Identification
Name:Triosephosphate isomerase
Synonyms:
  • TIM
  • Triose-phosphate isomerase
Gene Name:tpiA
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:D-glyceraldehyde 3-phosphate = glycerone phosphate
Cellular Location:Cytoplasm (Probable)
SMPDB Pathways:
KEGG Pathways:
  • Carbon fixation in photosynthetic organisms ec00710
  • Fructose and mannose metabolism ec00051
  • Glycolysis / Gluconeogenesis ec00010
  • Inositol phosphate metabolism ec00562
  • Metabolic pathways eco01100
  • Microbial metabolism in diverse environments ec01120
KEGG Reactions:
1.0Thumb1.0Thumb
1.0Thumb1.0Thumb
SMPDB Reactions:
1.0D-Glyceraldehyde 3-phosphate+1.0Thumb1.0Thumb
1.0D-Glyceraldehyde 3-phosphate + 1.0D-Glyceraldehyde 3-phosphate ↔ 1.0Dihydroxyacetone phosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb1.0Thumb
Complex Reactions:
1.0Thumb1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB01112D-Glyceraldehyde 3-phosphateMetaboCard
ECMDB01473Dihydroxyacetone phosphateMetaboCard
GO Classification:
Function
catalytic activity
intramolecular oxidoreductase activity
intramolecular oxidoreductase activity, interconverting aldoses and ketoses
isomerase activity
triose-phosphate isomerase activity
Process
metabolic process
Gene Properties
Blattner:b3919
Gene OrientationCounterclockwise
Centisome Percentage:88.56
Left Sequence End4108763
Right Sequence End4109530
Gene Sequence:
>768 bp
ATGTGCGAATTGCTCGGGATGAGCGCCAACGTCCCTACCGATATCTGCTTTAGTTTCACC
GGGCTTGTACAGCGTGGTGGTGGAACCGGGCCACATAAAGATGGCTGGGGCATTACCTTT
TACGAAGGTAAAGGCTGTCGCACATTTAAAGATCCACAACCCAGCTTTAATTCCCCCATC
GCCAAACTTGTCCAGGACTACCCGATAAAATCCTGTTCGGTGGTGGCTCATATTCGCCAG
GCTAATCGGGGCGAGGTGGCGCTGGAAAATACTCACCCATTTACCCGCGAGTTATGGGGG
CGTAACTGGACTTATGCCCATAACGGACAACTGACGGGCTACAAATCACTGGAAACCGGC
AACTTCCGCCCGGTAGGCGAAACCGACAGCGAAAAAGCCTTCTGCTGGCTCCTGCATAAA
TTAACGCAGCGTTACCCGCGCACACCGGGCAACATGGCGGCGGTATTTAAATATATCGCC
TCACTGGCGGATGAACTGCGGCAGAAGGGCGTTTTCAACATGCTGCTTTCGGACGGGCGC
TATGTAATGGCGTATTGCTCGACTAATTTACACTGGATCACCCGCCGCGCGCCGTTTGGC
GTGGCAACGTTGCTGGATCAGGATGTGGAAATCGACTTCAGCTCGCAGACCACACCGAAT
GATGTGGTCACGGTGATTGCAACACAGCCGCTGACGGGCAATGAAACCTGGCAAAAGATT
ATGCCAGGCGAATGGCGCTTATTTTGCCTCGGGGAGCGTGTAGTTTGA
Protein Properties
Pfam Domain Function:
Protein Residues:255
Protein Molecular Weight:26972
Protein Theoretical pI:6
PDB File:1TRE
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Triosephosphate isomerase
MRHPLVMGNWKLNGSRHMVHELVSNLRKELAGVAGCAVAIAPPEMYIDMAKREAEGSHIM
LGAQNVDLNLSGAFTGETSAAMLKDIGAQYIIIGHSERRTYHKESDELIAKKFAVLKEQG
LTPVLCIGETEAENEAGKTEEVCARQIDAVLKTQGAAAFEGAVIAYEPVWAIGTGKSATP
AQAQAVHKFIRDHIAKVDANIAEQVIIQYGGSVNASNAAELFAQPDIDGALVGGASLKAD
AFAVIVKAAEAAKQA
References
External Links:
ResourceLink
Uniprot ID:P0A858
Uniprot Name:TPIS_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4902959
PDB ID:1TRE
Ecogene ID:EG11015
Ecocyc:EG11015
ColiBase:b3919
Kegg Gene:b3919
EchoBASE ID:EB1008
CCDB:TPIS_ECOLI
BacMap:16131757
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Mainfroid, V., Goraj, K., Rentier-Delrue, F., Houbrechts, A., Loiseau, A., Gohimont, A. C., Noble, M. E., Borchert, T. V., Wierenga, R. K., Martial, J. A. (1993). "Replacing the (beta alpha)-unit 8 of E.coli TIM with its chicken homologue leads to a stable and active hybrid enzyme." Protein Eng 6:893-900. Pubmed: 8309937
  • Noble, M. E., Zeelen, J. P., Wierenga, R. K., Mainfroid, V., Goraj, K., Gohimont, A. C., Martial, J. A. (1993). "Structure of triosephosphate isomerase from Escherichia coli determined at 2.6 A resolution." Acta Crystallogr D Biol Crystallogr 49:403-417. Pubmed: 15299515
  • Pichersky, E., Gottlieb, L. D., Hess, J. F. (1984). "Nucleotide sequence of the triose phosphate isomerase gene of Escherichia coli." Mol Gen Genet 195:314-320. Pubmed: 6092857
  • Plunkett, G. 3rd, Burland, V., Daniels, D. L., Blattner, F. R. (1993). "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes." Nucleic Acids Res 21:3391-3398. Pubmed: 8346018
  • Wilkins, M. R., Gasteiger, E., Tonella, L., Ou, K., Tyler, M., Sanchez, J. C., Gooley, A. A., Walsh, B. J., Bairoch, A., Appel, R. D., Williams, K. L., Hochstrasser, D. F. (1998). "Protein identification with N and C-terminal sequence tags in proteome projects." J Mol Biol 278:599-608. Pubmed: 9600841