ID   TPIS_METBR              Reviewed;         226 AA.
AC   O74025;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Triosephosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:8925906};
DE            Short=TIM {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:8925906};
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;
OS   Methanobacterium bryantii.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX   NCBI_TaxID=2161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 862;
RA   Schramm A.;
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SUBUNIT.
RX   PubMed=8925906; DOI=10.1016/0014-5793(96)00249-9;
RA   Kohlhoff M., Dahm A., Hensel R.;
RT   "Tetrameric triosephosphate isomerase from hyperthermophilic Archaea.";
RL   FEBS Lett. 383:245-250(1996).
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:8925906}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Y11302; CAA72160.1; -; Genomic_DNA.
DR   AlphaFoldDB; O74025; -.
DR   SMR; O74025; -.
DR   PRIDE; O74025; -.
DR   BRENDA; 5.3.1.1; 3251.
DR   UniPathway; UPA00109; UER00189.
DR   UniPathway; UPA00138; -.
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   TIGRFAMs; TIGR00419; tim; 1.
DR   PROSITE; PS51440; TIM_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase.
FT   CHAIN           1..226
FT                   /note="Triosephosphate isomerase"
FT                   /id="PRO_0000090333"
FT   ACT_SITE        97
FT                   /note="Electrophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT   ACT_SITE        145
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT   BINDING         13..15
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT   BINDING         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT   BINDING         185
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT   BINDING         206..207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
SQ   SEQUENCE   226 AA;  23907 MW;  3A6B9DB84A54E546 CRC64;
     MNEIKETPIV ILNFKTYLES TGENALKLAK GSEMVAEETG VNIMVHPQYA DIYRIAHEVN
     IPVLAQHIDT IDAGGHTGSI LPECVKEAGA VGTLINHSER RVELFEIDAA IKKADSLGLS
     TVVCTNNIET SSAAATLNPD FVAIEPPELI GSGIPVSKPE PEIVEKTVES IHNINPEVRV
     LCGAGISTGD DLKAAIDLGS EGVLLASGII LADDPKKALL DLVSKI