TPIS_CAEEL
ID TPIS_CAEEL Reviewed; 247 AA.
AC Q10657; Q9U2R2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 143.
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=tpi-1; ORFNames=Y17G7B.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7667320; DOI=10.1073/pnas.92.18.8507;
RA Logsdon J.M. Jr., Tyshenko M.G., Dixon C., D-Jafari J., Walker V.K.,
RA Palmer J.D.;
RT "Seven newly discovered intron positions in the triose-phosphate isomerase
RT gene: evidence for the introns-late theory.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:8507-8511(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-247, AND HOMODIMERIZATION.
RX PubMed=12696058; DOI=10.1002/prot.10364;
RA Symersky J., Li S., Carson M., Luo M.;
RT "Structural genomics of Caenorhabditis elegans: triosephosphate
RT isomerase.";
RL Proteins 51:484-486(2003).
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 ECO:0000269|PubMed:12696058}.
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; U23081; AAA79846.1; -; Genomic_DNA.
DR EMBL; AL023828; CAA19447.1; -; Genomic_DNA.
DR PIR; T26493; T26493.
DR RefSeq; NP_496563.1; NM_064162.4.
DR PDB; 1MO0; X-ray; 1.70 A; A/B=2-247.
DR PDBsum; 1MO0; -.
DR AlphaFoldDB; Q10657; -.
DR SMR; Q10657; -.
DR BioGRID; 40148; 51.
DR STRING; 6239.Y17G7B.7; -.
DR World-2DPAGE; 0020:Q10657; -.
DR EPD; Q10657; -.
DR PaxDb; Q10657; -.
DR PeptideAtlas; Q10657; -.
DR EnsemblMetazoa; Y17G7B.7.1; Y17G7B.7.1; WBGene00006601.
DR UCSC; Y17G7B.7.1; c. elegans.
DR WormBase; Y17G7B.7; CE19040; WBGene00006601; tpi-1.
DR eggNOG; KOG1643; Eukaryota.
DR GeneTree; ENSGT00390000013354; -.
DR HOGENOM; CLU_024251_2_0_1; -.
DR InParanoid; Q10657; -.
DR OMA; QEVCGAI; -.
DR OrthoDB; 1272577at2759; -.
DR PhylomeDB; Q10657; -.
DR BRENDA; 5.3.1.1; 1045.
DR Reactome; R-CEL-70171; Glycolysis.
DR Reactome; R-CEL-70263; Gluconeogenesis.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; Q10657; -.
DR PRO; PR:Q10657; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006601; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030016; C:myofibril; HDA:WormBase.
DR GO; GO:0008929; F:methylglyoxal synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004807; F:triose-phosphate isomerase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IMP:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0019563; P:glycerol catabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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 3D-structure; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Lyase;
KW Reference proteome.
FT CHAIN 1..247
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090127"
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"
FT CONFLICT 218..219
FT /note="EL -> DV (in Ref. 1; AAA79846)"
FT /evidence="ECO:0000305"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:1MO0"
FT HELIX 17..29
FT /evidence="ECO:0007829|PDB:1MO0"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:1MO0"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:1MO0"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:1MO0"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:1MO0"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:1MO0"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:1MO0"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:1MO0"
FT HELIX 95..99
FT /evidence="ECO:0007829|PDB:1MO0"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:1MO0"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:1MO0"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:1MO0"
FT HELIX 138..150
FT /evidence="ECO:0007829|PDB:1MO0"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:1MO0"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:1MO0"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:1MO0"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:1MO0"
FT HELIX 177..194
FT /evidence="ECO:0007829|PDB:1MO0"
FT HELIX 197..202
FT /evidence="ECO:0007829|PDB:1MO0"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:1MO0"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:1MO0"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:1MO0"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:1MO0"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:1MO0"
FT HELIX 238..246
FT /evidence="ECO:0007829|PDB:1MO0"
SQ SEQUENCE 247 AA; 26574 MW; B4ADF85D0D1A37EA CRC64;
MTRKFFVGGN WKMNGDYASV DGIVTFLNAS ADNSSVDVVV APPAPYLAYA KSKLKAGVLV
AAQNCYKVPK GAFTGEISPA MIKDLGLEWV ILGHSERRHV FGESDALIAE KTVHALEAGI
KVVFCIGEKL EEREAGHTKD VNFRQLQAIV DKGVSWENIV IAYEPVWAIG TGKTASGEQA
QEVHEWIRAF LKEKVSPAVA DATRIIYGGS VTADNAAELG KKPDIDGFLV GGASLKPDFV
KIINARS
