TPIS_TRYBB
ID TPIS_TRYBB Reviewed; 250 AA.
AC P04789;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Triosephosphate isomerase, glycosomal;
DE Short=TIM;
DE Short=Triose-phosphate isomerase;
DE EC=5.3.1.1;
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3015595; DOI=10.1002/j.1460-2075.1986.tb04358.x;
RA Swinkels B.W., Gibson W.C., Osinga K.A., Kramer R., Veeneman G.H.,
RA van Boom J.H., Borst P.;
RT "Characterization of the gene for the microbody (glycosomal)
RT triosephosphate isomerase of Trypanosoma brucei.";
RL EMBO J. 5:1291-1298(1986).
RN [2]
RP PROTEIN SEQUENCE.
RX PubMed=3516224; DOI=10.1016/0167-4781(86)90044-8;
RA Borst P.;
RT "How proteins get into microbodies (peroxisomes, glyoxysomes,
RT glycosomes).";
RL Biochim. Biophys. Acta 866:179-203(1986).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND HOMODIMERIZATION.
RX PubMed=3430602; DOI=10.1016/0022-2836(87)90461-x;
RA Wierenga R.K., Kalk K.H., Hol W.G.J.;
RT "Structure determination of the glycosomal triosephosphate isomerase from
RT Trypanosoma brucei brucei at 2.4-A resolution.";
RL J. Mol. Biol. 198:109-121(1987).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS), AND HOMODIMERIZATION.
RX PubMed=1880808; DOI=10.1016/0022-2836(91)90368-g;
RA Wierenga R.K., Noble M.E.M., Vriend G., Nauche S., Hol W.G.J.;
RT "Refined 1.83 A structure of trypanosomal triosephosphate isomerase
RT crystallized in the presence of 2.4 M-ammonium sulphate. A comparison with
RT the structure of the trypanosomal triosephosphate isomerase-glycerol-3-
RT phosphate complex.";
RL J. Mol. Biol. 220:995-1015(1991).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
RX PubMed=2062828; DOI=10.1002/prot.340100106;
RA Noble M.E., Wierenga R.K., Lambeir A.-M., Opperdoes F.R., Thunnissen A.M.,
RA Kalk K.H., Groendijk H., Hol W.G.J.;
RT "The adaptability of the active site of trypanosomal triosephosphate
RT isomerase as observed in the crystal structures of three different
RT complexes.";
RL Proteins 10:50-69(1991).
RN [6]
RP COMPARISON OF X-RAY STRUCTURES.
RX PubMed=1569570; DOI=10.1016/0022-2836(92)90473-w;
RA Wierenga R.K., Noble M.E.M., Davenport R.C.;
RT "Comparison of the refined crystal structures of liganded and unliganded
RT chicken, yeast and trypanosomal triosephosphate isomerase.";
RL J. Mol. Biol. 224:1115-1126(1992).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND SEQUENCE REVISION TO 203.
RX PubMed=8436128; DOI=10.1111/j.1432-1033.1993.tb17599.x;
RA Borchert T.V., Pratt K., Zeelen J.P., Callens M., Noble M.E.M.,
RA Opperdoes F.R., Michels P.A.M., Wierenga R.K.;
RT "Overexpression of trypanosomal triosephosphate isomerase in Escherichia
RT coli and characterisation of a dimer-interface mutant.";
RL Eur. J. Biochem. 211:703-710(1993).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANTS IN COMPLEX WITH SUBSTRATE
RP ANALOGS.
RX PubMed=8591044; DOI=10.1016/s0969-2126(01)00202-7;
RA Borchert T.V., Kishan K.V., Zeelen J.P., Schliebs W., Thanki N.,
RA Abagyan R., Jaenicke R., Wierenga R.K.;
RT "Three new crystal structures of point mutation variants of monoTIM:
RT conformational flexibility of loop-1, loop-4 and loop-8.";
RL Structure 3:669-679(1995).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
RX PubMed=11997014; DOI=10.1016/s0014-5793(02)02639-x;
RA Kursula I., Partanen S., Lambeir A.-M., Wierenga R.K.;
RT "The importance of the conserved Arg191-Asp227 salt bridge of
RT triosephosphate isomerase for folding, stability, and catalysis.";
RL FEBS Lett. 518:39-42(2002).
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;
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate from glycerone phosphate: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11997014,
CC ECO:0000269|PubMed:2062828, ECO:0000269|PubMed:8591044}.
CC -!- SUBCELLULAR LOCATION: Glycosome.
CC -!- MISCELLANEOUS: The enzyme contains a high proportion of positively-
CC charged residues in beta-barrels V and VII (compared to the homologous
CC regions in other triose isomerase sequences). Since 2 clusters of
CC positive charges located at precise distances on the molecular surface
CC are common to 4 glycosomal enzymes, it has been speculated that this
CC might represent a signal for entry into glycosomes (PubMed:3015595).
CC {ECO:0000305|PubMed:3015595}.
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000305}.
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DR EMBL; X03921; CAA27559.1; -; Genomic_DNA.
DR PDB; 1AG1; X-ray; 2.36 A; O/T=1-250.
DR PDB; 1DKW; X-ray; 2.65 A; A/B=2-250.
DR PDB; 1IIG; X-ray; 2.60 A; A/B=1-250.
DR PDB; 1IIH; X-ray; 2.20 A; A/B=1-250.
DR PDB; 1KV5; X-ray; 1.65 A; A/B=1-250.
DR PDB; 1ML1; X-ray; 2.60 A; A/C/E/G/I/K=1-250.
DR PDB; 1MSS; X-ray; 2.40 A; A/B=1-250.
DR PDB; 1TPD; X-ray; 2.10 A; A/B=1-250.
DR PDB; 1TPE; X-ray; 2.10 A; A=1-250.
DR PDB; 1TPF; X-ray; 1.80 A; A/B=1-250.
DR PDB; 1TRD; X-ray; 2.50 A; A/B=1-250.
DR PDB; 1TRI; X-ray; 2.40 A; A=1-250.
DR PDB; 1TSI; X-ray; 2.84 A; A/B=1-250.
DR PDB; 1TTI; X-ray; 2.40 A; A=1-250.
DR PDB; 1TTJ; X-ray; 2.40 A; A=1-250.
DR PDB; 2J24; X-ray; 2.10 A; A/B=1-250.
DR PDB; 2J27; X-ray; 1.15 A; A/B=1-250.
DR PDB; 2V0T; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-250.
DR PDB; 2V2C; X-ray; 1.89 A; A=1-250.
DR PDB; 2V2D; X-ray; 2.30 A; A=1-250.
DR PDB; 2V2H; X-ray; 1.18 A; A/B/C=1-250.
DR PDB; 2V5L; X-ray; 2.40 A; A/B=1-250.
DR PDB; 2VEI; X-ray; 1.89 A; A/B/C=2-250.
DR PDB; 2VEK; X-ray; 1.60 A; A/B=2-250.
DR PDB; 2VEL; X-ray; 2.30 A; A/B=2-250.
DR PDB; 2VEM; X-ray; 2.20 A; A/B=2-250.
DR PDB; 2VEN; X-ray; 2.00 A; A/B=2-250.
DR PDB; 2WSQ; X-ray; 2.10 A; A/B/C/D=2-67, A/B/C/D=84-250.
DR PDB; 2WSR; X-ray; 1.65 A; A=2-67, A=84-250.
DR PDB; 2X16; X-ray; 2.13 A; A/B=2-250.
DR PDB; 2X1R; X-ray; 1.98 A; A/B=2-250.
DR PDB; 2X1S; X-ray; 1.93 A; A/B=2-250.
DR PDB; 2X1T; X-ray; 1.83 A; A/B=2-250.
DR PDB; 2X1U; X-ray; 1.84 A; A/B=2-250.
DR PDB; 2X2G; X-ray; 1.90 A; A/B=2-250.
DR PDB; 2Y6Z; X-ray; 2.60 A; A=1-250.
DR PDB; 2Y70; X-ray; 2.30 A; A/B/C/D=1-250.
DR PDB; 3Q37; X-ray; 1.65 A; A/B/C/D=2-35, A/B/C/D=92-119.
DR PDB; 3TIM; X-ray; 2.80 A; A/B=1-250.
DR PDB; 4JEQ; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L=1-250.
DR PDB; 4PC8; X-ray; 1.55 A; A=1-250.
DR PDB; 4PCF; X-ray; 2.71 A; A/B/C=1-250.
DR PDB; 4TIM; X-ray; 2.40 A; A/B=1-250.
DR PDB; 5I3F; X-ray; 1.72 A; A/B/C/D=1-250.
DR PDB; 5I3G; X-ray; 1.96 A; A/B/C/D=1-250.
DR PDB; 5I3H; X-ray; 2.25 A; A/B=1-250.
DR PDB; 5I3I; X-ray; 2.20 A; A/B/C/D=1-250.
DR PDB; 5I3J; X-ray; 1.80 A; A/B=1-250.
DR PDB; 5I3K; X-ray; 2.21 A; A/B/C/D=1-250.
DR PDB; 5TIM; X-ray; 1.83 A; A/B=1-250.
DR PDB; 6TIM; X-ray; 2.20 A; A/B=1-250.
DR PDBsum; 1AG1; -.
DR PDBsum; 1DKW; -.
DR PDBsum; 1IIG; -.
DR PDBsum; 1IIH; -.
DR PDBsum; 1KV5; -.
DR PDBsum; 1ML1; -.
DR PDBsum; 1MSS; -.
DR PDBsum; 1TPD; -.
DR PDBsum; 1TPE; -.
DR PDBsum; 1TPF; -.
DR PDBsum; 1TRD; -.
DR PDBsum; 1TRI; -.
DR PDBsum; 1TSI; -.
DR PDBsum; 1TTI; -.
DR PDBsum; 1TTJ; -.
DR PDBsum; 2J24; -.
DR PDBsum; 2J27; -.
DR PDBsum; 2V0T; -.
DR PDBsum; 2V2C; -.
DR PDBsum; 2V2D; -.
DR PDBsum; 2V2H; -.
DR PDBsum; 2V5L; -.
DR PDBsum; 2VEI; -.
DR PDBsum; 2VEK; -.
DR PDBsum; 2VEL; -.
DR PDBsum; 2VEM; -.
DR PDBsum; 2VEN; -.
DR PDBsum; 2WSQ; -.
DR PDBsum; 2WSR; -.
DR PDBsum; 2X16; -.
DR PDBsum; 2X1R; -.
DR PDBsum; 2X1S; -.
DR PDBsum; 2X1T; -.
DR PDBsum; 2X1U; -.
DR PDBsum; 2X2G; -.
DR PDBsum; 2Y6Z; -.
DR PDBsum; 2Y70; -.
DR PDBsum; 3Q37; -.
DR PDBsum; 3TIM; -.
DR PDBsum; 4JEQ; -.
DR PDBsum; 4PC8; -.
DR PDBsum; 4PCF; -.
DR PDBsum; 4TIM; -.
DR PDBsum; 5I3F; -.
DR PDBsum; 5I3G; -.
DR PDBsum; 5I3H; -.
DR PDBsum; 5I3I; -.
DR PDBsum; 5I3J; -.
DR PDBsum; 5I3K; -.
DR PDBsum; 5TIM; -.
DR PDBsum; 6TIM; -.
DR AlphaFoldDB; P04789; -.
DR SMR; P04789; -.
DR BindingDB; P04789; -.
DR PRIDE; P04789; -.
DR BRENDA; 5.3.1.1; 6519.
DR SABIO-RK; P04789; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; P04789; -.
DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR GO; GO:0020015; C:glycosome; IDA:GeneDB.
DR GO; GO:0004807; F:triose-phosphate isomerase activity; IDA:GeneDB.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR GO; GO:0006096; P:glycolytic process; IMP:GeneDB.
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; Direct protein sequencing; Gluconeogenesis; Glycolysis;
KW Glycosome; Isomerase; Peroxisome.
FT CHAIN 1..250
FT /note="Triosephosphate isomerase, glycosomal"
FT /id="PRO_0000090142"
FT ACT_SITE 95
FT /note="Electrophile"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT BINDING 11
FT /ligand="substrate"
FT BINDING 13
FT /ligand="substrate"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:2J27"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:1MSS"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:2J27"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:2J27"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:2J27"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:2J27"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:2J27"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2J27"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:2WSR"
FT HELIX 80..85
FT /evidence="ECO:0007829|PDB:2J27"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:2J27"
FT HELIX 96..101
FT /evidence="ECO:0007829|PDB:2J27"
FT HELIX 106..119
FT /evidence="ECO:0007829|PDB:2J27"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:2J27"
FT HELIX 131..135
FT /evidence="ECO:0007829|PDB:2J27"
FT HELIX 139..152
FT /evidence="ECO:0007829|PDB:2J27"
FT HELIX 156..161
FT /evidence="ECO:0007829|PDB:2J27"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:2J27"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:2J27"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:2V2H"
FT HELIX 180..197
FT /evidence="ECO:0007829|PDB:2J27"
FT HELIX 200..205
FT /evidence="ECO:0007829|PDB:2J27"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:2J27"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:2J27"
FT HELIX 219..223
FT /evidence="ECO:0007829|PDB:2J27"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:1TRD"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:2J27"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:2J27"
FT HELIX 242..247
FT /evidence="ECO:0007829|PDB:2J27"
SQ SEQUENCE 250 AA; 26835 MW; 189D7A00632040FE CRC64;
MSKPQPIAAA NWKCNGSQQS LSELIDLFNS TSINHDVQCV VASTFVHLAM TKERLSHPKF
VIAAQNAIAK SGAFTGEVSL PILKDFGVNW IVLGHSERRA YYGETNEIVA DKVAAAVASG
FMVIACIGET LQERESGRTA VVVLTQIAAI AKKLKKADWA KVVIAYEPVW AIGTGKVATP
QQAQEAHALI RSWVSSKIGA DVAGELRILY GGSVNGKNAR TLYQQRDVNG FLVGGASLKP
EFVDIIKATQ
