TPI1_GIAIN
ID TPI1_GIAIN Reviewed; 257 AA.
AC P36186;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Triosephosphate isomerase;
DE Short=TIM;
DE EC=5.3.1.1 {ECO:0000255|PROSITE-ProRule:PRU10127};
DE AltName: Full=Methylglyoxal synthase {ECO:0000250|UniProtKB:P00939};
DE EC=4.2.3.3 {ECO:0000250|UniProtKB:P00939};
DE AltName: Full=Triose-phosphate isomerase;
OS Giardia intestinalis (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=5741;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 30957 / WB;
RX PubMed=8299763; DOI=10.1006/expr.1994.1008;
RA Mowatt M.R., Weinbach E.C., Howard T.C., Nash T.E.;
RT "Complementation of an Escherichia coli glycolysis mutant by Giardia
RT lamblia triosephosphate isomerase.";
RL Exp. Parasitol. 78:85-92(1994).
CC -!- FUNCTION: Triosephosphate isomerase is an extremely efficient metabolic
CC enzyme that catalyzes the interconversion between dihydroxyacetone
CC phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis
CC and gluconeogenesis. {ECO:0000250|UniProtKB:P00939}.
CC -!- FUNCTION: It is also responsible for the non-negligible production of
CC methylglyoxal a reactive cytotoxic side-product that modifies and can
CC alter proteins, DNA and lipids. {ECO:0000250|UniProtKB:P00939}.
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|PROSITE-ProRule:PRU10127};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dihydroxyacetone phosphate = methylglyoxal + phosphate;
CC Xref=Rhea:RHEA:17937, ChEBI:CHEBI:17158, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57642; EC=4.2.3.3;
CC Evidence={ECO:0000250|UniProtKB:P00939};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|PROSITE-ProRule:PRU10127}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate from glycerone phosphate: step 1/1. {ECO:0000255|PROSITE-
CC ProRule:PRU10127}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|PROSITE-ProRule:PRU10127}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU10127}.
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000305}.
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DR EMBL; L02120; AAA18203.1; -; Unassigned_DNA.
DR RefSeq; XP_001706830.1; XM_001706778.1.
DR PDB; 2DP3; X-ray; 2.10 A; A=1-257.
DR PDB; 3PF3; X-ray; 2.10 A; A=1-257.
DR PDB; 4BI5; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-255.
DR PDB; 4BI6; X-ray; 1.45 A; A=1-257.
DR PDB; 4BI7; X-ray; 1.60 A; A=1-257.
DR PDBsum; 2DP3; -.
DR PDBsum; 3PF3; -.
DR PDBsum; 4BI5; -.
DR PDBsum; 4BI6; -.
DR PDBsum; 4BI7; -.
DR AlphaFoldDB; P36186; -.
DR SMR; P36186; -.
DR PRIDE; P36186; -.
DR GeneID; 5699725; -.
DR KEGG; gla:GL50803_0093938; -.
DR VEuPathDB; GiardiaDB:DHA2_93938; -.
DR VEuPathDB; GiardiaDB:GL50581_1369; -.
DR VEuPathDB; GiardiaDB:GL50803_0093938; -.
DR eggNOG; KOG1643; Eukaryota.
DR BRENDA; 5.3.1.1; 2401.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; P36186; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008929; F:methylglyoxal synthase activity; IEA:UniProtKB-EC.
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; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Lyase.
FT CHAIN 1..257
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090135"
FT ACT_SITE 96
FT /note="Electrophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT ACT_SITE 170
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT BINDING 13
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:4BI6"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:4BI6"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:4BI6"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:4BI6"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:4BI6"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:4BI6"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:4BI6"
FT HELIX 81..86
FT /evidence="ECO:0007829|PDB:4BI6"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:4BI6"
FT HELIX 97..101
FT /evidence="ECO:0007829|PDB:4BI6"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:4BI5"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:4BI6"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:4BI6"
FT HELIX 132..136
FT /evidence="ECO:0007829|PDB:4BI6"
FT HELIX 140..155
FT /evidence="ECO:0007829|PDB:4BI6"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:4BI6"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:4BI6"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:4BI6"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:4BI6"
FT HELIX 183..206
FT /evidence="ECO:0007829|PDB:4BI6"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:4BI6"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:4BI6"
FT HELIX 222..226
FT /evidence="ECO:0007829|PDB:4BI6"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:4BI6"
FT HELIX 238..241
FT /evidence="ECO:0007829|PDB:4BI6"
FT HELIX 244..255
FT /evidence="ECO:0007829|PDB:4BI6"
SQ SEQUENCE 257 AA; 27903 MW; 7CD7AC0AB1FB847A CRC64;
MPARRPFIGG NFKCNGSLDF IKSHVAAIAA HKIPDSVDVV IAPSAVHLST AIAANTSKQL
RIAAQNVYLE GNGAWTGETS VEMLQDMGLK HVIVGHSERR RIMGETDEQS AKKAKRALEK
GMTVIFCVGE TLDERKANRT MEVNIAQLEA LGKELGESKM LWKEVVIAYE PVWSIGTGVV
ATPEQAEEVH VGLRKWFAEK VCAEGAQHIR IIYGGSANGS NCEKLGQCPN IDGFLVGGAS
LKPEFMTMID ILTKTRT
