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Protein

Triosephosphate isomerase

Gene

TPI1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-glyceraldehyde 3-phosphate = glycerone phosphate.

Pathwayi: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

Pathwayi: glycolysis

This protein is involved in step 1 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate from glycerone phosphate.
Proteins known to be involved in this subpathway in this organism are:
  1. Triosephosphate isomerase (TPI1)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate from glycerone phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101Substrate1 Publication
Binding sitei12 – 121Substrate1 Publication
Active sitei95 – 951Electrophile
Active sitei165 – 1651Proton acceptor

GO - Molecular functioni

  • triose-phosphate isomerase activity Source: SGD

GO - Biological processi

  • gluconeogenesis Source: UniProtKB-UniPathway
  • glycolytic process Source: SGD
  • pentose-phosphate shunt Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Gluconeogenesis, Glycolysis, Pentose shunt

Enzyme and pathway databases

BioCyciYEAST:YDR050C-MONOMER.
BRENDAi5.3.1.1. 984.
ReactomeiR-SCE-70171. Glycolysis.
R-SCE-70263. Gluconeogenesis.
SABIO-RKP00942.
UniPathwayiUPA00109; UER00189.
UPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Triosephosphate isomerase (EC:5.3.1.1)
Short name:
TIM
Alternative name(s):
Triose-phosphate isomerase
Gene namesi
Name:TPI1
Ordered Locus Names:YDR050C
ORF Names:YD9609.05C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR050C.
SGDiS000002457. TPI1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 248247Triosephosphate isomerasePRO_0000090169Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei4 – 41PhosphothreonineCombined sources
Modified residuei71 – 711PhosphoserineCombined sources
Modified residuei215 – 2151PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP00942.
PeptideAtlasiP00942.
TopDownProteomicsiP00942.

2D gel databases

COMPLUYEAST-2DPAGEP00942.
SWISS-2DPAGEP00942.

PTM databases

iPTMnetiP00942.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi32104. 51 interactions.
DIPiDIP-6671N.
IntActiP00942. 10 interactions.
MINTiMINT-614733.

Structurei

Secondary structure

1
248
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106Combined sources
Helixi17 – 2913Combined sources
Beta strandi36 – 416Combined sources
Helixi44 – 463Combined sources
Helixi47 – 537Combined sources
Beta strandi59 – 646Combined sources
Beta strandi68 – 736Combined sources
Helixi80 – 856Combined sources
Beta strandi90 – 945Combined sources
Helixi96 – 1005Combined sources
Helixi106 – 11813Combined sources
Beta strandi122 – 1276Combined sources
Helixi131 – 1355Combined sources
Helixi139 – 15315Combined sources
Beta strandi160 – 1645Combined sources
Helixi167 – 1693Combined sources
Turni170 – 1723Combined sources
Helixi178 – 19619Combined sources
Helixi198 – 2036Combined sources
Beta strandi206 – 2116Combined sources
Turni214 – 2163Combined sources
Helixi217 – 2204Combined sources
Beta strandi228 – 2325Combined sources
Helixi233 – 2364Combined sources
Helixi239 – 2446Combined sources
Turni245 – 2473Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I45X-ray1.80A/B2-248[»]
1NEYX-ray1.20A/B2-248[»]
1NF0X-ray1.60A/B2-248[»]
1YPIX-ray1.90A/B2-248[»]
2YPIX-ray2.50A/B2-248[»]
3YPIX-ray2.80A/B2-248[»]
4FF7X-ray1.86A/B1-248[»]
7TIMX-ray1.90A/B2-248[»]
DisProtiDP00430.
ProteinModelPortaliP00942.
SMRiP00942. Positions 2-248.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00942.

Family & Domainsi

Sequence similaritiesi

Belongs to the triosephosphate isomerase family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000013354.
HOGENOMiHOG000226413.
InParanoidiP00942.
KOiK01803.
OMAiIEKNGTM.
OrthoDBiEOG79W9GP.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00147_B. TIM_B.
InterProiIPR013785. Aldolase_TIM.
IPR022896. TrioseP_Isoase_bac/euk.
IPR000652. Triosephosphate_isomerase.
IPR020861. Triosephosphate_isomerase_AS.
[Graphical view]
PANTHERiPTHR21139. PTHR21139. 1 hit.
PfamiPF00121. TIM. 1 hit.
[Graphical view]
SUPFAMiSSF51351. SSF51351. 1 hit.
TIGRFAMsiTIGR00419. tim. 1 hit.
PROSITEiPS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00942-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARTFFVGGN FKLNGSKQSI KEIVERLNTA SIPENVEVVI CPPATYLDYS
60 70 80 90 100
VSLVKKPQVT VGAQNAYLKA SGAFTGENSV DQIKDVGAKW VILGHSERRS
110 120 130 140 150
YFHEDDKFIA DKTKFALGQG VGVILCIGET LEEKKAGKTL DVVERQLNAV
160 170 180 190 200
LEEVKDWTNV VVAYEPVWAI GTGLAATPED AQDIHASIRK FLASKLGDKA
210 220 230 240
ASELRILYGG SANGSNAVTF KDKADVDGFL VGGASLKPEF VDIINSRN
Length:248
Mass (Da):26,795
Last modified:January 23, 2007 - v2
Checksum:i8429251C4DF51F86
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01366 Genomic DNA. Translation: AAA88757.1.
Z49209 Genomic DNA. Translation: CAA89080.1.
AY557654 Genomic DNA. Translation: AAS55980.1.
BK006938 Genomic DNA. Translation: DAA11897.1.
PIRiA01168. ISBYT.
RefSeqiNP_010335.1. NM_001180358.1.

Genome annotation databases

EnsemblFungiiYDR050C; YDR050C; YDR050C.
GeneIDi851620.
KEGGisce:YDR050C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01366 Genomic DNA. Translation: AAA88757.1.
Z49209 Genomic DNA. Translation: CAA89080.1.
AY557654 Genomic DNA. Translation: AAS55980.1.
BK006938 Genomic DNA. Translation: DAA11897.1.
PIRiA01168. ISBYT.
RefSeqiNP_010335.1. NM_001180358.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I45X-ray1.80A/B2-248[»]
1NEYX-ray1.20A/B2-248[»]
1NF0X-ray1.60A/B2-248[»]
1YPIX-ray1.90A/B2-248[»]
2YPIX-ray2.50A/B2-248[»]
3YPIX-ray2.80A/B2-248[»]
4FF7X-ray1.86A/B1-248[»]
7TIMX-ray1.90A/B2-248[»]
DisProtiDP00430.
ProteinModelPortaliP00942.
SMRiP00942. Positions 2-248.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32104. 51 interactions.
DIPiDIP-6671N.
IntActiP00942. 10 interactions.
MINTiMINT-614733.

PTM databases

iPTMnetiP00942.

2D gel databases

COMPLUYEAST-2DPAGEP00942.
SWISS-2DPAGEP00942.

Proteomic databases

MaxQBiP00942.
PeptideAtlasiP00942.
TopDownProteomicsiP00942.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR050C; YDR050C; YDR050C.
GeneIDi851620.
KEGGisce:YDR050C.

Organism-specific databases

EuPathDBiFungiDB:YDR050C.
SGDiS000002457. TPI1.

Phylogenomic databases

GeneTreeiENSGT00390000013354.
HOGENOMiHOG000226413.
InParanoidiP00942.
KOiK01803.
OMAiIEKNGTM.
OrthoDBiEOG79W9GP.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00189.
UPA00138.
BioCyciYEAST:YDR050C-MONOMER.
BRENDAi5.3.1.1. 984.
ReactomeiR-SCE-70171. Glycolysis.
R-SCE-70263. Gluconeogenesis.
SABIO-RKP00942.

Miscellaneous databases

EvolutionaryTraceiP00942.
PROiP00942.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00147_B. TIM_B.
InterProiIPR013785. Aldolase_TIM.
IPR022896. TrioseP_Isoase_bac/euk.
IPR000652. Triosephosphate_isomerase.
IPR020861. Triosephosphate_isomerase_AS.
[Graphical view]
PANTHERiPTHR21139. PTHR21139. 1 hit.
PfamiPF00121. TIM. 1 hit.
[Graphical view]
SUPFAMiSSF51351. SSF51351. 1 hit.
TIGRFAMsiTIGR00419. tim. 1 hit.
PROSITEiPS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the triose phosphate isomerase gene of Saccharomyces cerevisiae."
    Alber T., Kawasaki G.
    J. Mol. Appl. Genet. 1:419-434(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Crystallization of yeast triose phosphate isomerase from polyethylene glycol."
    Alber T., Hartman F.C., Johnson R.M., Petsko G.A., Tsernoglou D.
    J. Biol. Chem. 256:1356-1361(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-15.
  6. Cited for: PROTEIN SEQUENCE OF 56-84 AND 90-101.
    Strain: ATCC 204508 / S288c.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  9. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71 AND SER-215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4; SER-71 AND SER-215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Structure of yeast triosephosphate isomerase at 1.9-A resolution."
    Lolis E., Alber T.C., Davenport R.C., Rose D., Hartman F.C., Petsko G.A.
    Biochemistry 29:6609-6618(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  14. "Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis."
    Lolis E., Petsko G.A.
    Biochemistry 29:6619-6625(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH 2-P-GLYCOLATE.
  15. "Comparison of the refined crystal structures of liganded and unliganded chicken, yeast and trypanosomal triosephosphate isomerase."
    Wierenga R.K., Noble M.E.M., Davenport R.C.
    J. Mol. Biol. 224:1115-1126(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPARISON OF X-RAY STRUCTURES.
  16. "Crystallography and site-directed mutagenesis of yeast triosephosphate isomerase: what can we learn about catalysis from a 'simple' enzyme?"
    Alber T.C., Davenport R.C., Giammona D.A., Lolis E., Petsko G.A., Ringe D.
    Cold Spring Harb. Symp. Quant. Biol. 52:603-613(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  17. "Optimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution."
    Jogl G., Rozovsky S., McDermott A.E., Tong L.
    Proc. Natl. Acad. Sci. U.S.A. 100:50-55(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, HOMODIMERIZATION.

Entry informationi

Entry nameiTPIS_YEAST
AccessioniPrimary (citable) accession number: P00942
Secondary accession number(s): D6VS37
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 174 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 207000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.