TPIS_SCHMA
ID TPIS_SCHMA Reviewed; 253 AA.
AC P48501;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Triosephosphate isomerase;
DE Short=TIM;
DE EC=5.3.1.1;
DE AltName: Full=Triose-phosphate isomerase;
GN Name=TPI;
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1542681; DOI=10.1073/pnas.89.5.1842;
RA Shoemaker C., Gross A., Gebremichael A., Harn D.;
RT "cDNA cloning and functional expression of the Schistosoma mansoni
RT protective antigen triose-phosphate isomerase.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:1842-1846(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Puerto Rican;
RX PubMed=8341322; DOI=10.1016/0166-6851(93)90221-i;
RA Dos Reis M.G., Davis R.E., Singh H., Skelly P.J., Shoemaker C.B.;
RT "Characterization of the Schistosoma mansoni gene encoding the glycolytic
RT enzyme, triosephosphate isomerase.";
RL Mol. Biochem. Parasitol. 59:235-242(1993).
RN [3]
RP PROTEIN SEQUENCE OF 87-98; 182-192 AND 210-222.
RX PubMed=1729373;
RA Harn D.A., Gu W., Oligino L.D., Mitsuyama M., Gebremichael A., Richter D.;
RT "A protective monoclonal antibody specifically recognizes and alters the
RT catalytic activity of schistosome triose-phosphate isomerase.";
RL J. Immunol. 148:562-567(1992).
CC -!- FUNCTION: Antigen to the host M.1 monoclonal antibody.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000305}.
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DR EMBL; M83294; AAA29941.1; -; mRNA.
DR EMBL; L07286; AAA29919.1; -; Genomic_DNA.
DR EMBL; L06636; AAA29919.1; JOINED; Genomic_DNA.
DR EMBL; L07283; AAA29919.1; JOINED; Genomic_DNA.
DR EMBL; L07284; AAA29919.1; JOINED; Genomic_DNA.
DR EMBL; L07285; AAA29919.1; JOINED; Genomic_DNA.
DR PIR; A38233; A38233.
DR PDB; 6OOI; X-ray; 2.14 A; A/B/C/D/E/F/G/H=1-253.
DR PDBsum; 6OOI; -.
DR AlphaFoldDB; P48501; -.
DR SMR; P48501; -.
DR STRING; 6183.Smp_003990.1; -.
DR eggNOG; KOG1643; Eukaryota.
DR HOGENOM; CLU_024251_2_0_1; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000008854; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; Direct protein sequencing; Gluconeogenesis;
KW Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..253
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090140"
FT ACT_SITE 96
FT /note="Electrophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 14
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:6OOI"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:6OOI"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:6OOI"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:6OOI"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:6OOI"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:6OOI"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:6OOI"
FT HELIX 81..86
FT /evidence="ECO:0007829|PDB:6OOI"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:6OOI"
FT HELIX 97..101
FT /evidence="ECO:0007829|PDB:6OOI"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:6OOI"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:6OOI"
FT HELIX 132..136
FT /evidence="ECO:0007829|PDB:6OOI"
FT HELIX 140..152
FT /evidence="ECO:0007829|PDB:6OOI"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:6OOI"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:6OOI"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:6OOI"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:6OOI"
FT HELIX 182..199
FT /evidence="ECO:0007829|PDB:6OOI"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:6OOI"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:6OOI"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:6OOI"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:6OOI"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:6OOI"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:6OOI"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:6OOI"
FT TURN 248..251
FT /evidence="ECO:0007829|PDB:6OOI"
SQ SEQUENCE 253 AA; 28122 MW; 883459137F6C9847 CRC64;
MSGSRKFFVG GNWKMNGSRD DNDKLLKLLS EAHFDDNTEV LIAPPSVFLH EIRKSLKKEI
HVAAQNCYKV SKGAFTGEIS PAMIRDIGCD WVILGHSERR NIFGESDELI AEKVQHALAE
GLSVIACIGE TLSERESNKT EEVCVRQLKA IANKIKSADE WKRVVVAYEP VWAIGTGKVA
TPQQAQEVHN FLRKWFKTNA PNGVDEKIRI IYGGSVTAAN CKELAQQHDV DGFLVGGASL
KPEFTEICKA RQR
