TB Genome Annotation Portal

Rv0855 (far)

• Current annotations:
  • TBCAP: (community-based annotations - see table at bottom of page)
  • TBDB: fatty-acid-CoA racemase far
  • REFSEQ: fatty-acid-CoA racemase
  • PATRIC: Alpha-methylacyl-CoA racemase (EC 5.1.99.4)
  • TUBERCULIST: Probable fatty-acid-CoA racemase Far
  • NCBI: Probable fatty-acid-CoA racemase Far
  • updated information (H37Rv4):
    • gene name: far
    • function:
    • reference:
• Type: Not Target
• Start: 951632
• End: 952711
• Operon:


• Trans-membrane region:
  
• Role: I.A.3 - Fatty acids
• GO terms:
  • GO:0003824 - catalytic activity (Uniprot)
• Reaction(s) (based on iSM810 metabolic model):
  • SMMALONYLCOA[c] <=> RMMALONYLCOA[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: 2g04
• Search for Homologs in PDB
• Top 10 Homologs in PDB (as of Nov 2020):
  

  PDB	aa ident	species	PDB title
  2G04	99%	Mycobacterium tuberculosis	Crystal structure of fatty acid-CoA racemase from Mycobacterium tuberculosis H37Rv
  2YIM	56%	MYCOBACTERIUM TUBERCULOSIS	The enolisation chemistry of a thioester-dependent racemase: the 1.4 A crystal structure of a complex with a planar reaction intermediate analogue
  2GD6	56%	Mycobacterium tuberculosis	The 1,1-proton transfer reaction mechanism by alpha-methylacyl-CoA racemase is catalyzed by an aspartate/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety
  2GD2	56%	Mycobacterium tuberculosis	The 1,1-proton transfer reaction mechanism by alpha-methylacyl-CoA racemase is catalyzed by an aspartate/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety
  2GD0	56%	Mycobacterium tuberculosis	The 1,1-proton transfer reaction mechanism by alpha-methylacyl-CoA racemase is catalyzed by an aspartate/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety
  2GCI	56%	Mycobacterium tuberculosis	The 1,1-proton transfer reaction mechanism by alpha-methylacyl-CoA racemase is catalyzed by an asparte/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety
  2GCE	56%	Mycobacterium tuberculosis	The 1,1-proton transfer reaction mechanism by alpha-methylacyl-CoA racemase is catalyzed by an aspartate/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety
  1X74	56%	Mycobacterium tuberculosis	Alpha-methylacyl-CoA racemase from Mycobacterium tuberculosis- mutational and structural characterization of the fold and active site

• Links to additional information on far:
  • TBDB (updated)
  • Phyre2 structure prediction, model: final.casp.pdb (from Mao et al, 2013)
  • UniProt
  • AlphaFold model
  • Vulnerability = 0.933 (from Jeremy Rock's lab)
  • KEGG - nucleotide and amino acid sequences of gene
  • Mycobrowser
  • PATRIC
  • BioCyc
  • Systems Biology

Amino Acid Sequence

VTTGGPLAGVKVIELGGIGPGPHAGMVLADLGADVVRVRRPGGLTMPSEDRDLLHRGKRIVDLDVKTQPQAMLELAAKADVLLDCFRPGTCERLGIGPDD
CASVNPRLIFARITGWGQDGPLASTAGHDINYLSQTGALAAFGYADRPPMPPLNLVADFGGGSMLVLLGIVVALYERERSGVGQVVDAAMVDGVSVLAQM
MWTMKGIGSLRDQRESFLLDGGAPFYRCYETSDGKYMAVGAIEPQFFAALLSGLGLSAADVPTQLDVAGYPQMYDIFAERFASRTRDEWTRVFAGTDACV
TPVLAWSEAANNDHLKARSTVITAHGVQQAAPAPRFSRTPAGPVRPPPAAATPIDEINW

Additional Information