TPIS_THETK
ID TPIS_THETK Reviewed; 226 AA.
AC Q8NKN9; G4RNL7;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, 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}; Synonyms=tpi;
GN OrderedLocusNames=TTX_0494;
OS Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435
OS / Kra 1).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermoproteus.
OX NCBI_TaxID=768679;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1;
RA Schramm A.;
RL Thesis (1998), Universitaet-GH Essen, Germany.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1;
RA Tjaden B.;
RT "Regulation of the carbohydrate metabolism of the hyperthermophilic
RT crenarchaeote Thermoproteus tenax.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1;
RX PubMed=22003381; DOI=10.1371/journal.pone.0024222;
RA Siebers B., Zaparty M., Raddatz G., Tjaden B., Albers S.V., Bell S.D.,
RA Blombach F., Kletzin A., Kyrpides N., Lanz C., Plagens A., Rampp M.,
RA Rosinus A., von Jan M., Makarova K.S., Klenk H.P., Schuster S.C.,
RA Hensel R.;
RT "The complete genome sequence of Thermoproteus tenax: a physiologically
RT versatile member of the Crenarchaeota.";
RL PLoS ONE 6:E24222-E24222(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, AND
RP SUBUNIT.
RX PubMed=15342242; DOI=10.1016/j.jmb.2004.07.067;
RA Walden H., Taylor G.L., Lorentzen E., Pohl E., Lilie H., Schramm A.,
RA Knura T., Stubbe K., Tjaden B., Hensel R.;
RT "Structure and function of a regulated archaeal triosephosphate isomerase
RT adapted to high temperature.";
RL J. Mol. Biol. 342:861-875(2004).
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, ECO:0000269|PubMed:15342242}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00147,
CC ECO:0000305}.
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00147}.
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DR EMBL; AJ012066; CAB66162.1; -; Genomic_DNA.
DR EMBL; AJ515539; CAD56500.1; -; Genomic_DNA.
DR EMBL; FN869859; CCC81161.1; -; Genomic_DNA.
DR RefSeq; WP_014126418.1; NC_016070.1.
DR PDB; 1W0M; X-ray; 2.50 A; A/B/C/D/E/F/G/H=1-226.
DR PDBsum; 1W0M; -.
DR AlphaFoldDB; Q8NKN9; -.
DR SMR; Q8NKN9; -.
DR STRING; 768679.TTX_0494; -.
DR EnsemblBacteria; CCC81161; CCC81161; TTX_0494.
DR GeneID; 11263496; -.
DR KEGG; ttn:TTX_0494; -.
DR PATRIC; fig|768679.9.peg.509; -.
DR eggNOG; arCOG01087; Archaea.
DR HOGENOM; CLU_104921_0_0_2; -.
DR OMA; IPVYAQH; -.
DR OrthoDB; 60670at2157; -.
DR BRENDA; 5.3.1.1; 6329.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; Q8NKN9; -.
DR Proteomes; UP000002654; 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 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..226
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090349"
FT ACT_SITE 93
FT /note="Electrophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT ACT_SITE 141
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 146
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147,
FT ECO:0000269|PubMed:15342242"
FT BINDING 202..203
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147,
FT ECO:0000269|PubMed:15342242"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:1W0M"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:1W0M"
FT HELIX 19..35
FT /evidence="ECO:0007829|PDB:1W0M"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:1W0M"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:1W0M"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:1W0M"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:1W0M"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:1W0M"
FT HELIX 78..84
FT /evidence="ECO:0007829|PDB:1W0M"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:1W0M"
FT HELIX 100..112
FT /evidence="ECO:0007829|PDB:1W0M"
FT STRAND 116..123
FT /evidence="ECO:0007829|PDB:1W0M"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:1W0M"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:1W0M"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1W0M"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:1W0M"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:1W0M"
FT HELIX 157..170
FT /evidence="ECO:0007829|PDB:1W0M"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:1W0M"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:1W0M"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:1W0M"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:1W0M"
FT HELIX 211..224
FT /evidence="ECO:0007829|PDB:1W0M"
SQ SEQUENCE 226 AA; 23283 MW; 53BE6A0A5F492857 CRC64;
MRLPILIINF KAYGEAAGKR AVELAKAAER AARELGVNIV VAPNHLELGL VSQSVDIPVY
AQGADVEAGG AHTAHVSLEN IKEAGGSGVI LNHSEAPLKL NDLARLVAKA KSLGLDVVVC
APDPRTSLAA AALGPHAVAV EPPELIGTGR AVSRYKPEAI VETVGLVSRH FPEVSVITGA
GIESGDDVAA ALRLGTRGVL LASAAVKAKD PYAKIVELAK PLSELR
