ID TPIS_GEOSE Reviewed; 253 AA. AC P00943; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 2. DT 02-SEP-2026, entry version 135. DE RecName: Full=Triosephosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:8421318}; DE Short=TIM {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:8421318}; DE Short=TPI {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:8421318}; DE EC=5.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00147}; DE AltName: Full=Triose-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:8421318}; GN Name=tpiA {ECO:0000255|HAMAP-Rule:MF_00147}; Synonyms=tpi; OS Geobacillus stearothermophilus (Bacillus stearothermophilus). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Anoxybacillaceae; OC Geobacillus. OX NCBI_TaxID=1422; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=8421318; DOI=10.1006/jmbi.1993.1010; RA Rentier-Delrue F., Mande S.C., Moyens S., Terpstra P., Mainfroid V., RA Goraj K., Lion M., Hol W.G.J., Martial J.A.; RT "Cloning and overexpression of the triosephosphate isomerase genes from RT psychrophilic and thermophilic bacteria. Structural comparison of the RT predicted protein sequences."; RL J. Mol. Biol. 229:85-93(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8244026; DOI=10.1016/0378-1119(93)90188-9; RA Rentier-Delrue F., Moyens S., Lion M., Martial J.A.; RT "Sequence of the triosephosphate isomerase-encoding gene isolated from the RT thermophile Bacillus stearothermophilus."; RL Gene 134:137-138(1993). RN [3] RP PRELIMINARY PROTEIN SEQUENCE. RX PubMed=6105959; DOI=10.1111/j.1432-1033.1980.tb04755.x; RA Artavanis-Tsakonas S., Harris J.I.; RT "Primary structure of triosephosphate isomerase from Bacillus RT stearothermophilus."; RL Eur. J. Biochem. 108:599-611(1980). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, AND RP SUBUNIT. RX PubMed=8580851; DOI=10.1002/pro.5560041217; RA Delboni L.F., Mande S.C., Rentier-Delrue F., Mainfroid V., Turley S., RA Vellieux F.M.D., Martial J.A., Hol W.G.J.; RT "Crystal structure of recombinant triosephosphate isomerase from Bacillus RT stearothermophilus. An analysis of potential thermostability factors in six RT isomerases with known three-dimensional structures points to the importance RT of hydrophobic interactions."; RL Protein Sci. 4:2594-2604(1995). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT ASN-13 AND GLY-14 IN RP COMPLEX WITH SUBSTRATE ANALOG, MUTAGENESIS OF HIS-13 AND LYS-14, RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. RX PubMed=10383424; DOI=10.1074/jbc.274.27.19181; RA Alvarez M., Wouters J., Maes D., Mainfroid V., Rentier-Delrue F., Wyns L., RA Depiereux E., Martial J.A.; RT "Lys13 plays a crucial role in the functional adaptation of the RT thermophilic triose-phosphate isomerase from Bacillus stearothermophilus to RT high temperatures."; RL J. Biol. Chem. 274:19181-19187(1999). 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 ECO:0000269|PubMed:8421318}. 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 -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Temperature dependence: CC Optimum temperature is 60 degrees Celsius (PubMed:8421318). CC Thermostable (PubMed:10383424). {ECO:0000269|PubMed:10383424, CC ECO:0000269|PubMed:8421318}; 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 ECO:0000269|PubMed:10383424, ECO:0000269|PubMed:8580851}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X66129; CAA46920.1; -; Genomic_DNA. DR PIR; JT0768; ISBSTF. DR PDB; 1BTM; X-ray; 2.80 A; A/B=2-253. DR PDB; 2BTM; X-ray; 2.40 A; A/B=2-253. DR AlphaFoldDB; P00943; -. DR SMR; P00943; -. DR DrugBank; DB02726; 2-Phosphoglycolic Acid. DR BRENDA; 5.3.1.1; 623. DR UniPathway; UPA00109; UER00189. DR UniPathway; UPA00138; -. DR EvolutionaryTrace; P00943; -. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule. DR GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; IEA:TreeGrafter. DR GO; GO:0019563; P:glycerol catabolic process; IEA:TreeGrafter. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule. DR CDD; cd00311; TIM; 1. DR FunFam; 3.20.20.70:FF:000016; Triosephosphate isomerase; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 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 NCBIfam; TIGR00419; tim; 1. DR PANTHER; PTHR21139; TRIOSEPHOSPHATE ISOMERASE; 1. DR PANTHER; PTHR21139:SF42; TRIOSEPHOSPHATE ISOMERASE; 1. DR Pfam; PF00121; TIM; 1. DR SUPFAM; SSF51351; Triosephosphate isomerase (TIM); 1. DR PROSITE; PS00171; TIM_1; 1. DR PROSITE; PS51440; TIM_2; 1. DR PDBsum; 1BTM; -. DR PDBsum; 2BTM; -. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Gluconeogenesis; KW Glycolysis; Isomerase; Phosphoprotein. FT CHAIN 1..253 FT /note="Triosephosphate isomerase" FT /id="PRO_0000090178" FT ACT_SITE 95 FT /note="Electrophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147, FT ECO:0000305|PubMed:10383424, ECO:0000305|PubMed:8580851" FT ACT_SITE 167 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147, FT ECO:0000305|PubMed:10383424" FT BINDING 9..11 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147, FT ECO:0000269|PubMed:10383424, ECO:0000269|PubMed:8580851" FT BINDING 173 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147, FT ECO:0000269|PubMed:10383424, ECO:0000269|PubMed:8580851" FT BINDING 213 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147, FT ECO:0000269|PubMed:10383424, ECO:0000269|PubMed:8580851" FT BINDING 234..235 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147, FT ECO:0000269|PubMed:10383424, ECO:0000269|PubMed:8580851" FT MOD_RES 213 FT /note="Phosphoserine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147" FT MUTAGEN 13 FT /note="H->N: Displays poor thermostability, with an FT inactivation temperature of 37 degrees Celsius; when FT associated with G-14." FT /evidence="ECO:0000269|PubMed:10383424" FT MUTAGEN 14 FT /note="K->G: Displays poor thermostability, with an FT inactivation temperature of 37 degrees Celsius; when FT associated with N-13." FT /evidence="ECO:0000269|PubMed:10383424" FT CONFLICT 37 FT /note="I -> D (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 41 FT /note="Missing (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 47..48 FT /note="Missing (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 59 FT /note="L -> LQ (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 100 FT /note="Q -> H (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 135 FT /note="E -> Q (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 138..140 FT /note="QTN -> ETD (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 144 FT /note="Missing (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 157..158 FT /note="EQ -> QE (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 161..164 FT /note="QAVI -> IIL (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 169 FT /note="I -> L (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 231 FT /note="P -> A (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 248 FT /note="E -> Q (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 5..9 FT /evidence="ECO:0007829|PDB:2BTM" FT HELIX 16..26 FT /evidence="ECO:0007829|PDB:2BTM" FT TURN 27..29 FT /evidence="ECO:0007829|PDB:2BTM" FT TURN 33..35 FT /evidence="ECO:0007829|PDB:2BTM" FT STRAND 37..42 FT /evidence="ECO:0007829|PDB:2BTM" FT HELIX 44..46 FT /evidence="ECO:0007829|PDB:2BTM" FT HELIX 47..54 FT /evidence="ECO:0007829|PDB:2BTM" FT STRAND 57..64 FT /evidence="ECO:0007829|PDB:2BTM" FT STRAND 68..73 FT /evidence="ECO:0007829|PDB:2BTM" FT HELIX 80..86 FT /evidence="ECO:0007829|PDB:2BTM" FT STRAND 90..94 FT /evidence="ECO:0007829|PDB:2BTM" FT HELIX 96..101 FT /evidence="ECO:0007829|PDB:2BTM" FT HELIX 106..119 FT /evidence="ECO:0007829|PDB:2BTM" FT STRAND 122..127 FT /evidence="ECO:0007829|PDB:2BTM" FT HELIX 131..135 FT /evidence="ECO:0007829|PDB:2BTM" FT HELIX 139..151 FT /evidence="ECO:0007829|PDB:2BTM" FT HELIX 156..159 FT /evidence="ECO:0007829|PDB:2BTM" FT STRAND 163..166 FT /evidence="ECO:0007829|PDB:2BTM" FT HELIX 169..171 FT /evidence="ECO:0007829|PDB:2BTM" FT TURN 172..174 FT /evidence="ECO:0007829|PDB:2BTM" FT HELIX 177..179 FT /evidence="ECO:0007829|PDB:2BTM" FT HELIX 180..198 FT /evidence="ECO:0007829|PDB:2BTM" FT HELIX 200..203 FT /evidence="ECO:0007829|PDB:2BTM" FT STRAND 206..213 FT /evidence="ECO:0007829|PDB:2BTM" FT TURN 216..218 FT /evidence="ECO:0007829|PDB:2BTM" FT HELIX 219..223 FT /evidence="ECO:0007829|PDB:2BTM" FT STRAND 230..234 FT /evidence="ECO:0007829|PDB:2BTM" FT HELIX 235..237 FT /evidence="ECO:0007829|PDB:2BTM" FT HELIX 240..248 FT /evidence="ECO:0007829|PDB:2BTM" SQ SEQUENCE 253 AA; 27206 MW; 6532B5235362946C CRC64; MRKPIIAGNW KMHKTLAEAV QFVEDVKGHV PPADEVISVV CAPFLFLDRL VQAADGTDLK IGAQTMHFAD QGAYTGEVSP VMLKDLGVTY VILGHSERRQ MFAETDETVN KKVLAAFTRG LIPIICCGES LEEREAGQTN AVVASQVEKA LAGLTPEQVK QAVIAYEPIW AIGTGKSSTP EDANSVCGHI RSVVSRLFGP EAAEAIRIQY GGSVKPDNIR DFLAQQQIDG PLVGGASLEP ASFLQLVEAG RHE //