ID TPIS_MORMI Reviewed; 256 AA. AC P50921; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 02-SEP-2026, entry version 120. DE RecName: Full=Triosephosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:9442062}; DE Short=TIM {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:9442062}; DE Short=TPI {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:9442062}; DE EC=5.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000269|PubMed:9442062}; DE AltName: Full=Triose-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:9442062}; GN Name=tpiA {ECO:0000255|HAMAP-Rule:MF_00147, GN ECO:0000303|PubMed:9442062}; Synonyms=tim, tpi; OS Moritella marina (Vibrio marinus). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Alteromonadales; Moritellaceae; Moritella. OX NCBI_TaxID=90736; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN RP COMPLEX WITH SUBSTRATE ANALOG, FUNCTION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ALA-238, AND SUBUNIT. RC STRAIN=ATCC 15382; RX PubMed=9442062; DOI=10.1074/jbc.273.4.2199; RA Alvarez M., Zeelen J.P., Mainfroid V., Rentier-Delrue F., Martial J.A., RA Wyns L., Wierenga R.K., Maes D.; RT "Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio RT marinus. Kinetic and structural properties."; RL J. Biol. Chem. 273:2199-2206(1998). 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:9442062}. 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 ECO:0000269|PubMed:9442062}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.9 mM for D-glyceraldehyde 3-phosphate (at pH 7.6 and 10 degrees CC Celsius) {ECO:0000269|PubMed:9442062}; CC Note=kcat is 420000 min(-1) for isomerase activity with CC D-glyceraldehyde 3-phosphate as substrate (at pH 7.6 and 10 degrees CC Celsius). {ECO:0000269|PubMed:9442062}; CC Temperature dependence: CC Optimum temperature is 15 degrees Celsius. CC {ECO:0000269|PubMed:9442062}; 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:9442062}. 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; U48935; AAA88910.1; -; Genomic_DNA. DR PDB; 1AW1; X-ray; 2.70 A; A/B/D/E/G/H/J/K=1-256. DR PDB; 1AW2; X-ray; 2.65 A; A/B/D/E/G/H/J/K=1-256. DR AlphaFoldDB; P50921; -. DR MDposit; P50921; -. DR MDRepo; P50921; -. DR SMR; P50921; -. DR DrugBank; DB02726; 2-Phosphoglycolic Acid. DR BRENDA; 5.3.1.1; 6633. DR UniPathway; UPA00109; UER00189. DR UniPathway; UPA00138; -. DR EvolutionaryTrace; P50921; -. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004807; F:triose-phosphate isomerase activity; EXP:UniProtKB. 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:000020; 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; 1AW1; -. DR PDBsum; 1AW2; -. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase. FT CHAIN 1..256 FT /note="Triosephosphate isomerase" FT /id="PRO_0000090314" FT ACT_SITE 97 FT /note="Electrophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147, FT ECO:0000305|PubMed:9442062" FT ACT_SITE 169 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 ECO:0000269|PubMed:9442062" FT BINDING 175 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147, FT ECO:0000269|PubMed:9442062" FT BINDING 214 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147, FT ECO:0000269|PubMed:9442062" FT BINDING 235..236 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147, FT ECO:0000269|PubMed:9442062" FT MUTAGEN 238 FT /note="A->S: Reduces catalytic efficiency and affinity, but FT increases thermal stability." FT /evidence="ECO:0000269|PubMed:9442062" FT STRAND 5..9 FT /evidence="ECO:0007829|PDB:1AW2" FT HELIX 16..29 FT /evidence="ECO:0007829|PDB:1AW2" FT TURN 30..32 FT /evidence="ECO:0007829|PDB:1AW2" FT STRAND 35..41 FT /evidence="ECO:0007829|PDB:1AW2" FT HELIX 44..46 FT /evidence="ECO:0007829|PDB:1AW2" FT HELIX 47..57 FT /evidence="ECO:0007829|PDB:1AW2" FT STRAND 62..66 FT /evidence="ECO:0007829|PDB:1AW2" FT STRAND 72..75 FT /evidence="ECO:0007829|PDB:1AW2" FT HELIX 82..88 FT /evidence="ECO:0007829|PDB:1AW2" FT STRAND 92..96 FT /evidence="ECO:0007829|PDB:1AW2" FT HELIX 98..103 FT /evidence="ECO:0007829|PDB:1AW2" FT HELIX 108..121 FT /evidence="ECO:0007829|PDB:1AW2" FT STRAND 124..129 FT /evidence="ECO:0007829|PDB:1AW2" FT HELIX 133..137 FT /evidence="ECO:0007829|PDB:1AW2" FT HELIX 141..156 FT /evidence="ECO:0007829|PDB:1AW2" FT HELIX 158..161 FT /evidence="ECO:0007829|PDB:1AW2" FT STRAND 165..168 FT /evidence="ECO:0007829|PDB:1AW2" FT TURN 171..175 FT /evidence="ECO:0007829|PDB:1AW2" FT HELIX 179..181 FT /evidence="ECO:0007829|PDB:1AW1" FT HELIX 182..197 FT /evidence="ECO:0007829|PDB:1AW2" FT HELIX 201..206 FT /evidence="ECO:0007829|PDB:1AW2" FT STRAND 208..211 FT /evidence="ECO:0007829|PDB:1AW2" FT TURN 217..219 FT /evidence="ECO:0007829|PDB:1AW2" FT HELIX 220..223 FT /evidence="ECO:0007829|PDB:1AW2" FT STRAND 231..235 FT /evidence="ECO:0007829|PDB:1AW2" FT HELIX 236..239 FT /evidence="ECO:0007829|PDB:1AW2" FT HELIX 241..254 FT /evidence="ECO:0007829|PDB:1AW2" SQ SEQUENCE 256 AA; 26740 MW; 5CC4BB8CFF27070A CRC64; MRHPVVMGNW KLNGSKEMVV DLLNGLNAEL EGVTGVDVAV APPALFVDLA ERTLTEAGSA IILGAQNTDL NNSGAFTGDM SPAMLKEFGA THIIIGHSER REYHAESDEF VAKKFAFLKE NGLTPVLCIG ESDAQNEAGE TMAVCARQLD AVINTQGVEA LEGAIIAYEP IWAIGTGKAA TAEDAQRIHA QIRAHIAEKS EAVAKNVVIQ YGGSVKPENA AAYFAQPDID GALVGGAALD AKSFAAIAKA AAEAKA //