P00942 (TPIS_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Triosephosphate isomerase
Short name=TIM
EC=5.3.1.1

Alternative name(s):
Triose-phosphate isomerase

Gene names

Name:	TPI1
Ordered Locus Names:	YDR050C
ORF Names:	YD9609.05C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	248 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	D-glyceraldehyde 3-phosphate = glycerone phosphate.
Pathway	Carbohydrate biosynthesis; gluconeogenesis. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1.
Subunit structure	Homodimer. Ref.14
Miscellaneous	Present with 207000 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the triosephosphate isomerase family.

Ontologies

Keywords
Biological process	Gluconeogenesis Glycolysis Pentose shunt
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	gluconeogenesis Inferred from electronic annotation. Source: UniProtKB-UniPathway glycolysis Inferred from mutant phenotype PubMed 11329176. Source: SGD pentose-phosphate shunt Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrion Inferred from direct assay PubMed 16962558. Source: SGD plasma membrane Inferred from direct assay PubMed 16622836. Source: SGD
Molecular_function	triose-phosphate isomerase activity Inferred from direct assay PubMed 236471. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 248

247

Triosephosphate isomerase

PRO_0000090169

Sites

Active site

95

1

Electrophile

Active site

165

1

Proton acceptor

Binding site

10

1

Substrate

Binding site

12

1

Substrate

Amino acid modifications

Modified residue

71

1

Phosphoserine Ref.9

Modified residue

96

1

Phosphoserine Ref.8

Modified residue

100

1

Phosphoserine Ref.8

Modified residue

211

1

Phosphoserine Ref.9

Modified residue

215

1

Phosphoserine Ref.9

Secondary structure

1

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248

Helix Strand Turn

Details...

Beta strand

5 – 10

6

Helix

17 – 29

13

Beta strand

36 – 41

6

Helix

44 – 46

3

Helix

47 – 53

7

Beta strand

59 – 64

6

Beta strand

68 – 73

6

Helix

80 – 85

6

Beta strand

90 – 94

5

Helix

96 – 100

5

Helix

106 – 118

13

Beta strand

122 – 127

6

Helix

131 – 135

5

Helix

139 – 153

15

Beta strand

160 – 164

5

Helix

167 – 169

3

Turn

170 – 172

3

Helix

178 – 196

19

Helix

198 – 203

6

Beta strand

206 – 211

6

Turn

214 – 216

3

Helix

217 – 220

4

Beta strand

228 – 232

5

Helix

233 – 236

4

Helix

239 – 244

6

Turn

245 – 247

3

Sequences

	Sequence		Length	Mass (Da)
	P00942 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 8429251C4DF51F86	FASTA	248	26,795
	10 20 30 40 50 60 MARTFFVGGN FKLNGSKQSI KEIVERLNTA SIPENVEVVI CPPATYLDYS VSLVKKPQVT 70 80 90 100 110 120 VGAQNAYLKA SGAFTGENSV DQIKDVGAKW VILGHSERRS YFHEDDKFIA DKTKFALGQG 130 140 150 160 170 180 VGVILCIGET LEEKKAGKTL DVVERQLNAV LEEVKDWTNV VVAYEPVWAI GTGLAATPED 190 200 210 220 230 240 AQDIHASIRK FLASKLGDKA ASELRILYGG SANGSNAVTF KDKADVDGFL VGGASLKPEF VDIINSRN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] 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]	"Protein identifications for a Saccharomyces cerevisiae protein database." Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S. Electrophoresis 15:1466-1486(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 56-84 AND 90-101. Strain: ATCC 204508 / S288c.
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-100, MASS SPECTROMETRY.
[9]	"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; SER-211 AND SER-215, MASS SPECTROMETRY.
[10]	"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).
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J01366 Genomic DNA. Translation: AAA88757.1.
Z49209 Genomic DNA. Translation: CAA89080.1.
AY557654 Genomic DNA. Translation: AAS55980.1.
BK006938 Genomic DNA. Translation: DAA11897.1.

PIR

ISBYT. A01168.

RefSeq

NP_010335.1. NM_001180358.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I45	X-ray	1.80	A/B	2-247	[»]
1NEY	X-ray	1.20	A/B	2-248	[»]
1NF0	X-ray	1.60	A/B	2-248	[»]
1YPI	X-ray	1.90	A/B	2-248	[»]
2YPI	X-ray	2.50	A/B	2-248	[»]
3YPI	X-ray	2.80	A/B	2-247	[»]
4FF7	X-ray	1.86	A/B	1-248	[»]
7TIM	X-ray	1.90	A/B	2-247	[»]

DisProt

DP00430.

ProteinModelPortal

P00942.

SMR

P00942. Positions 2-248.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6671N.

IntAct

P00942. 6 interactions.

MINT

MINT-614733.

STRING

4932.YDR050C.

2D gel databases

COMPLUYEAST-2DPAGE

P00942.

SWISS-2DPAGE

P00942.

Proteomic databases

PaxDb

P00942.

PeptideAtlas

P00942.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDR050C; YDR050C; YDR050C.

GeneID

851620.

KEGG

sce:YDR050C.

Organism-specific databases

SGD

S000002457. TPI1.

Phylogenomic databases

eggNOG

COG0149.

GeneTree

ENSGT00390000013354.

HOGENOM

HOG000226413.

KO

K01803.

OMA

QEVCGAI.

OrthoDB

EOG479JH2.

Enzyme and pathway databases

SABIO-RK

P00942.

UniPathway

UPA00109; UER00189.
UPA00138.

Gene expression databases

Genevestigator

P00942.

GermOnline

YDR050C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

InterPro

IPR013785. Aldolase_TIM.
IPR022896. TrioseP_Isoase_bac/euk.
IPR000652. Triosephosphate_isomerase.
IPR020861. Triosephosphate_isomerase_AS.
[Graphical view]

PANTHER

PTHR21139. PTHR21139. 1 hit.

Pfam

PF00121. TIM. 1 hit.
[Graphical view]

SUPFAM

SSF51351. Triophos_ismrse. 1 hit.

TIGRFAMs

TIGR00419. tim. 1 hit.

PROSITE

PS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00942.

NextBio

969151.

Entry information

Entry name

TPIS_YEAST

Accession

Primary (citable) accession number: P00942
Secondary accession number(s): D6VS37

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 147 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program