TPIS_YEAST
ID TPIS_YEAST Reviewed; 248 AA.
AC P00942; D6VS37;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=Triosephosphate isomerase;
DE Short=TIM;
DE EC=5.3.1.1;
DE AltName: Full=Triose-phosphate isomerase;
GN Name=TPI1; OrderedLocusNames=YDR050C; ORFNames=YD9609.05C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6759603;
RA Alber T., Kawasaki G.;
RT "Nucleotide sequence of the triose phosphate isomerase gene of
RT Saccharomyces cerevisiae.";
RL J. Mol. Appl. Genet. 1:419-434(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP PROTEIN SEQUENCE OF 2-15.
RX PubMed=7005233; DOI=10.1016/s0021-9258(19)69972-2;
RA Alber T., Hartman F.C., Johnson R.M., Petsko G.A., Tsernoglou D.;
RT "Crystallization of yeast triose phosphate isomerase from polyethylene
RT glycol.";
RL J. Biol. Chem. 256:1356-1361(1981).
RN [6]
RP PROTEIN SEQUENCE OF 56-84 AND 90-101.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7895733; DOI=10.1002/elps.11501501210;
RA Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
RA Volpe T., Warner J.R., McLaughlin C.S.;
RT "Protein identifications for a Saccharomyces cerevisiae protein database.";
RL Electrophoresis 15:1466-1486(1994).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71 AND SER-215, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4; SER-71 AND SER-215, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [12]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-223, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=2204417; DOI=10.1021/bi00480a009;
RA Lolis E., Alber T.C., Davenport R.C., Rose D., Hartman F.C., Petsko G.A.;
RT "Structure of yeast triosephosphate isomerase at 1.9-A resolution.";
RL Biochemistry 29:6609-6618(1990).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH 2-P-GLYCOLATE.
RX PubMed=2204418; DOI=10.1021/bi00480a010;
RA Lolis E., Petsko G.A.;
RT "Crystallographic analysis of the complex between triosephosphate isomerase
RT and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis.";
RL Biochemistry 29:6619-6625(1990).
RN [15]
RP COMPARISON OF X-RAY STRUCTURES.
RX PubMed=1569570; DOI=10.1016/0022-2836(92)90473-w;
RA Wierenga R.K., Noble M.E.M., Davenport R.C.;
RT "Comparison of the refined crystal structures of liganded and unliganded
RT chicken, yeast and trypanosomal triosephosphate isomerase.";
RL J. Mol. Biol. 224:1115-1126(1992).
RN [16]
RP REVIEW.
RX PubMed=3331346; DOI=10.1101/sqb.1987.052.01.069;
RA Alber T.C., Davenport R.C., Giammona D.A., Lolis E., Petsko G.A., Ringe D.;
RT "Crystallography and site-directed mutagenesis of yeast triosephosphate
RT isomerase: what can we learn about catalysis from a 'simple' enzyme?";
RL Cold Spring Harb. Symp. Quant. Biol. 52:603-613(1987).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, AND
RP HOMODIMERIZATION.
RX PubMed=12509510; DOI=10.1073/pnas.0233793100;
RA Jogl G., Rozovsky S., McDermott A.E., Tong L.;
RT "Optimal alignment for enzymatic proton transfer: structure of the
RT Michaelis complex of triosephosphate isomerase at 1.2-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:50-55(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate;
CC Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776;
CC EC=5.3.1.1;
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate from glycerone phosphate: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12509510}.
CC -!- MISCELLANEOUS: Present with 207000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000305}.
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DR EMBL; J01366; AAA88757.1; -; Genomic_DNA.
DR EMBL; Z49209; CAA89080.1; -; Genomic_DNA.
DR EMBL; AY557654; AAS55980.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11897.1; -; Genomic_DNA.
DR PIR; A01168; ISBYT.
DR RefSeq; NP_010335.1; NM_001180358.1.
DR PDB; 1I45; X-ray; 1.80 A; A/B=2-248.
DR PDB; 1NEY; X-ray; 1.20 A; A/B=2-248.
DR PDB; 1NF0; X-ray; 1.60 A; A/B=2-248.
DR PDB; 1YPI; X-ray; 1.90 A; A/B=2-248.
DR PDB; 2YPI; X-ray; 2.50 A; A/B=2-248.
DR PDB; 3YPI; X-ray; 2.80 A; A/B=2-248.
DR PDB; 4FF7; X-ray; 1.86 A; A/B=1-248.
DR PDB; 7TIM; X-ray; 1.90 A; A/B=2-248.
DR PDBsum; 1I45; -.
DR PDBsum; 1NEY; -.
DR PDBsum; 1NF0; -.
DR PDBsum; 1YPI; -.
DR PDBsum; 2YPI; -.
DR PDBsum; 3YPI; -.
DR PDBsum; 4FF7; -.
DR PDBsum; 7TIM; -.
DR AlphaFoldDB; P00942; -.
DR BMRB; P00942; -.
DR PCDDB; P00942; -.
DR SMR; P00942; -.
DR BioGRID; 32104; 158.
DR DIP; DIP-6671N; -.
DR IntAct; P00942; 14.
DR MINT; P00942; -.
DR STRING; 4932.YDR050C; -.
DR iPTMnet; P00942; -.
DR COMPLUYEAST-2DPAGE; P00942; -.
DR SWISS-2DPAGE; P00942; -.
DR MaxQB; P00942; -.
DR PaxDb; P00942; -.
DR PRIDE; P00942; -.
DR TopDownProteomics; P00942; -.
DR EnsemblFungi; YDR050C_mRNA; YDR050C; YDR050C.
DR GeneID; 851620; -.
DR KEGG; sce:YDR050C; -.
DR SGD; S000002457; TPI1.
DR VEuPathDB; FungiDB:YDR050C; -.
DR eggNOG; KOG1643; Eukaryota.
DR GeneTree; ENSGT00390000013354; -.
DR HOGENOM; CLU_024251_2_0_1; -.
DR InParanoid; P00942; -.
DR OMA; QEVCGAI; -.
DR BioCyc; YEAST:YDR050C-MON; -.
DR BRENDA; 5.3.1.1; 984.
DR Reactome; R-SCE-70171; Glycolysis.
DR Reactome; R-SCE-70263; Gluconeogenesis.
DR SABIO-RK; P00942; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; P00942; -.
DR PRO; PR:P00942; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P00942; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0004807; F:triose-phosphate isomerase activity; IDA:SGD.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0019563; P:glycerol catabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IMP:SGD.
DR CDD; cd00311; TIM; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00147_B; TIM_B; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035990; TIM_sf.
DR InterPro; IPR022896; TrioseP_Isoase_bac/euk.
DR InterPro; IPR000652; Triosephosphate_isomerase.
DR InterPro; IPR020861; Triosephosphate_isomerase_AS.
DR PANTHER; PTHR21139; PTHR21139; 1.
DR Pfam; PF00121; TIM; 1.
DR SUPFAM; SSF51351; SSF51351; 1.
DR TIGRFAMs; TIGR00419; tim; 1.
DR PROSITE; PS00171; TIM_1; 1.
DR PROSITE; PS51440; TIM_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Gluconeogenesis; Glycolysis;
KW Isomerase; Isopeptide bond; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7005233"
FT CHAIN 2..248
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090169"
FT ACT_SITE 95
FT /note="Electrophile"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12509510"
FT BINDING 12
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12509510"
FT MOD_RES 4
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CROSSLNK 223
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:1NEY"
FT HELIX 17..29
FT /evidence="ECO:0007829|PDB:1NEY"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:1NEY"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:1NEY"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:1NEY"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:1NEY"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:1NEY"
FT HELIX 80..85
FT /evidence="ECO:0007829|PDB:1NEY"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:1NEY"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:1NEY"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:1NEY"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:1NEY"
FT HELIX 131..135
FT /evidence="ECO:0007829|PDB:1NEY"
FT HELIX 139..153
FT /evidence="ECO:0007829|PDB:1NEY"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:1NEY"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:4FF7"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:1NEY"
FT HELIX 178..196
FT /evidence="ECO:0007829|PDB:1NEY"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:1NEY"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:1NEY"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:1NEY"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:1NEY"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:1NEY"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:1NEY"
FT HELIX 239..244
FT /evidence="ECO:0007829|PDB:1NEY"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:1NEY"
SQ SEQUENCE 248 AA; 26795 MW; 8429251C4DF51F86 CRC64;
MARTFFVGGN FKLNGSKQSI KEIVERLNTA SIPENVEVVI CPPATYLDYS VSLVKKPQVT
VGAQNAYLKA SGAFTGENSV DQIKDVGAKW VILGHSERRS YFHEDDKFIA DKTKFALGQG
VGVILCIGET LEEKKAGKTL DVVERQLNAV LEEVKDWTNV VVAYEPVWAI GTGLAATPED
AQDIHASIRK FLASKLGDKA ASELRILYGG SANGSNAVTF KDKADVDGFL VGGASLKPEF
VDIINSRN
