ID TPIS_PROCL Reviewed; 248 AA. AC F5A6E9; DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 1. DT 13-SEP-2023, entry version 37. DE RecName: Full=Triosephosphate isomerase {ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000255|RuleBase:RU363013, ECO:0000303|PubMed:28072528}; DE Short=TIM {ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000303|PubMed:28072528}; DE EC=5.3.1.1 {ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000255|RuleBase:RU363013}; 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 {ECO:0000255|PROSITE-ProRule:PRU10127}; DE AltName: Allergen=Pro c 8.0101 {ECO:0000305}; OS Procambarus clarkii (Red swamp crayfish). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea; OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea; OC Astacoidea; Cambaridae; Procambarus. OX NCBI_TaxID=6728 {ECO:0000312|EMBL:AEB54655.1}; RN [1] {ECO:0000312|EMBL:AEB54655.1} RP NUCLEOTIDE SEQUENCE [MRNA]. RA Dong Z., Zhao Q.; RT "Molecular cloning of 47 genes in the red swamp crayfish, Procambarus RT clarkii."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP PROTEIN SEQUENCE OF 7-14; 20-30; 53-68; 72-84; 99-112; 113-122; 123-134; RP 135-148; 149-159; 175-189; 188-193; 190-205; 206-222 AND 223-248, RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, IDENTIFICATION BY MASS RP SPECTROMETRY, ALLERGEN, 3D-STRUCTURE MODELING, REGIONS, AND CIRCULAR RP DICHROISM ANALYSIS. RC TISSUE=Skeletal muscle {ECO:0000303|PubMed:28072528}; RX PubMed=28072528; DOI=10.1021/acs.jafc.6b04587; RA Yang Y., Zhang Y.X., Liu M., Maleki S.J., Zhang M.L., Liu Q.M., Cao M.J., RA Su W.J., Liu G.M.; RT "Triosephosphate Isomerase and Filamin C Share Common Epitopes as Novel RT Allergens of Procambarus clarkii."; RL J. Agric. Food Chem. 65:950-963(2017). 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=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 ECO:0000255|RuleBase:RU363013}; 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 -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Unstable only at extreme acidic (pH 1.0) or alkaline conditions (pH CC 11.0). IgE-binding activity is relatively stable under acidic and CC alkaline conditions, however the activity is increased between pH CC 2.0-3.0. {ECO:0000269|PubMed:28072528}; CC Temperature dependence: CC Stable up to 100 degrees Celsius. IgE-binding activity is reduced CC with increasing temperature higher than 60 degrees Celsius. CC {ECO:0000269|PubMed:28072528}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000255|RuleBase:RU363013}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate from glycerone phosphate: step 1/1. {ECO:0000255|PROSITE- CC ProRule:PRU10127, ECO:0000255|RuleBase:RU363013}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|PROSITE-ProRule:PRU10127}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU10127}. CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle (at protein level). CC {ECO:0000269|PubMed:28072528}. CC -!- ALLERGEN: Causes an allergic reaction in human. Binds weakly to IgE in CC 38% of the 13 patients tested allergic to crustaceans (crayfish and CC shrimp). {ECO:0000269|PubMed:28072528}. CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family. CC {ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000255|RuleBase:RU363013}. 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; HQ414580; AEB54655.1; -; mRNA. DR AlphaFoldDB; F5A6E9; -. DR SMR; F5A6E9; -. DR Allergome; 12144; Pro c 8. DR Allergome; 12145; Pro c 8.0101. DR EnsemblMetazoa; XM_045749886.1; XP_045605842.1; LOC123762994. DR OrthoDB; 167479at2759; -. DR UniPathway; UPA00109; UER00189. DR UniPathway; UPA00138; -. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW. 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:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway. DR GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; ISS:UniProtKB. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. 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 Allergen; Cytoplasm; Direct protein sequencing; Gluconeogenesis; KW Glycolysis; IgE-binding protein; Isomerase; Lyase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P00940" FT CHAIN 2..248 FT /note="Triosephosphate isomerase" FT /id="PRO_0000449137" FT REGION 16..30 FT /note="IgE-binding" FT /evidence="ECO:0000269|PubMed:28072528" FT REGION 166..180 FT /note="IgE-binding" FT /evidence="ECO:0000269|PubMed:28072528" FT REGION 205..219 FT /note="IgE-binding" FT /evidence="ECO:0000269|PubMed:28072528" FT ACT_SITE 95 FT /note="Electrophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127" FT ACT_SITE 165 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127" FT BINDING 12 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127" FT BINDING 14 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127" SQ SEQUENCE 248 AA; 27146 MW; D00C3C38C1DBCB83 CRC64; MANQRKFFVG GNWKMNGDRA GIDSIISFMK GPLSADTEVV VGCPQCYLMY TREHLPSNIG VAAQNCYKVA KGAFTGEISP SMIKDCGCEW VILGHSERRN VFNEPDTLIS EKVGHALEAG LKVIPCIGEK LEERESNRTE EVVFAQMKAL VPNISDWSRV VIAYEPVWAI GTGKTATPEQ AQEVHAKLRQ WLRDNVNAEV ADSTRIIYGG SVTPGNCKEL AKTGDIDGFL VGGASLKPDF VQIINARD //