TPI1 triose-phosphate isomerase TPI1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: TPI1
Official Full Name: triose-phosphate isomerase TPI1
Primary source: SGD:S000002457
Locus tag: YDR050C
See related: AllianceGenome:SGD:S000002457; FungiDB:YDR050C; VEuPathDB:YDR050C
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Enables triose-phosphate isomerase activity. Involved in glycolytic process. Located in mitochondrion. Used to study cancer and triosephosphate isomerase deficiency. Human ortholog(s) of this gene implicated in carbohydrate metabolic disorder and triosephosphate isomerase deficiency. Orthologous to human TPI1 (triosephosphate isomerase 1). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See TPI1 in Genome Data Viewer

Location:: chromosome: IV

Exon count:: 1

Sequence:: Chromosome: IV; NC_001136.10 (555726..556472, complement)

Chromosome IV - NC_001136.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001136.10

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Phenylpyrrole fungicides act on triosephosphate isomerase to induce methylglyoxal stress and alter hybrid histidine kinase activity.
Title: Phenylpyrrole fungicides act on triosephosphate isomerase to induce methylglyoxal stress and alter hybrid histidine kinase activity.
temperature-induced unfolding of yeast TIM shows three kinetic phases
Title: Complex kinetics and residual structure in the thermal unfolding of yeast triosephosphate isomerase.
Cysteine-to-serine mutation in triosephosphate isomerase is associated with altered structure and stability.
Title: Effects of a buried cysteine-to-serine mutation on yeast triosephosphate isomerase structure and stability.
Information on most of the active-site residues involved in chemistry, including some that were not reported in a previous solution NMR study, such as the side-chain carbons of His95 of yeast triosephosphate isomerase, was obtained.
Title: Triosephosphate isomerase: 15N and 13C chemical shift assignments and conformational change upon ligand binding by magic-angle spinning solid-state NMR spectroscopy.
These results indicate that renaturation of yTIM occurs through a uni-bimolecular mechanism in which refolding of the monomer most likely begins at the C-terminal half of its polypeptide chain.
Title: The conserved salt bridge linking two C-terminal beta/alpha units in homodimeric triosephosphate isomerase determines the folding rate of the monomer.
relative stabilities of different folding units are similar so that subtle alterations in their stability produce a total transformation of the folding pathway
Title: Hydrophobic repacking of the dimer interface of triosephosphate isomerase by in silico design and directed evolution.
Temperature-jump kinetic promote a mechanism consistent with osmolyte-induced shifts in the [BI]/[BC] ratio of enzyme conformers. Salt affects the binding constant through its effect on the activity coefficients of substrate, enzyme, and E-S complex.
Title: Effects of cell volume regulating osmolytes on glycerol 3-phosphate binding to triosephosphate isomerase.
unfolding and refolding of the Triose phosphate isomerase from baker's yeast (yTIM
Title: Pressure and denaturants in the unfolding of triosephosphate isomerase: the monomeric intermediates of the enzymes from Saccharomyces cerevisiae and Entamoeba histolytica.
The predominance of dihydroxyacetone phosphate (DHAP) on the enzyme supports a mechanism in which the initial proton abstraction in the reaction from DHAP to D-glyceraldehyde 3-phosphate is significantly slower than the subsequent chemical steps.
Title: Substrate product equilibrium on a reversible enzyme, triosephosphate isomerase.

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Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables isomerase activity	IEA Inferred from Electronic Annotation more info
enables triose-phosphate isomerase activity	IBA Inferred from Biological aspect of Ancestor more info
enables triose-phosphate isomerase activity	IDA Inferred from Direct Assay more info	PubMed
enables triose-phosphate isomerase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in gluconeogenesis	IBA Inferred from Biological aspect of Ancestor more info
involved_in gluconeogenesis	IEA Inferred from Electronic Annotation more info
involved_in glyceraldehyde-3-phosphate biosynthetic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in glycerol catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in glycolytic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in glycolytic process	IEA Inferred from Electronic Annotation more info
involved_in glycolytic process	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	HDA more info	PubMed
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrion	HDA more info	PubMed
located_in mitochondrion	IDA Inferred from Direct Assay more info	PubMed
located_in plasma membrane	HDA more info	PubMed

General protein information

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Preferred Names: triose-phosphate isomerase TPI1

NP_010335.1

EC 5.3.1.1

Triose phosphate isomerase, abundant glycolytic enzyme; mRNA half-life is regulated by iron availability; transcription is controlled by activators Reb1p, Gcr1p, and Rap1p through binding sites in the 5' non-coding region; inhibition of Tpi1p activity by PEP (phosphoenolpyruvate) stimulates redox metabolism in respiring cells; E104D mutation in human homolog TPI1 causes a rare autosomal disease; human TPI1 can complement yeast null mutant

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001136.10 Reference assembly

Range

555726..556472 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001180358.1 → NP_010335.1 TPA: triose-phosphate isomerase TPI1 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_010335.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VS37, P00942

UniProtKB/TrEMBL

A6ZY16, B3LGL8, B5VFV0, C7GTA0, C8Z4W9, G2WAF5, N1P6G4

Conserved Domains (1) summary

cd00311
Location:5 → 245

TIM; Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of dihydroxyacetone phosphate and D-glyceraldehyde-3-phosphate. The reaction is very efficient and requires neither cofactors nor metal ions. TIM, usually ...