TB Genome Annotation Portal

Rv1689 (tyrS)

• Current annotations:
  • TBCAP: (community-based annotations - see table at bottom of page)
  • TBDB: tyrosyl-tRNA synthetase
  • REFSEQ: tyrosyl-tRNA synthetase
  • PATRIC: Tyrosyl-tRNA synthetase (EC 6.1.1.1)
  • TUBERCULIST: Probable tyrosyl-tRNA synthase TyrS (TYRRS)
  • NCBI: Probable tyrosyl-tRNA synthase TyrS (TYRRS)
  • updated information (H37Rv4):
    • gene name: tyrS
    • function:
    • reference:
• Type: Not Target
• Start: 1913602
• End: 1914876
• Operon:


• Trans-membrane region:
  
• Role: II.A.3 - Aminoacyl tRNA synthases and their modification
• GO terms:
  • GO:0043039 - tRNA aminoacylation (Uniprot)
  • GO:0040007 - growth (Uniprot)
  • GO:0016874 - ligase activity (Uniprot)
  • GO:0006437 - tyrosyl-tRNA aminoacylation (Uniprot)
  • GO:0006418 - tRNA aminoacylation for protein translation (Uniprot)
  • GO:0006412 - translation (Uniprot)
  • GO:0005886 - plasma membrane (Uniprot)
  • GO:0005829 - cytosol (Uniprot)
  • GO:0005737 - cytoplasm (Uniprot)
  • GO:0005618 - cell wall (Uniprot)
  • GO:0005524 - ATP binding (Uniprot)
  • GO:0004831 - tyrosine-tRNA ligase activity (Uniprot)
  • GO:0004812 - aminoacyl-tRNA ligase activity (Uniprot)
  • GO:0003723 - RNA binding (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: 2jan
• Search for Homologs in PDB
• Top 10 Homologs in PDB (as of Nov 2020):
  

  PDB	aa ident	species	PDB title
  2JAN	100%	MYCOBACTERIUM TUBERCULOSIS	TYROSYL-TRNA SYNTHETASE FROM MYCOBACTERIUM TUBERCULOSIS IN UNLIGANDED STATE
  1TYC	56%	Geobacillus stearothermophilus	STRUCTURAL ANALYSIS OF A SERIES OF MUTANTS OF TYROSYL-TRNA SYNTHETASE: ENHANCEMENT OF CATALYSIS BY HYDROPHOBIC INTERACTIONS
  4TS1	55%	Geobacillus stearothermophilus	CRYSTAL STRUCTURE OF A DELETION MUTANT OF A TYROSYL-T/RNA SYNTHETASE COMPLEXED WITH TYROSINE
  1TYD	55%	Geobacillus stearothermophilus	STRUCTURE OF TYROSYL-TRNA SYNTHETASE REFINED AT 2.3 ANGSTROMS RESOLUTION. INTERACTION OF THE ENZYME WITH THE TYROSYL ADENYLATE INTERMEDIATE
  1TYB	55%	Geobacillus stearothermophilus	STRUCTURAL ANALYSIS OF A SERIES OF MUTANTS OF TYROSYL-TRNA SYNTHETASE: ENHANCEMENT OF CATALYSIS BY HYDROPHOBIC INTERACTIONS
  1TYA	55%	Geobacillus stearothermophilus	STRUCTURAL ANALYSIS OF A SERIES OF MUTANTS OF TYROSYL-TRNA SYNTHETASE: ENHANCEMENT OF CATALYSIS BY HYDROPHOBIC INTERACTIONS
  1VBM	53%	Escherichia coli	Crystal structure of the Escherichia coli tyrosyl-tRNA synthetase complexed with Tyr-AMS
  1X8X	53%	Escherichia coli	Tyrosyl t-RNA Synthetase from E.coli Complexed with Tyrosine
  1VBN	52%	Escherichia coli	Escherichia coli tyrosyl-tRNA synthetase mutant complexed with Tyr-AMS
  2YXN	52%	Escherichia coli	Structual basis of azido-tyrosine recognition by engineered bacterial Tyrosyl-tRNA synthetase

• Links to additional information on tyrS:
  • TBDB (updated)
  • Phyre2 structure prediction, model: final.casp.pdb (from Mao et al, 2013)
  • UniProt
  • AlphaFold model
  • Vulnerability = -9.774 (from Jeremy Rock's lab)
  • KEGG - nucleotide and amino acid sequences of gene
  • Mycobrowser
  • PATRIC
  • BioCyc
  • Systems Biology

Amino Acid Sequence

MSGMILDELSWRGLIAQSTDLDTLAAEAQRGPMTVYAGFDPTAPSLHAGHLVPLLTLRRFQRAGHRPIVLAGGATGMIGDPRDVGERSLNEADTVAEWTE
RIRGQLERFVDFDDSPMGAIVENNLEWTGSLSAIEFLRDIGKHFSVNVMLARDTIRRRLAGEGISYTEFSYLLLQANDYVELHRRHGCTLQIGGADQWGN
IIAGVRLVRQKLGATVHALTVPLVTAADGTKFGKSTGGGSLWLDPQMTSPYAWYQYFVNTADADVIRYLRWFTFLSADELAELEQATAQRPQQRAAQRRL
ASELTVLVHGEAATAAVEHASRALFGRGELARLDEATLAAALRETTVAELKPGSPDGIVDLLVASGLSASKGAARRTIHEGGVSVNNIRVDNEEWVPQSS
DFLHGRWLVLRRGKRSIAGVERIG

Additional Information