TB Genome Annotation Portal

Rv3089 (fadD13)

• Current annotations:
  • TBCAP: (community-based annotations - see table at bottom of page)
  • TBDB: O-succinylbenzoate-CoA ligase
  • REFSEQ: chain-fatty-acid-CoA ligase
  • PATRIC: Long-chain-fatty-acid--CoA ligase (EC 6.2.1.3)
  • TUBERCULIST: Probable chain -fatty-acid-CoA ligase FadD13 (fatty-acyl-CoA synthetase)
  • NCBI: Probable chain-fatty-acid-CoA ligase FadD13 (fatty-acyl-CoA synthetase)
  • updated information (H37Rv4):
    • gene name: fadD13
    • function:
    • reference:
• Type: Not Target
• Start: 3455761
• End: 3457272
• Operon:


• Trans-membrane region:
  
• Role: I.A.3 - Fatty acids
• GO terms:
  • GO:0102391 - decanoate-CoA ligase activity (Uniprot)
  • GO:0044119 - growth of symbiont in host cell (Uniprot)
  • GO:0016874 - ligase activity (Uniprot)
  • GO:0016020 - membrane (Uniprot)
  • GO:0010447 - response to acidic pH (Uniprot)
  • GO:0008152 - metabolic process (Uniprot)
  • GO:0006633 - fatty acid biosynthetic process (Uniprot)
  • GO:0006631 - fatty acid metabolic process (Uniprot)
  • GO:0006629 - lipid metabolic process (Uniprot)
  • GO:0005886 - plasma membrane (Uniprot)
  • GO:0005829 - cytosol (Uniprot)
  • GO:0005618 - cell wall (Uniprot)
  • GO:0005524 - ATP binding (Uniprot)
  • GO:0005515 - protein binding (Uniprot)
  • GO:0004467 - long-chain fatty acid-CoA ligase activity (Uniprot)
  • GO:0004321 - fatty-acyl-CoA synthase activity (Uniprot)
  • GO:0003824 - catalytic activity (Uniprot)
  • GO:0001676 - long-chain fatty acid metabolic process (Uniprot)
  • GO:0000166 - nucleotide binding (Uniprot)
• Reaction(s) (based on iSM810 metabolic model):
• 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: 3r44, 3t5c, 3t5b
• Search for Homologs in PDB
• Top 10 Homologs in PDB (as of Nov 2020):
  

  PDB	aa ident	species	PDB title
  5ZRN	100%	Mycobacterium tuberculosis CDC1551	Inhibitor bound crystal structure of N-terminal domain of FACL13 from Mycobacterium tuberculosis
  3T5C	100%	Mycobacterium tuberculosis	Crystal structure of N-terminal domain of FACL13 from Mycobacterium tuberculosis in different space group C2
  3T5B	100%	Mycobacterium tuberculosis	Crystal structure of N-terminal domain of FACL13 from Mycobacterium tuberculosis
  3R44	100%	Mycobacterium tuberculosis	Mycobacterium tuberculosis fatty acyl CoA synthetase
  6EQO	36%	Erythrobacter sp. NAP1	Tri-functional propionyl-CoA synthase of Erythrobacter sp. NAP1 with bound NADP+ and phosphomethylphosphonic acid adenylate ester

• Links to additional information on fadD13:
  • TBDB (updated)
  • Phyre2 structure prediction, model: final.casp.pdb (from Mao et al, 2013)
  • UniProt
  • AlphaFold model
  • Vulnerability = 1.293 (from Jeremy Rock's lab)
  • KEGG - nucleotide and amino acid sequences of gene
  • Mycobrowser
  • PATRIC
  • BioCyc
  • Systems Biology

Amino Acid Sequence

MKNIGWMLRQRATVSPRLQAYVEPSTDVRMTYAQMNALANRCADVLTALGIAKGDRVALLMPNSVEFCCLFYGAAKLGAVAVPINTRLAAPEVSFILSDS
GSKVVIYGAPSAPVIDAIRAQADPPGTVTDWIGADSLAERLRSAAADEPAVECGGDDNLFIMYTSGTTGHPKGVVHTHESVHSAASSWASTIDVRYRDRL
LLPLPMFHVAALTTVIFSAMRGVTLISMPQFDATKVWSLIVEERVCIGGAVPAILNFMRQVPEFAELDAPDFRYFITGGAPMPEALIKIYAAKNIEVVQG
YALTESCGGGTLLLSEDALRKAGSAGRATMFTDVAVRGDDGVIREHGEGEVVIKSDILLKEYWNRPEATRDAFDNGWFRTGDIGEIDDEGYLYIKDRLKD
MIISGGENVYPAEIESVIIGVPGVSEVAVIGLPDEKWGEIAAAIVVADQNEVSEQQIVEYCGTRLARYKLPKKVIFAEAIPRNPTGKILKTVLREQYSAT
VPK

Additional Information