ID TPIS_CHICK Reviewed; 248 AA. AC P00940; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 174. DE RecName: Full=Triosephosphate isomerase; DE Short=TIM; DE EC=5.3.1.1 {ECO:0000255|PROSITE-ProRule:PRU10127}; DE AltName: Full=Methylglyoxal synthase {ECO:0000250|UniProtKB:P00939}; DE EC=4.2.3.3 {ECO:0000250|UniProtKB:P00939}; DE AltName: Full=Triose-phosphate isomerase; GN Name=TPI1; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3885220; DOI=10.1073/pnas.82.7.2014; RA Straus D., Gilbert W.; RT "Chicken triosephosphate isomerase complements an Escherichia coli RT deficiency."; RL Proc. Natl. Acad. Sci. U.S.A. 82:2014-2018(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3837846; DOI=10.1128/mcb.5.12.3497-3506.1985; RA Straus D., Gilbert W.; RT "Genetic engineering in the Precambrian: structure of the chicken RT triosephosphate isomerase gene."; RL Mol. Cell. Biol. 5:3497-3506(1985). RN [3] RP PROTEIN SEQUENCE OF 2-248. RX PubMed=4463937; DOI=10.1042/bj1390011; RA Furth A.J., Milman J.D., Priddle J.D., Offord R.E.; RT "Studies on the subunit structure and amino acid sequence of trisoe RT phosphate isomerase from chicken breast muscle."; RL Biochem. J. 139:11-22(1974). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND SEQUENCE REVISION. RX PubMed=1134550; DOI=10.1038/255609a0; RA Banner D.W., Bloomer A.C., Petsko G.A., Phillips D.C., Pogson C.I., RA Wilson I.A., Corran P.H., Furth A.J., Milman J.D., Offord R.E., RA Priddle J.D., Waley S.G.; RT "Structure of chicken muscle triose phosphate isomerase determined RT crystallographically at 2.5-A resolution using amino acid sequence data."; RL Nature 255:609-614(1975). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND MUTAGENESIS OF HIS-95 AND RP GLU-165. RX PubMed=2361134; DOI=10.1021/bi00469a012; RA Blacklow S.C., Knowles J.R.; RT "How can a catalytic lesion be offset? The energetics of two RT pseudorevertant triosephosphate isomerases."; RL Biochemistry 29:4099-4108(1990). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=985462; DOI=10.1016/0006-291x(76)90972-4; RA Banner D.W., Bloomer A.C., Petsko G.A., Phillips D.C., Wilson I.A.; RT "Atomic coordinates for triose phosphate isomerase from chicken muscle."; RL Biochem. Biophys. Res. Commun. 72:146-155(1976). RN [7] 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 [8] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT ASP-165 IN COMPLEX WITH RP SUBSTRATE ANALOG, ACTIVE SITE, AND SUBSTRATE BINDING-SITE. RX PubMed=8130195; DOI=10.1021/bi00176a012; RA Zhang Z., Sugio S., Komives E.A., Liu K.D., Knowles J.R., Petsko G.A., RA Ringe D.; RT "Crystal structure of recombinant chicken triosephosphate isomerase- RT phosphoglycolohydroxamate complex at 1.8-A resolution."; RL Biochemistry 33:2830-2837(1994). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RA Artymiuk P.J., Taylor W.R., Phillips D.C.; RL Submitted (AUG-1998) to the PDB data bank. CC -!- FUNCTION: Triosephosphate isomerase is an extremely efficient metabolic CC enzyme that catalyzes the interconversion between dihydroxyacetone CC phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis CC and gluconeogenesis. {ECO:0000250|UniProtKB:P00939}. CC -!- FUNCTION: It is also responsible for the non-negligible production of CC methylglyoxal a reactive cytotoxic side-product that modifies and can CC alter proteins, DNA and lipids. {ECO:0000250|UniProtKB:P00939}. CC -!- CATALYTIC ACTIVITY: CC Reaction=dihydroxyacetone phosphate = methylglyoxal + phosphate; CC Xref=Rhea:RHEA:17937, ChEBI:CHEBI:17158, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57642; EC=4.2.3.3; CC Evidence={ECO:0000250|UniProtKB:P00939}; 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; Evidence={ECO:0000255|PROSITE-ProRule:PRU10127}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate from glycerone phosphate: step 1/1. {ECO:0000255|PROSITE- CC ProRule:PRU10127}. CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000255|PROSITE-ProRule:PRU10127}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|PROSITE-ProRule:PRU10127, CC ECO:0000269|PubMed:8130195}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU10127}. CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M11314; AAA49094.1; -; mRNA. DR EMBL; M11941; AAA49095.1; -; Genomic_DNA. DR PIR; A23448; ISCHT. DR RefSeq; NP_990782.1; NM_205451.1. DR PDB; 1SPQ; X-ray; 2.16 A; A/B=2-248. DR PDB; 1SQ7; X-ray; 2.85 A; A/B=2-248. DR PDB; 1SSD; X-ray; 2.90 A; A/B=2-248. DR PDB; 1SSG; X-ray; 2.90 A; A/B=2-248. DR PDB; 1SU5; X-ray; 2.70 A; A/B=2-248. DR PDB; 1SW0; X-ray; 1.71 A; A/B=1-248. DR PDB; 1SW3; X-ray; 2.03 A; A/B=1-248. DR PDB; 1SW7; X-ray; 2.22 A; A/B=1-248. DR PDB; 1TIM; X-ray; 2.50 A; A/B=2-248. DR PDB; 1TPB; X-ray; 1.90 A; 1/2=2-248. DR PDB; 1TPC; X-ray; 1.90 A; 1/2=2-248. DR PDB; 1TPH; X-ray; 1.80 A; 1/2=2-248. DR PDB; 1TPU; X-ray; 1.90 A; A/B=2-248. DR PDB; 1TPV; X-ray; 1.90 A; A/B=2-248. DR PDB; 1TPW; X-ray; 1.90 A; A/B=2-248. DR PDB; 4P61; X-ray; 1.34 A; A/B=1-248. DR PDB; 8TIM; X-ray; 2.50 A; A/B=2-248. DR PDBsum; 1SPQ; -. DR PDBsum; 1SQ7; -. DR PDBsum; 1SSD; -. DR PDBsum; 1SSG; -. DR PDBsum; 1SU5; -. DR PDBsum; 1SW0; -. DR PDBsum; 1SW3; -. DR PDBsum; 1SW7; -. DR PDBsum; 1TIM; -. DR PDBsum; 1TPB; -. DR PDBsum; 1TPC; -. DR PDBsum; 1TPH; -. DR PDBsum; 1TPU; -. DR PDBsum; 1TPV; -. DR PDBsum; 1TPW; -. DR PDBsum; 4P61; -. DR PDBsum; 8TIM; -. DR AlphaFoldDB; P00940; -. DR BMRB; P00940; -. DR SMR; P00940; -. DR BioGRID; 676684; 1. DR IntAct; P00940; 1. DR STRING; 9031.ENSGALP00000023396; -. DR PaxDb; 9031-ENSGALP00000023396; -. DR Ensembl; ENSGALT00000071768; ENSGALP00000044536; ENSGALG00000014526. DR Ensembl; ENSGALT00010057016.1; ENSGALP00010034676.1; ENSGALG00010023392.1. DR Ensembl; ENSGALT00015019746; ENSGALP00015010895; ENSGALG00015008236. DR GeneID; 396435; -. DR KEGG; gga:396435; -. DR CTD; 7167; -. DR VEuPathDB; HostDB:geneid_396435; -. DR eggNOG; KOG1643; Eukaryota. DR GeneTree; ENSGT00390000013354; -. DR HOGENOM; CLU_024251_2_0_1; -. DR InParanoid; P00940; -. DR OMA; GNWKMHM; -. DR OrthoDB; 167479at2759; -. DR PhylomeDB; P00940; -. DR TreeFam; TF300829; -. DR BRENDA; 5.3.1.1; 1306. DR Reactome; R-GGA-352875; Gluconeogenesis. DR Reactome; R-GGA-352882; Glycolysis. DR Reactome; R-GGA-70171; Glycolysis. DR Reactome; R-GGA-70263; Gluconeogenesis. DR SABIO-RK; P00940; -. DR UniPathway; UPA00109; UER00189. DR UniPathway; UPA00138; -. DR EvolutionaryTrace; P00940; -. DR PRO; PR:P00940; -. DR Proteomes; UP000000539; Chromosome 1. DR Bgee; ENSGALG00000014526; Expressed in muscle tissue and 14 other cell types or tissues. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008929; F:methylglyoxal synthase activity; ISS:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0004807; F:triose-phosphate isomerase activity; ISS:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl. DR GO; GO:0061621; P:canonical glycolysis; IEA:Ensembl. DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central. DR GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; ISS:UniProtKB. DR GO; GO:0019563; P:glycerol catabolic process; IBA:GO_Central. DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central. DR GO; GO:0019242; P:methylglyoxal biosynthetic process; ISS:UniProtKB. DR CDD; cd00311; TIM; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 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 NCBIfam; TIGR00419; tim; 1. DR PANTHER; PTHR21139; TRIOSEPHOSPHATE ISOMERASE; 1. DR PANTHER; PTHR21139:SF2; TRIOSEPHOSPHATE ISOMERASE; 1. DR Pfam; PF00121; TIM; 1. DR SUPFAM; SSF51351; Triosephosphate isomerase (TIM); 1. DR PROSITE; PS00171; TIM_1; 1. DR PROSITE; PS51440; TIM_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Gluconeogenesis; KW Glycolysis; Isomerase; Lyase; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:4463937" FT CHAIN 2..248 FT /note="Triosephosphate isomerase" FT /id="PRO_0000090121" FT ACT_SITE 95 FT /note="Electrophile" FT /evidence="ECO:0000269|PubMed:8130195, FT ECO:0007744|PDB:1TPH" FT ACT_SITE 165 FT /note="Proton acceptor" FT /evidence="ECO:0000269|PubMed:8130195, FT ECO:0007744|PDB:1TPH" FT BINDING 11 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:8130195, FT ECO:0007744|PDB:1TPH" FT BINDING 13 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:8130195, FT ECO:0007744|PDB:1TPH" FT MUTAGEN 95 FT /note="H->N: Reduces activity 5000-fold." FT /evidence="ECO:0000269|PubMed:2361134" FT MUTAGEN 165 FT /note="E->D: Reduces activity 300-fold." FT /evidence="ECO:0000269|PubMed:2361134" FT CONFLICT 17..18 FT /note="DK -> KR (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 29 FT /note="N -> D (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 145..146 FT /note="EQ -> QE (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 194 FT /note="S -> T (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 202..204 FT /note="QST -> VQS (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 6..11 FT /evidence="ECO:0007829|PDB:4P61" FT HELIX 18..30 FT /evidence="ECO:0007829|PDB:4P61" FT STRAND 37..43 FT /evidence="ECO:0007829|PDB:4P61" FT HELIX 45..47 FT /evidence="ECO:0007829|PDB:4P61" FT HELIX 48..54 FT /evidence="ECO:0007829|PDB:4P61" FT STRAND 59..64 FT /evidence="ECO:0007829|PDB:4P61" FT STRAND 68..73 FT /evidence="ECO:0007829|PDB:4P61" FT HELIX 80..85 FT /evidence="ECO:0007829|PDB:4P61" FT STRAND 90..94 FT /evidence="ECO:0007829|PDB:4P61" FT HELIX 96..100 FT /evidence="ECO:0007829|PDB:4P61" FT HELIX 106..118 FT /evidence="ECO:0007829|PDB:4P61" FT STRAND 122..127 FT /evidence="ECO:0007829|PDB:4P61" FT HELIX 131..136 FT /evidence="ECO:0007829|PDB:4P61" FT HELIX 139..151 FT /evidence="ECO:0007829|PDB:4P61" FT HELIX 157..159 FT /evidence="ECO:0007829|PDB:4P61" FT STRAND 160..164 FT /evidence="ECO:0007829|PDB:4P61" FT HELIX 167..169 FT /evidence="ECO:0007829|PDB:1SW0" FT STRAND 170..173 FT /evidence="ECO:0007829|PDB:1SW0" FT HELIX 178..195 FT /evidence="ECO:0007829|PDB:4P61" FT HELIX 198..203 FT /evidence="ECO:0007829|PDB:4P61" FT STRAND 206..208 FT /evidence="ECO:0007829|PDB:4P61" FT TURN 214..216 FT /evidence="ECO:0007829|PDB:4P61" FT HELIX 217..221 FT /evidence="ECO:0007829|PDB:4P61" FT STRAND 228..232 FT /evidence="ECO:0007829|PDB:4P61" FT HELIX 233..236 FT /evidence="ECO:0007829|PDB:4P61" FT HELIX 240..244 FT /evidence="ECO:0007829|PDB:4P61" FT TURN 245..247 FT /evidence="ECO:0007829|PDB:4P61" SQ SEQUENCE 248 AA; 26620 MW; AFCC258E574DE982 CRC64; MAPRKFFVGG NWKMNGDKKS LGELIHTLNG AKLSADTEVV CGAPSIYLDF ARQKLDAKIG VAAQNCYKVP KGAFTGEISP AMIKDIGAAW VILGHSERRH VFGESDELIG QKVAHALAEG LGVIACIGEK LDEREAGITE KVVFEQTKAI ADNVKDWSKV VLAYEPVWAI GTGKTATPQQ AQEVHEKLRG WLKSHVSDAV AQSTRIIYGG SVTGGNCKEL ASQHDVDGFL VGGASLKPEF VDIINAKH //