ID   TPIS_METS3              Reviewed;         222 AA.
AC   A5ULP6;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=Msm_0919;
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA   Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT   human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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; CP000678; ABQ87124.1; -; Genomic_DNA.
DR   RefSeq; WP_011954172.1; NC_009515.1.
DR   AlphaFoldDB; A5ULP6; -.
DR   SMR; A5ULP6; -.
DR   STRING; 420247.Msm_0919; -.
DR   EnsemblBacteria; ABQ87124; ABQ87124; Msm_0919.
DR   GeneID; 5217483; -.
DR   KEGG; msi:Msm_0919; -.
DR   PATRIC; fig|420247.28.peg.915; -.
DR   eggNOG; arCOG01087; Archaea.
DR   HOGENOM; CLU_104921_0_0_2; -.
DR   OMA; IPVYAQH; -.
DR   UniPathway; UPA00109; UER00189.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001992; 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   3: Inferred from homology;
KW   Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase.
FT   CHAIN           1..222
FT                   /note="Triosephosphate isomerase"
FT                   /id="PRO_0000307604"
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   BINDING         202..203
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
SQ   SEQUENCE   222 AA;  23306 MW;  E67FFEF085D3C74B CRC64;
     MNTPIVILNY KTYLESSGEN ALELARALKS ASEESGITMV AAPQAADIYR IQDQISLPIF
     AQHIDPITPG GHTGSNLIET LIEAGISGSL INHSENRMKL ADIDEVIQLC KQNDIESCVC
     TNNIATSKAI ATFSPDAVAV EPPELIGTGI PVSQAQPEVV EDSVKGVKSI NKKIKVLCGA
     GISTGDDMKA AMDLGADGVL LASGIVKAKN PKEALLDLVS KL