ID   TPIS_ERWT9              Reviewed;         255 AA.
AC   B2VF53;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Triosephosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147};
DE            Short=TIM {ECO:0000255|HAMAP-Rule:MF_00147};
DE            Short=TPI {ECO:0000255|HAMAP-Rule:MF_00147};
DE            EC=5.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00147};
DE   AltName: Full=Triose-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147};
GN   Name=tpiA {ECO:0000255|HAMAP-Rule:MF_00147}; OrderedLocusNames=ETA_01060;
OS   Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS   4357 / Et1/99).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=465817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99;
RX   PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA   Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA   Geider K.;
RT   "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT   bacterium in the genus Erwinia.";
RL   Environ. Microbiol. 10:2211-2222(2008).
CC   -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes stereospecifically
CC       the conversion of dihydroxyacetone phosphate (DHAP) to D-
CC       glyceraldehyde-3-phosphate (G3P). {ECO:0000255|HAMAP-Rule:MF_00147}.
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|HAMAP-Rule:MF_00147};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00147}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate from glycerone phosphate: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_00147}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00147}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00147}.
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00147}.
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DR   EMBL; CU468135; CAO95152.1; -; Genomic_DNA.
DR   RefSeq; WP_012439878.1; NC_010694.1.
DR   AlphaFoldDB; B2VF53; -.
DR   SMR; B2VF53; -.
DR   STRING; 465817.ETA_01060; -.
DR   EnsemblBacteria; CAO95152; CAO95152; ETA_01060.
DR   KEGG; eta:ETA_01060; -.
DR   eggNOG; COG0149; Bacteria.
DR   HOGENOM; CLU_024251_2_1_6; -.
DR   OMA; QEVCGAI; -.
DR   OrthoDB; 1266295at2; -.
DR   UniPathway; UPA00109; UER00189.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001726; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT   CHAIN           1..255
FT                   /note="Triosephosphate isomerase"
FT                   /id="PRO_1000096497"
FT   ACT_SITE        95
FT                   /note="Electrophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT   ACT_SITE        167
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT   BINDING         9..11
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT   BINDING         173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT   BINDING         212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT   BINDING         233..234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
SQ   SEQUENCE   255 AA;  26610 MW;  8D36FDA3FDA6BBDF CRC64;
     MRHPLVMGNW KLNGNKQMVN ELIAGLRTEL SGVDGCGVAI APPVMYLEQA KHAISGSPVA
     LGAQNVDVNL SGAFTGEVSA DMLKDIGAQY IIIGHSERRT WHAESDDAIA KKFAVLKQTG
     LIPVLCIGET EAENEAGKTE EVCARQIDAV LNTQGADAFK GVVIAYEPVW AIGTGKSATP
     AQAQAVHKFI RDHIAKKDAT VAAQVIIQYG GSVNDKNAAE LFAQPDIDGA LVGGASLKAD
     AFAAIVKAAA AAKKA