TPIS_MORMI
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 03-AUG-2022, entry version 109.
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, ECO:0000303|PubMed:9442062};
GN Synonyms=tim, tpi;
OS Moritella marina (Vibrio marinus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC 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 D-
CC 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}.
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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 PDBsum; 1AW1; -.
DR PDBsum; 1AW2; -.
DR AlphaFoldDB; 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: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 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..87
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..120
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 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
