIPO[c] + ACCOA[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
  2L5T	52%	Thermoplasma acidophilum	Solution NMR structure of E2 lipoyl domain from Thermoplasma acidophilum
  1PMR	49%	Escherichia coli	LIPOYL DOMAIN FROM THE DIHYDROLIPOYL SUCCINYLTRANSFERASE COMPONENT OF THE 2-OXOGLUTARATE DEHYDROGENASE MULTIENZYME COMPLEX OF ESCHERICHIA COLI, NMR, 25 STRUCTURES
  6L1Q	42%	Acidithiobacillus ferrooxidans ATCC 23270	Crystal structure of AfCbbQ2, a MoxR AAA+-ATPase and CbbQO-type Rubisco activase from Acidithiobacillus ferrooxidans
  1LAC	42%	Geobacillus stearothermophilus	THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX
  1LAB	42%	Geobacillus stearothermophilus	THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX
  1GHK	41%	Azotobacter vinelandii	SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE 2-OXOGLUTARATE DEHYDROGENASE COMPLEX FROM AZOTOBACTER VINELAND II, NMR, 25 STRUCTURES
  1GHJ	41%	Azotobacter vinelandii	SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE 2-OXOGLUTARATE DEHYDROGENASE COMPLEX FROM AZOTOBACTER VINELAND II, NMR, MINIMIZED AVERAGE STRUCTURE
  6PBR	41%	Escherichia coli	Catalytic domain of E.coli dihydrolipoamide succinyltransferase in I4 space group
  1SCZ	41%	Escherichia coli	Improved structural model for the catalytic domain of E.coli dihydrolipoamide succinyltransferase
  1E2O	41%	Escherichia coli	CATALYTIC DOMAIN FROM DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE

• Links to additional information on dlaT:
  • TBDB (updated)
  • Phyre2 structure prediction, model: final.casp.pdb (from Mao et al, 2013)
  • UniProt
  • AlphaFold model
  • Vulnerability = -4.484 (from Jeremy Rock's lab)
  • KEGG - nucleotide and amino acid sequences of gene
  • Mycobrowser
  • PATRIC
  • BioCyc
  • Systems Biology

Amino Acid Sequence

MAFSVQMPALGESVTEGTVTRWLKQEGDTVELDEPLVEVSTDKVDTEIPSPAAGVLTKIIAQEDDTVEVGGELAVIGDAKDAGEAAAPAPEKVPAAQPES
KPAPEPPPVQPTSGAPAGGDAKPVLMPELGESVTEGTVIRWLKKIGDSVQVDEPLVEVSTDKVDTEIPSPVAGVLVSISADEDATVPVGGELARIGVAAD
IGAAPAPKPAPKPVPEPAPTPKAEPAPSPPAAQPAGAAEGAPYVTPLVRKLASENNIDLAGVTGTGVGGRIRKQDVLAAAEQKKRAKAPAPAAQAAAAPA
PKAPPAPAPALAHLRGTTQKASRIRQITANKTRESLQATAQLTQTHEVDMTKIVGLRARAKAAFAEREGVNLTFLPFFAKAVIDALKIHPNINASYNEDT
KEITYYDAEHLGFAVDTEQGLLSPVIHDAGDLSLAGLARAIADIAARARSGNLKPDELSGGTFTITNIGSQGALFDTPILVPPQAAMLGTGAIVKRPRVV
VDASGNESIGVRSVCYLPLTYDHRLIDGADAGRFLTTIKHRLEEGAFEADLGL

Additional Information