TPIS_STRMK
ID TPIS_STRMK Reviewed; 251 AA.
AC B2FNY1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Triosephosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147};
DE Short=TIM {ECO:0000255|HAMAP-Rule:MF_00147};
DE Short=TPI {ECO:0000255|HAMAP-Rule:MF_00147};
DE EC=5.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00147};
DE AltName: Full=Triose-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147};
GN Name=tpiA {ECO:0000255|HAMAP-Rule:MF_00147}; OrderedLocusNames=Smlt3407;
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a;
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(2008).
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 -!- 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 -!- 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 -!- 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; AM743169; CAQ46835.1; -; Genomic_DNA.
DR RefSeq; WP_005410466.1; NC_010943.1.
DR PDB; 6W4U; X-ray; 1.70 A; A/B=1-251.
DR PDBsum; 6W4U; -.
DR AlphaFoldDB; B2FNY1; -.
DR SMR; B2FNY1; -.
DR STRING; 522373.Smlt3407; -.
DR EnsemblBacteria; CAQ46835; CAQ46835; Smlt3407.
DR GeneID; 61466901; -.
DR KEGG; sml:Smlt3407; -.
DR eggNOG; COG0149; Bacteria.
DR HOGENOM; CLU_024251_2_1_6; -.
DR OMA; QEVCGAI; -.
DR OrthoDB; 1266295at2; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000008840; Chromosome.
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; Gluconeogenesis; Glycolysis; Isomerase;
KW Reference proteome.
FT CHAIN 1..251
FT /note="Triosephosphate isomerase"
FT /id="PRO_1000096537"
FT ACT_SITE 94
FT /note="Electrophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 9..11
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 232..233
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:6W4U"
FT HELIX 16..28
FT /evidence="ECO:0007829|PDB:6W4U"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:6W4U"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:6W4U"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:6W4U"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:6W4U"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:6W4U"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:6W4U"
FT HELIX 95..100
FT /evidence="ECO:0007829|PDB:6W4U"
FT HELIX 105..118
FT /evidence="ECO:0007829|PDB:6W4U"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:6W4U"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:6W4U"
FT HELIX 138..153
FT /evidence="ECO:0007829|PDB:6W4U"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:6W4U"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:6W4U"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:6W4U"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:6W4U"
FT HELIX 179..194
FT /evidence="ECO:0007829|PDB:6W4U"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:6W4U"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:6W4U"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:6W4U"
FT HELIX 217..221
FT /evidence="ECO:0007829|PDB:6W4U"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:6W4U"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:6W4U"
FT HELIX 238..250
FT /evidence="ECO:0007829|PDB:6W4U"
SQ SEQUENCE 251 AA; 26192 MW; 4646050F7F219820 CRC64;
MRRKIVAGNW KLHGSRQFAN ELLGQVAAGL PLEGVDVVIL PPLPYLGELV EDFGETGLAF
GAQDVSSNEK GAYTGEVCAA MLVEVGARYG LVGHSERRQY HHESSELVAR KFAAAQHAGL
VPVLCVGETL EQREAGQTEA VIASQLAPVL ELVGAAGFAQ AVVAYEPVWA IGTGRTATKE
QAQQVHAFIR GEVARIDARI ADSLPIVYGG SVKPDNAGEL FAQPDVDGGL VGGASLVAAD
FLAIARAAAA N
