Triosephosphate isomerase
Details
- Name
- Triosephosphate isomerase
- Kind
- protein
- Synonyms
- 5.3.1.1
- TIM
- tpi
- Triose-phosphate isomerase
- Gene Name
- tpiA
- UniProtKB Entry
- P00943Swiss-Prot
- Organism
- Geobacillus stearothermophilus
- NCBI Taxonomy ID
- 1422
- 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
- Functionstriose-phosphate isomerase activityProcessesgluconeogenesis / glycolytic process / pentose-phosphate shuntComponentscytoplasm
- General Function
- Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
- Specific Function
- triose-phosphate isomerase activity
- Pfam Domain Function
- TIM (PF00121)
- Signal Regions
- Not Available
- 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
Resource Link UniProtKB ID P00943 UniProtKB Entry Name TPIS_GEOSE GenBank Protein ID 49093 GenBank Gene ID X66129 PDB ID(s) 1BTM, 2BTM - General References
- 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]
- 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]
- Artavanis-Tsakonas S, Harris JI: Primary structure of triosephosphate isomerase from Bacillus stearothermophilus. Eur J Biochem. 1980 Jul;108(2):599-611. [Article]
- 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]
- 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]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details 2-Phosphoglycolic Acid experimental unknown target Details