ID   TPIS_XENLA              Reviewed;         248 AA.
AC   Q7ZWN5;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 87.
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; Synonyms=tpi;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU10127}.
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; BC046864; AAH46864.1; -; mRNA.
DR   RefSeq; NP_001080476.1; NM_001087007.1.
DR   AlphaFoldDB; Q7ZWN5; -.
DR   SMR; Q7ZWN5; -.
DR   BioGRID; 98410; 1.
DR   DNASU; 380168; -.
DR   GeneID; 380168; -.
DR   KEGG; xla:380168; -.
DR   CTD; 380168; -.
DR   Xenbase; XB-GENE-866354; tpi1.S.
DR   OMA; IEKNGTM; -.
DR   OrthoDB; 1272577at2759; -.
DR   UniPathway; UPA00109; UER00189.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000186698; Chromosome 7S.
DR   Bgee; 380168; Expressed in oocyte and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Lyase;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..248
FT                   /note="Triosephosphate isomerase"
FT                   /id="PRO_0000345142"
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         11
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT   BINDING         13
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
SQ   SEQUENCE   248 AA;  26762 MW;  2EC929CD0CF6E804 CRC64;
     MSPRKFFVGG NWKMNGDKKS LGELINTLNS GKMNADTEVV CGAPAIYLDF ARQKLDAKIA
     LSAQNCYKVA KGAFTGEISP AMIKDCGATW VILGHSERRH VFGECDELIG QKVAHALSEG
     IGVIACIGEK LDQREAGITE KVVFEQTKAI ADNVKDWSKV VLAYEPVWAI GTGKTATPEQ
     AQEVHKKLRE WVKTNVSEGV AQSVRIIYGG SVTGGTCREL AGQPDIDGFL VGGASLKPEF
     IEIINAKH