ID   TPIS_LATCH              Reviewed;         247 AA.
AC   P00941;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 96.
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};
OS   Latimeria chalumnae (Coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=4824206; DOI=10.1042/bj1370185;
RA   Kolb E., Harris J.I., Bridgen J.;
RT   "Triose phosphate isomerase from the coelacanth. An approach to the rapid
RT   determination of an amino acid sequence with small amounts of material.";
RL   Biochem. J. 137:185-197(1974).
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   -!- 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   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {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   -!- 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   PIR; A01167; ISLAT.
DR   AlphaFoldDB; P00941; -.
DR   SMR; P00941; -.
DR   UniPathway; UPA00109; UER00189.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000008672; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008929; F:methylglyoxal synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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   Cytoplasm; Direct protein sequencing; Gluconeogenesis; Glycolysis;
KW   Isomerase; Lyase; Reference proteome.
FT   CHAIN           1..247
FT                   /note="Triosephosphate isomerase"
FT                   /id="PRO_0000090122"
FT   ACT_SITE        94
FT                   /note="Electrophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT   ACT_SITE        164
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT   BINDING         10
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT   BINDING         12
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
SQ   SEQUENCE   247 AA;  26731 MW;  AE3C9B92AEF8D6B0 CRC64;
     APRKFFVGGN WKMNGDKKSL GELIQTLNAA KVPFTGEIVC APPEAYLDFA RLKVDPKFGV
     AAQNCYKVSK GAFTGEISPA MIKDCGVTWV ILGHSERRHV FGESDELIGQ KVSHALSEGL
     GVVACIGEKL DEREAGITEG VVFEVTEVIA DDVKDWSKVV LAYEPVWAIG TGKTASPQQS
     QELHGKLRKW LKENVSETVA DSVRIIYGGS VTGATCKELA SEPDVDGFLV GGASLKPEFV
     EYKDVRQ