TPIS_ENTHI
ID TPIS_ENTHI Reviewed; 261 AA.
AC O02611;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Triosephosphate isomerase;
DE Short=TIM;
DE EC=5.3.1.1;
DE AltName: Full=Triose-phosphate isomerase;
GN Name=TPI;
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RX PubMed=9249046; DOI=10.1111/j.1432-1033.1997.00348.x;
RA Landa A., Rojo-Dominguez A., Jimenez L., Fernandez-Velasco D.A.;
RT "Sequencing, expression and properties of triosephosphate isomerase from
RT Entamoeba histolytica.";
RL Eur. J. Biochem. 247:348-355(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), SEQUENCE REVISION TO 261, AND
RP HOMODIMERIZATION.
RX PubMed=12270704; DOI=10.1016/s0022-2836(02)00809-4;
RA Rodriguez-Romero A., Hernandez-Santoyo A., del Pozo Yauner L.,
RA Kornhauser A., Fernandez-Velasco D.A.;
RT "Structure and inactivation of triosephosphate isomerase from Entamoeba
RT histolytica.";
RL J. Mol. Biol. 322:669-675(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.
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000305}.
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DR EMBL; Y13387; CAA73817.1; -; mRNA.
DR PDB; 1M6J; X-ray; 1.50 A; A/B=1-261.
DR PDBsum; 1M6J; -.
DR AlphaFoldDB; O02611; -.
DR SMR; O02611; -.
DR STRING; 5759.rna_EHI_056480-1; -.
DR VEuPathDB; AmoebaDB:EHI5A_015860; -.
DR VEuPathDB; AmoebaDB:EHI7A_083420; -.
DR VEuPathDB; AmoebaDB:EHI8A_145350; -.
DR VEuPathDB; AmoebaDB:EHI_056480; -.
DR VEuPathDB; AmoebaDB:KM1_061580; -.
DR eggNOG; KOG1643; Eukaryota.
DR BRENDA; 5.3.1.1; 2080.
DR SABIO-RK; O02611; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; O02611; -.
DR GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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; Gluconeogenesis; Glycolysis; Isomerase.
FT CHAIN 1..261
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090133"
FT ACT_SITE 102
FT /note="Electrophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 13
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 261
FT /note="L -> F (in Ref. 1; CAA73817)"
FT /evidence="ECO:0000305"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:1M6J"
FT HELIX 18..31
FT /evidence="ECO:0007829|PDB:1M6J"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:1M6J"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:1M6J"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1M6J"
FT HELIX 51..59
FT /evidence="ECO:0007829|PDB:1M6J"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1M6J"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:1M6J"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:1M6J"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:1M6J"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:1M6J"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:1M6J"
FT HELIX 113..126
FT /evidence="ECO:0007829|PDB:1M6J"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:1M6J"
FT HELIX 138..142
FT /evidence="ECO:0007829|PDB:1M6J"
FT HELIX 146..160
FT /evidence="ECO:0007829|PDB:1M6J"
FT HELIX 164..168
FT /evidence="ECO:0007829|PDB:1M6J"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:1M6J"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:1M6J"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:1M6J"
FT HELIX 187..204
FT /evidence="ECO:0007829|PDB:1M6J"
FT HELIX 207..212
FT /evidence="ECO:0007829|PDB:1M6J"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:1M6J"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:1M6J"
FT HELIX 226..230
FT /evidence="ECO:0007829|PDB:1M6J"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:1M6J"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:1M6J"
FT HELIX 247..254
FT /evidence="ECO:0007829|PDB:1M6J"
FT HELIX 255..259
FT /evidence="ECO:0007829|PDB:1M6J"
SQ SEQUENCE 261 AA; 27935 MW; 07CC091A400EFC6B CRC64;
MGAGKFVVGG NWKCNGTLAS IETLTKGVAA SVDAELAKKV EVIVGVPFIY IPKVQQILAG
EANGANILVS AENAWTKSGA YTGEVHVGML VDCQVPYVIL GHSERRQIFH ESNEQVAEKV
KVAIDAGLKV IACIGETEAQ RIANQTEEVV AAQLKAINNA ISKEAWKNII LAYEPVWAIG
TGKTATPDQA QEVHQYIRKW MTENISKEVA EATRIQYGGS VNPANCNELA KKADIDGFLV
GGASLDAAKF KTIINSVSEK L
