TPIS_PROCL
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 03-AUG-2022, entry version 34.
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}.
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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 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; -; 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 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
