TPIS_GEOSE
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 03-AUG-2022, entry version 125.
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; Firmicutes; Bacilli; Bacillales; Bacillaceae; 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}.
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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=2-252.
DR PDBsum; 1BTM; -.
DR PDBsum; 2BTM; -.
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: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; 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..118
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 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
