TPIS_LEPIN
ID TPIS_LEPIN Reviewed; 250 AA.
AC Q8F5I5;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=LA_1696;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=189518;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601;
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
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; AE010300; AAN48895.1; -; Genomic_DNA.
DR RefSeq; NP_711877.1; NC_004342.2.
DR RefSeq; WP_001232577.1; NC_004342.2.
DR PDB; 4X22; X-ray; 2.08 A; A=1-250.
DR PDB; 4YMZ; X-ray; 1.87 A; A/B=2-250.
DR PDBsum; 4X22; -.
DR PDBsum; 4YMZ; -.
DR AlphaFoldDB; Q8F5I5; -.
DR SMR; Q8F5I5; -.
DR STRING; 189518.LA_1696; -.
DR EnsemblBacteria; AAN48895; AAN48895; LA_1696.
DR KEGG; lil:LA_1696; -.
DR PATRIC; fig|189518.3.peg.1689; -.
DR HOGENOM; CLU_024251_2_3_12; -.
DR InParanoid; Q8F5I5; -.
DR OMA; QEVCGAI; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001408; Chromosome I.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004807; F:triose-phosphate isomerase activity; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0019563; P:glycerol catabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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..250
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090237"
FT ACT_SITE 96
FT /note="Electrophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT ACT_SITE 168
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 174
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 237..238
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:4YMZ"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:4X22"
FT HELIX 16..33
FT /evidence="ECO:0007829|PDB:4YMZ"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:4YMZ"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:4YMZ"
FT HELIX 48..55
FT /evidence="ECO:0007829|PDB:4YMZ"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:4YMZ"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:4YMZ"
FT HELIX 81..86
FT /evidence="ECO:0007829|PDB:4YMZ"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:4YMZ"
FT HELIX 97..102
FT /evidence="ECO:0007829|PDB:4YMZ"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:4YMZ"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:4YMZ"
FT HELIX 132..136
FT /evidence="ECO:0007829|PDB:4YMZ"
FT HELIX 140..151
FT /evidence="ECO:0007829|PDB:4YMZ"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:4X22"
FT HELIX 157..162
FT /evidence="ECO:0007829|PDB:4YMZ"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:4YMZ"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:4YMZ"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:4YMZ"
FT HELIX 181..196
FT /evidence="ECO:0007829|PDB:4YMZ"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:4YMZ"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:4YMZ"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:4YMZ"
FT HELIX 219..226
FT /evidence="ECO:0007829|PDB:4YMZ"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:4YMZ"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:4YMZ"
FT HELIX 243..247
FT /evidence="ECO:0007829|PDB:4YMZ"
SQ SEQUENCE 250 AA; 27309 MW; DB306147132BEE7D CRC64;
MRKTIIAGNW KMNLSLKEAV FLAHSIREKI PSISKDKVSM VFPSTLHLEN VSKILEGSSV
IVGAQNCYHS GLAAFTGETS PDQLKEIGVK VVMVGHSERR QFLGESNFFC NDKIRFLLKN
EFTVLYCVGE TLSERESGKT LEVLSSQIRE GLKGIDSVFF SNLILAYEPV WAIGTGKVAT
PSQAQEVHSF IRKEISGLFV GASSISESIS ILYGGSVKPD NIQDLLKEKD IDGGLVGGAS
QKISSFAELF
