TPIS_FRATT
ID TPIS_FRATT Reviewed; 253 AA.
AC Q5NII7;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=FTT_0080;
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4;
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
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; AJ749949; CAG44713.1; -; Genomic_DNA.
DR RefSeq; WP_003019651.1; NZ_CP010290.1.
DR RefSeq; YP_169155.1; NC_006570.2.
DR PDB; 5UJW; X-ray; 2.65 A; A/B/C/D/E/F=1-253.
DR PDBsum; 5UJW; -.
DR AlphaFoldDB; Q5NII7; -.
DR SMR; Q5NII7; -.
DR STRING; 177416.FTT_0080; -.
DR DNASU; 3191461; -.
DR EnsemblBacteria; CAG44713; CAG44713; FTT_0080.
DR GeneID; 60806006; -.
DR KEGG; ftu:FTT_0080; -.
DR eggNOG; COG0149; Bacteria.
DR OMA; QEVCGAI; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001174; 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..253
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000307468"
FT ACT_SITE 93
FT /note="Electrophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 8..10
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 231..232
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:5UJW"
FT HELIX 15..25
FT /evidence="ECO:0007829|PDB:5UJW"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:5UJW"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:5UJW"
FT HELIX 46..51
FT /evidence="ECO:0007829|PDB:5UJW"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:5UJW"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:5UJW"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:5UJW"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:5UJW"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:5UJW"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:5UJW"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:5UJW"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:5UJW"
FT HELIX 129..133
FT /evidence="ECO:0007829|PDB:5UJW"
FT HELIX 137..143
FT /evidence="ECO:0007829|PDB:5UJW"
FT HELIX 146..151
FT /evidence="ECO:0007829|PDB:5UJW"
FT HELIX 154..159
FT /evidence="ECO:0007829|PDB:5UJW"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:5UJW"
FT TURN 167..172
FT /evidence="ECO:0007829|PDB:5UJW"
FT HELIX 178..193
FT /evidence="ECO:0007829|PDB:5UJW"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:5UJW"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:5UJW"
FT TURN 217..221
FT /evidence="ECO:0007829|PDB:5UJW"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:5UJW"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:5UJW"
FT HELIX 237..252
FT /evidence="ECO:0007829|PDB:5UJW"
SQ SEQUENCE 253 AA; 27656 MW; 77B677D0CE375737 CRC64;
MQKLIMGNWK MNGNSTSIKE LCSGISQVQY DTSRVAIAVF PSSVYVKEVI SQLPEKVGVG
LQNITFYDDG AYTGEISARM LEDIGCDYLL IGHSERRSLF AESDEDVFKK LNKIIDTTIT
PVVCIGESLD DRQSGKLKQV LATQLSLILE NLSVEQLAKV VIAYEPVWAI GTGVVASLEQ
IQETHQFIRS LLAKVDERLA KNIKIVYGGS LKAENAKDIL SLPDVDGGLI GGASLKAAEF
NEIINQANKI CTE
