TPIS_PYRWO
ID TPIS_PYRWO Reviewed; 228 AA.
AC P62003; P95583;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Triosephosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:8925906};
DE Short=TIM {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:8925906};
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}; Synonyms=tpi;
OS Pyrococcus woesei.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=2262;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-29,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 49860 / DSM 3773 / JCM 8421 / Vul4;
RX PubMed=8925906; DOI=10.1016/0014-5793(96)00249-9;
RA Kohlhoff M., Dahm A., Hensel R.;
RT "Tetrameric triosephosphate isomerase from hyperthermophilic Archaea.";
RL FEBS Lett. 383:245-250(1996).
RN [2]
RP SEQUENCE REVISION TO 211-228.
RA Schramm A.;
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, AND
RP SUBUNIT.
RX PubMed=11243785; DOI=10.1006/jmbi.2000.4433;
RA Walden H., Bell G.S., Russell R.J., Siebers B., Hensel R., Taylor G.L.;
RT "Tiny TIM: a small, tetrameric, hyperthermostable triosephosphate
RT isomerase.";
RL J. Mol. Biol. 306:745-757(2001).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermostable. The formation of the dimer of dimers is important to
CC increase the thermostability. {ECO:0000269|PubMed:8925906};
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: Homotetramer; dimer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_00147, ECO:0000269|PubMed:11243785,
CC ECO:0000269|PubMed:8925906}.
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; Y09481; CAA70690.2; -; Genomic_DNA.
DR PIR; S66212; S66212.
DR PDB; 1HG3; X-ray; 2.70 A; A/B/C/D/E/F/G/H=1-225.
DR PDBsum; 1HG3; -.
DR AlphaFoldDB; P62003; -.
DR SMR; P62003; -.
DR BioCyc; MetaCyc:MON-11811; -.
DR BRENDA; 5.3.1.1; 5249.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; P62003; -.
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_A; TIM_A; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035990; TIM_sf.
DR InterPro; IPR000652; Triosephosphate_isomerase.
DR InterPro; IPR022891; Triosephosphate_isomerase_arc.
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; Direct protein sequencing; Gluconeogenesis;
KW Glycolysis; Isomerase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8925906"
FT CHAIN 2..228
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090344"
FT ACT_SITE 96
FT /note="Electrophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 12..14
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147,
FT ECO:0000269|PubMed:11243785"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147,
FT ECO:0000269|PubMed:11243785"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 205..206
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147,
FT ECO:0000269|PubMed:11243785"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:1HG3"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:1HG3"
FT HELIX 21..36
FT /evidence="ECO:0007829|PDB:1HG3"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:1HG3"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:1HG3"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:1HG3"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1HG3"
FT HELIX 81..86
FT /evidence="ECO:0007829|PDB:1HG3"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:1HG3"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1HG3"
FT HELIX 103..116
FT /evidence="ECO:0007829|PDB:1HG3"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:1HG3"
FT HELIX 127..134
FT /evidence="ECO:0007829|PDB:1HG3"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:1HG3"
FT TURN 146..151
FT /evidence="ECO:0007829|PDB:1HG3"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:1HG3"
FT HELIX 161..173
FT /evidence="ECO:0007829|PDB:1HG3"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:1HG3"
FT HELIX 188..196
FT /evidence="ECO:0007829|PDB:1HG3"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:1HG3"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:1HG3"
FT HELIX 214..223
FT /evidence="ECO:0007829|PDB:1HG3"
SQ SEQUENCE 228 AA; 24066 MW; 1F24C7A2D71BB6F2 CRC64;
MAKLKEPIIA INFKTYIEAT GKRALEIAKA AEKVYKETGV TIVVAPQLVD LRMIAESVEI
PVFAQHIDPI KPGSHTGHVL PEAVKEAGAV GTLLNHSENR MILADLEAAI RRAEEVGLMT
MVCSNNPAVS AAVAALNPDY VAVEPPELIG TGIPVSKAKP EVITNTVELV KKVNPEVKVL
CGAGISTGED VKKAIELGTV GVLLASGVTK AKDPEKAIWD LVSGIIKE
