TPIS_THEAC
ID TPIS_THEAC Reviewed; 216 AA.
AC Q9HLB6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=Ta0313;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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: Homotetramer; dimer of dimers. {ECO:0000255|HAMAP-
CC 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; AL445063; CAC11458.1; -; Genomic_DNA.
DR RefSeq; WP_010900742.1; NC_002578.1.
DR PDB; 5CSR; X-ray; 1.94 A; A/B/C/D=1-216.
DR PDB; 5CSS; X-ray; 2.17 A; A/B/C/D=1-216.
DR PDBsum; 5CSR; -.
DR PDBsum; 5CSS; -.
DR AlphaFoldDB; Q9HLB6; -.
DR SMR; Q9HLB6; -.
DR STRING; 273075.Ta0313; -.
DR EnsemblBacteria; CAC11458; CAC11458; CAC11458.
DR GeneID; 1455936; -.
DR KEGG; tac:Ta0313; -.
DR eggNOG; arCOG01087; Archaea.
DR HOGENOM; CLU_104921_0_0_2; -.
DR OMA; IPVYAQH; -.
DR OrthoDB; 60670at2157; -.
DR BRENDA; 5.3.1.1; 6324.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001024; 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_A; TIM_A; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035990; TIM_sf.
DR InterPro; IPR000652; Triosephosphate_isomerase.
DR InterPro; IPR022891; Triosephosphate_isomerase_arc.
DR PANTHER; PTHR21139; PTHR21139; 1.
DR Pfam; PF00121; TIM; 1.
DR SUPFAM; SSF51351; SSF51351; 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..216
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090348"
FT ACT_SITE 89
FT /note="Electrophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT ACT_SITE 137
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 7..9
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 196..197
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:5CSR"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:5CSR"
FT HELIX 17..25
FT /evidence="ECO:0007829|PDB:5CSR"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:5CSR"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:5CSR"
FT HELIX 44..50
FT /evidence="ECO:0007829|PDB:5CSR"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:5CSR"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:5CSR"
FT HELIX 74..80
FT /evidence="ECO:0007829|PDB:5CSR"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:5CSR"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:5CSR"
FT STRAND 112..119
FT /evidence="ECO:0007829|PDB:5CSR"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:5CSR"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:5CSR"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:5CSR"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:5CSR"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:5CSS"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:5CSR"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:5CSR"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:5CSR"
FT HELIX 179..187
FT /evidence="ECO:0007829|PDB:5CSR"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:5CSR"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:5CSR"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:5CSR"
FT HELIX 205..213
FT /evidence="ECO:0007829|PDB:5CSR"
SQ SEQUENCE 216 AA; 23848 MW; D3477E54F993EBAF CRC64;
MYTAIVNLKT YREATGANFT RFMEKFEPVQ GKFELIFSPS LLDLEKAAKC GKFRFFAQHV
DAEPYGAYTG HVPMDMMIDL GITGSILNHS ERRLPRDTII NTLKKASKLD FTIVLCVENA
EEAKYFREYE PDFIAYEPRD LIGGDVSVST AKPEIIEDIV KIYEGTGTSV LVGAGIKTGE
DVRRSIGLGA RGILVASGVV KSADPTKSLN SLIELK
