TPIS_THET8
ID TPIS_THET8 Reviewed; 250 AA.
AC Q5SJR1;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=TTHA0947;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), AND SUBUNIT.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of tt0473, putative triosephosphate isomerase from
RT Thermus thermophilus HB8.";
RL Submitted (MAR-2005) to the PDB data bank.
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 ECO:0000269|Ref.2}.
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; AP008226; BAD70770.1; -; Genomic_DNA.
DR RefSeq; WP_011228317.1; NC_006461.1.
DR RefSeq; YP_144213.1; NC_006461.1.
DR PDB; 1YYA; X-ray; 1.60 A; A/B=1-250.
DR PDBsum; 1YYA; -.
DR AlphaFoldDB; Q5SJR1; -.
DR SMR; Q5SJR1; -.
DR STRING; 300852.55772329; -.
DR PRIDE; Q5SJR1; -.
DR EnsemblBacteria; BAD70770; BAD70770; BAD70770.
DR GeneID; 3169211; -.
DR KEGG; ttj:TTHA0947; -.
DR PATRIC; fig|300852.9.peg.929; -.
DR eggNOG; COG0149; Bacteria.
DR HOGENOM; CLU_024251_2_1_0; -.
DR OMA; QEVCGAI; -.
DR PhylomeDB; Q5SJR1; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; Q5SJR1; -.
DR Proteomes; UP000000532; 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..250
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000307417"
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 212
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 233..234
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:1YYA"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:1YYA"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:1YYA"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1YYA"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:1YYA"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:1YYA"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:1YYA"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:1YYA"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:1YYA"
FT HELIX 95..100
FT /evidence="ECO:0007829|PDB:1YYA"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:1YYA"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:1YYA"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:1YYA"
FT HELIX 138..149
FT /evidence="ECO:0007829|PDB:1YYA"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:1YYA"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:1YYA"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:1YYA"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:1YYA"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:1YYA"
FT HELIX 179..197
FT /evidence="ECO:0007829|PDB:1YYA"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:1YYA"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:1YYA"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:1YYA"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:1YYA"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:1YYA"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:1YYA"
FT HELIX 239..249
FT /evidence="ECO:0007829|PDB:1YYA"
SQ SEQUENCE 250 AA; 27095 MW; 45BF047ACD02AD1A CRC64;
MRRVLVAGNW KMHKTPSEAR VWFAELKRLL PPLQSEAAVL PAFPILPVAK EVLAETQVGY
GAQDVSAHKE GAYTGEVSAR MLSDLGCRYA IVGHSERRRY HGETDALVAE KAKRLLEEGI
TPILCVGEPL EVREKGEAVP YTLRQLRGSL EGVEPPGPEA LVIAYEPVWA IGTGKNATPE
DAEAMHQAIR KALSERYGEA FASRVRILYG GSVNPKNFAD LLSMPNVDGG LVGGASLELE
SFLALLRIAG
