Triosephosphate isomerase

Details

Name
Triosephosphate isomerase
Synonyms
  • 5.3.1.1
  • TIM
  • tpi
  • Triose-phosphate isomerase
Gene Name
tpiA
Organism
Geobacillus stearothermophilus
Amino acid sequence
>lcl|BSEQ0011346|Triosephosphate isomerase
MRKPIIAGNWKMHKTLAEAVQFVEDVKGHVPPADEVISVVCAPFLFLDRLVQAADGTDLK
IGAQTMHFADQGAYTGEVSPVMLKDLGVTYVILGHSERRQMFAETDETVNKKVLAAFTRG
LIPIICCGESLEEREAGQTNAVVASQVEKALAGLTPEQVKQAVIAYEPIWAIGTGKSSTP
EDANSVCGHIRSVVSRLFGPEAAEAIRIQYGGSVKPDNIRDFLAQQQIDGPLVGGASLEP
ASFLQLVEAGRHE
Number of residues
253
Molecular Weight
27205.89
Theoretical pI
5.0
GO Classification
Functions
triose-phosphate isomerase activity
Processes
gluconeogenesis / glycolytic process / pentose-phosphate shunt
Components
cytoplasm
General Function
Triose-phosphate isomerase activity
Specific Function
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0003718|762 bp
ATGAGAAAACCGATCATTGCAGGCAACTGGAAAATGCATAAAACATTAGCGGAAGCTGTC
CAATTTGTCGAGGACGTAAAAGGGCACGTGCCGCCGGCCGACGAAGTCATTTCCGTCGTT
TGCGCGCCGTTTCTCTTTTTGGATCGGTTGGTGCAAGCGGCAGACGGCACGGATTTAAAA
ATCGGGGCGCAAACGATGCACTTTGCCGATCAAGGGGCGTACACAGGCGAAGTGAGCCCG
GTCATGCTGAAAGACCTCGGCGTCACGTACGTCATCCTCGGCCATTCGGAGCGCCGGCAA
ATGTTCGCCGAAACAGATGAGACCGTGAACAAAAAAGTGTTGGCCGCCTTCACCCGCGGG
CTTATACCGATTATTTGCTGCGGTGAATCGCTTGAGGAGCGGGAAGCGGGCCAGACGAAC
GCGGTTGTCGCCTCGCAAGTGGAAAAAGCGCTCGCCGGCTTGACGCCGGAACAAGTGAAG
CAAGCGGTCATCGCTTACGAGCCGATTTGGGCGATCGGGACGGGCAAATCATCAACACCG
GAAGACGCCAACAGCGTCTGCGGCCATATCCGTTCGGTTGTTTCGCGCCTGTTTGGCCCG
GAGGCGGCGGAAGCGATCCGCATTCAATACGGCGGCAGCGTCAAACCAGACAACATCCGC
GACTTCTTGGCGCAACAACAGATCGACGGGCCCTTAGTCGGCGGGGCGAGCCTCGAGCCG
GCTTCATTCTTGCAATTGGTGGAGGCGGGGCGTCATGAGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP00943
UniProtKB Entry NameTPIS_GEOSE
GenBank Protein ID49093
GenBank Gene IDX66129
General References
  1. Rentier-Delrue F, Mande SC, Moyens S, Terpstra P, Mainfroid V, Goraj K, Lion M, Hol WG, Martial JA: Cloning and overexpression of the triosephosphate isomerase genes from psychrophilic and thermophilic bacteria. Structural comparison of the predicted protein sequences. J Mol Biol. 1993 Jan 5;229(1):85-93. [Article]
  2. Rentier-Delrue F, Moyens S, Lion M, Martial JA: Sequence of the triosephosphate isomerase-encoding gene isolated from the thermophile Bacillus stearothermophilus. Gene. 1993 Nov 30;134(1):137-8. [Article]
  3. Artavanis-Tsakonas S, Harris JI: Primary structure of triosephosphate isomerase from Bacillus stearothermophilus. Eur J Biochem. 1980 Jul;108(2):599-611. [Article]
  4. Delboni LF, Mande SC, Rentier-Delrue F, Mainfroid V, Turley S, Vellieux FM, Martial JA, Hol WG: Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interactions. Protein Sci. 1995 Dec;4(12):2594-604. [Article]
  5. Alvarez M, Wouters J, Maes D, Mainfroid V, Rentier-Delrue F, Wyns L, Depiereux E, Martial JA: Lys13 plays a crucial role in the functional adaptation of the thermophilic triose-phosphate isomerase from Bacillus stearothermophilus to high temperatures. J Biol Chem. 1999 Jul 2;274(27):19181-7. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB027262-Phosphoglycolic AcidexperimentalunknownDetails