TB Genome Annotation Portal

Rv0126 (treS)

• Current annotations:
  • TBCAP: (community-based annotations - see table at bottom of page)
  • TBDB: trehalose synthase
  • REFSEQ: trehalose synthase TRES
  • PATRIC: Trehalose synthase (EC 5.4.99.16)
  • TUBERCULIST: Trehalose synthase TreS
  • NCBI: Trehalose synthase TreS
  • updated information (H37Rv4):
    • gene name: treS
    • function:
    • reference:
• Coordinates in H37Rv: 152324 - 154129
• Gene length: 1806 bp (with stop codon), 601 aa (without stop codon)
• Operon:


• Trans-membrane region:
  
• Role: II.A.8 - Polysaccharides (cytoplasmic)
• GO terms:
  • GO:0103025 - alpha-amylase activity (releasing maltohexaose) (Uniprot)
  • GO:0047471 - maltose alpha-D-glucosyltransferase activity (Uniprot)
  • GO:0046872 - metal ion binding (Uniprot)
  • GO:0045227 - capsule polysaccharide biosynthetic process (Uniprot)
  • GO:0016853 - isomerase activity (Uniprot)
  • GO:0016798 - hydrolase activity, acting on glycosyl bonds (Uniprot)
  • GO:0016787 - hydrolase activity (Uniprot)
  • GO:0016161 - beta-amylase activity (Uniprot)
  • GO:0008152 - metabolic process (Uniprot)
  • GO:0005992 - trehalose biosynthetic process (Uniprot)
  • GO:0005991 - trehalose metabolic process (Uniprot)
  • GO:0005978 - glycogen biosynthetic process (Uniprot)
  • GO:0005977 - glycogen metabolic process (Uniprot)
  • GO:0005975 - carbohydrate metabolic process (Uniprot)
  • GO:0005886 - plasma membrane (Uniprot)
  • GO:0005829 - cytosol (Uniprot)
  • GO:0005509 - calcium ion binding (Uniprot)
  • GO:0004556 - alpha-amylase activity (Uniprot)
  • GO:0003824 - catalytic activity (Uniprot)
  • GO:0000272 - polysaccharide catabolic process (Uniprot)
  • GO:0000023 - maltose metabolic process (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:
• Search for Latest Homologs in PDB
• Top 10 Homologs in PDB (as of Apr 2026):
  

  PDB	aa ident	species	PDB title
  8UZH	100%	Saccharomyces cerevisiae	SUMO fused Trehalose Synthase (TreS) of Mycobacterium tuberculosis
  4LXF	100%	Mycobacterium tuberculosis	Crystal structure of M. tuberculosis TreS
  8UQV	99%	Mycobacterium tuberculosis	Trehalose Synthase (TreS) of Mycobacterium tuberculosis in complex with 6-TreAz compound
  5JY7	85%	Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)	Complex of Mycobacterium smegmatis trehalose synthase with maltokinase
  3ZOA	85%	MYCOBACTERIUM SMEGMATIS	The structure of Trehalose Synthase (TreS) of Mycobacterium smegmatis in complex with acarbose
  3ZO9	85%	MYCOBACTERIUM SMEGMATIS	The structure of Trehalose Synthase (TreS) of Mycobacterium smegmatis
  5H2T	77%	Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / NBRC 15933 / NCIMB 10081 / Henssen B9)	Structure of trehalose synthase
  5X7U	63%	Thermobaculum terrenum	Trehalose synthase from Thermobaculum terrenum
  8Z2T	55%	Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539	Crystal structure of trehalose synthase from Deinococcus radiodurans complexed with validoxylamine A (VAA)
  4TVU	55%	Deinococcus radiodurans	Crystal structure of trehalose synthase from Deinococcus radiodurans reveals a closed conformation for catalysis of the intramolecular isomerization

• Links to additional information on treS:
  • TBDB (updated)
  • Phyre2 structure prediction, model: final.casp.pdb (from Mao et al, 2013)
  • UniProt
  • AlphaFold model
  • Vulnerability = -1.651 (from Jeremy Rock's lab)
  • KEGG - nucleotide and amino acid sequences of gene
  • Mycobrowser
  • PATRIC
  • BioCyc
  • Systems Biology

Amino Acid Sequence

MNEAEHSVEHPPVQGSHVEGGVVEHPDAKDFGSAAALPADPTWFKHAVFYEVLVRAFFDASADGSGDLRGLIDRLDYLQWLGIDCIWLPPFYDSPLRDGG
YDIRDFYKVLPEFGTVDDFVALVDAAHRRGIRIITDLVMNHTSESHPWFQESRRDPDGPYGDYYVWSDTSERYTDARIIFVDTEESNWSFDPVRRQFYWH
RFFSHQPDLNYDNPAVQEAMIDVIRFWLGLGIDGFRLDAVPYLFEREGTNCENLPETHAFLKRVRKVVDDEFPGRVLLAEANQWPGDVVEYFGDPNTGGD
ECHMAFHFPLMPRIFMAVRRESRFPISEIIAQTPPIPDMAQWGIFLRNHDELTLEMVTDEERDYMYAEYAKDPRMKANVGIRRRLAPLLDNDRNQIELFT
ALLLSLPGSPVLYYGDEIGMGDVIWLGDRDGVRIPMQWTPDRNAGFSTANPGRLYLPPSQDPVYGYQAVNVEAQRDTSTSLLNFTRTMLAVRRRHPAFAV
GAFQELGGSNPSVLAYVRQVAGDDGDTVLCVNNLSRFPQPIELDLQQWTNYTPVELTGHVEFPRIGQVPYLLTLPGHGFYWFQLTTHEVGAPPTCGGERR
L

Additional Information

Analysis of Positive Selection in Clinical Isolates *new*

• data from Culviner et al (2025) (55,259 Mtb clinical isolates)
  • overall pN/pS for Rv0126: 0.458947128
  • lineage-specific pN/pS in L1: 0.477973637
  • lineage-specific pN/pS in L2: 0.413935071
  • lineage-specific pN/pS in L3: 0.420461075
  • lineage-specific pN/pS in L4: 0.477175151

• Analysis of dN/dS (omega) in a global collection of 10k Mtb clinical isolates using GenomegaMap (Window model)
• clinical isolates collection: global set of 10,626 Mtb genomes
• In the omega plots, the black line shows the mean estimate of omega (dN/dS) at each codon, and the blue lines are the bounds for the 95% credible interval (95%CI, from MCMC sampling).
• A gene is under significant positive selection if the lower-bound of the 95%CI of omega (lower blue line) exceeds 1.0 at any codon.

	global set of 10,626 Mtb clinical isolates
under significant positive selection?	NO
omega peak height (95%CI lower bound)	1.23 (0.53)
codons under selection
omega plots
genetic variants*	link