TB Genome Annotation Portal

Rv0975c (fadE13)

• Current annotations:
  • TBCAP: (community-based annotations - see table at bottom of page)
  • TBDB: acyl-CoA dehydrogenase
  • REFSEQ: acyl-CoA dehydrogenase FADE13
  • PATRIC: Isovaleryl-CoA dehydrogenase (EC 1.3.99.10)
  • TUBERCULIST: Probable acyl-CoA dehydrogenase FadE13
  • NCBI: Probable acyl-CoA dehydrogenase FadE13
  • updated information (H37Rv4):
    • gene name: fadE13
    • function:
    • reference:
• Type: Not Target
• Start: 1087348
• End: 1088496
• Operon:


• Trans-membrane region:
  
• Role: I.A.3 - Fatty acids
• GO terms:
  • GO:0055114 - oxidation-reduction process (Uniprot)
  • GO:0050660 - flavin adenine dinucleotide binding (Uniprot)
  • GO:0016627 - oxidoreductase activity, acting on the CH-CH group of donors (Uniprot)
  • GO:0016491 - oxidoreductase activity (Uniprot)
  • GO:0008152 - metabolic process (Uniprot)
  • GO:0003995 - acyl-CoA dehydrogenase activity (Uniprot)
• Reaction(s) (based on iSM810 metabolic model):
  • NAD[c] + COA[c] + FAD[c] + OCTACOSANOYL_COA[c] -> NADH[c] + ACCOA[c] + FADH2[c] + HEXACOSANOYL_COA[c]
  • NAD[c] + COA[c] + FAD[c] + HEXACOSANOYL_COA[c] -> NADH[c] + ACCOA[c] + FADH2[c] + TETRACOSANOYL_COA[c]
  • NAD[c] + COA[c] + FAD[c] + TETRACOSANOYL_COA[c] -> NADH[c] + ACCOA[c] + FADH2[c] + DOCOSANOYL_COA[c]
  • NAD[c] + COA[c] + FAD[c] + DOCOSANOYL_COA[c] -> NADH[c] + ACCOA[c] + FADH2[c] + EICOSANOYL_COA[c]
  • NAD[c] + COA[c] + FAD[c] + EICOSANOYL_COA[c] -> NADH[c] + ACCOA[c] + FADH2[c] + OCTADECANOYL_COA[c]
  • NAD[c] + COA[c] + FAD[c] + OCTADECANOYL_COA[c] -> NADH[c] + ACCOA[c] + FADH2[c] + HEXADECANOYL_COA[c]
  • NAD[c] + COA[c] + FAD[c] + HEXADECANOYL_COA[c] -> NADH[c] + ACCOA[c] + FADH2[c] + TETRADECANOYL_COA[c]
  • NAD[c] + COA[c] + FAD[c] + TETRADECANOYL_COA[c] -> NADH[c] + ACCOA[c] + FADH2[c] + DODECANOYL_COA[c]
  • NAD[c] + COA[c] + FAD[c] + DODECANOYL_COA[c] -> NADH[c] + ACCOA[c] + FADH2[c] + DECANOYL_COA[c]
  • NAD[c] + COA[c] + FAD[c] + DECANOYL_COA[c] -> NADH[c] + ACCOA[c] + FADH2[c] + OCTANOYL_COA[c]
  • NAD[c] + COA[c] + FAD[c] + OCTANOYL_COA[c] -> NADH[c] + ACCOA[c] + FADH2[c] + HEXANOYL_COA[c]
  • NAD[c] + COA[c] + FAD[c] + HEXANOYL_COA[c] -> NADH[c] + ACCOA[c] + FADH2[c] + BUTANOYL_COA[c]
  • NAD[c] + COA[c] + FAD[c] + BUTANOYL_COA[c] -> NADH[c] + 2 ACCOA[c] + FADH2[c]
  • NAD[c] + COA[c] + FAD[c] + 9_OCTADECENOYL_COA[c] -> NADH[c] + ACCOA[c] + FADH2[c] + 9_HEXADECENOYL_COA[c]
  • NAD[c] + COA[c] + FAD[c] + 9_HEXADECENOYL_COA[c] -> NADH[c] + ACCOA[c] + FADH2[c] + CIS_DELTA_5_TETRADECANOYL_COA[c]
  • NAD[c] + COA[c] + FAD[c] + CIS_DELTA_5_TETRADECANOYL_COA[c] -> NADH[c] + ACCOA[c] + FADH2[c] + CIS_DELTA_3_DODECANOYL_COA[c]
  • CIS_DELTA_3_DODECANOYL_COA[c] -> TRANS_DELTA_2_DODECANOYL_COA[c]
  • TRANS_DELTA_2_DODECANOYL_COA[c] -> TRANS_DELTA_2_HYDROXY_DODECANOYL_COA[c]
  • NAD[c] + TRANS_DELTA_2_HYDROXY_DODECANOYL_COA[c] -> NADH[c] + DODECANOYL_COA[c]
  • NAD[c] + COA[c] + FAD[c] + NONADECANOYL_COA[c] -> NADH[c] + ACCOA[c] + FADH2[c] + HEPTADECANOYL_COA[c]
  • NAD[c] + COA[c] + FAD[c] + HEPTADECANOYL_COA[c] -> NADH[c] + ACCOA[c] + FADH2[c] + PENTADECANOYL_COA[c]
  • NAD[c] + COA[c] + FAD[c] + PENTADECANOYL_COA[c] -> NADH[c] + ACCOA[c] + FADH2[c] + TRIDECANOYL_COA[c]
  • NAD[c] + COA[c] + FAD[c] + TRIDECANOYL_COA[c] -> NADH[c] + ACCOA[c] + FADH2[c] + UNDECANOYL_COA[c]
  • NAD[c] + COA[c] + FAD[c] + UNDECANOYL_COA[c] -> NADH[c] + ACCOA[c] + FADH2[c] + NOOYL_COA[c]
  • NAD[c] + COA[c] + FAD[c] + NOOYL_COA[c] -> NADH[c] + ACCOA[c] + FADH2[c] + HEPTANOYL_COA[c]
  • NAD[c] + COA[c] + FAD[c] + HEPTANOYL_COA[c] -> NADH[c] + ACCOA[c] + FADH2[c] + PENTANOYL_COA[c]
  • NAD[c] + COA[c] + FAD[c] + PENTANOYL_COA[c] -> NADH[c] + ACCOA[c] + PROPIONYLCOA[c] + FADH2[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
  3P4T	84%	Mycobacterium smegmatis	Crystal structure of a putative acyl-CoA dehydrogenase from Mycobacterium smegmatis
  3OIB	84%	Mycobacterium smegmatis	Crystal structure of a putative ACYL-COA Dehydrogenase from mycobacterium smegmatis, Iodide soak
  3R7K	62%	Mycobacterium abscessus	Crystal structure of a probable acyl CoA dehydrogenase from Mycobacterium abscessus ATCC 19977 / DSM 44196
  2PG0	38%	Geobacillus kaustophilus	Crystal structure of acyl-CoA dehydrogenase from Geobacillus kaustophilus
  5LNX	37%	Bacillus subtilis (strain 168)	Crystal structure of MmgC, an acyl-CoA dehydrogenase from bacillus subtilis.
  4IV6	36%	Mycobacterium smegmatis	X-ray crystal structure of an isovaleryl-CoA dehydrogenase from Mycobacterium smegmatis
  5OL2	36%	Clostridioides difficile	The electron transferring flavoprotein/butyryl-CoA dehydrogenase complex from Clostridium difficile
  1UKW	35%	Thermus thermophilus	Crystal structure of medium-chain acyl-CoA dehydrogenase from Thermus thermophilus HB8
  4U83	35%	Brucella abortus	Structure of Brucella Abortus Butyryl-CoA dehydrogenase

• Links to additional information on fadE13:
  • TBDB (updated)
  • Phyre2 structure prediction, model: final.casp.pdb (from Mao et al, 2013)
  • UniProt
  • AlphaFold model
  • Vulnerability = -1.182 (from Jeremy Rock's lab)
  • KEGG - nucleotide and amino acid sequences of gene
  • Mycobrowser
  • PATRIC
  • BioCyc
  • Systems Biology

Amino Acid Sequence

VNIWTTPERQQLRKTVRAFAEREILPHVDEWERIGELPRGLHRLAGAAGLLGAGFPEAVGGGGGDGADPVIICEEMHQAGAPGGVYASLFTCGIAVPHMV
ASGDERLIATYVRPTLAGEKIGALAITEPGGGSDVGHLRTSAVRDGDHYVINGAKTYITSGVRADYVVTAVRTGGPGAAGVSLLVVEKDTPGFEVTRKLD
KMGWRSSDTAELCYTDVAVPATNLVGAENSGFTQIARAFVSERIGLAAQAYSSAQRCLDLTAQWCRDRETFGRPLISRQSVQNTLAEMARRIDVARVYAH
HVVERQLAGETDLIAQVCFAKNTAVQAGEWVANQAVQLFGGMGYMAESEVERQYRDMRILGIGGGTTEILTALAAKTLGYQS

Additional Information