ID   TPIS_SULDN              Reviewed;         240 AA.
AC   Q30PQ5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Triosephosphate isomerase {ECO:0000250|UniProtKB:P9WG43};
DE            Short=TIM {ECO:0000250|UniProtKB:P9WG43};
DE            Short=TPI {ECO:0000250|UniProtKB:P9WG43};
DE            EC=5.3.1.1 {ECO:0000250|UniProtKB:P9WG43};
DE   AltName: Full=Triose-phosphate isomerase {ECO:0000250|UniProtKB:P9WG43};
GN   Name=tpiA {ECO:0000250|UniProtKB:P9WG43}; OrderedLocusNames=Suden_1752;
OS   Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira
OS   denitrificans (strain ATCC 33889 / DSM 1251)).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Thiovulaceae; Sulfurimonas.
OX   NCBI_TaxID=326298;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33889 / DSM 1251;
RX   PubMed=18065616; DOI=10.1128/aem.01844-07;
RA   Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., Hemp J.,
RA   Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A.,
RA   Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., Diaz E.,
RA   Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., Long A.,
RA   Mobberley J.M., Pantry S.N., Pazder G., Peterson S., Quintanilla J.D.,
RA   Sprinkle R., Stephens J., Thomas P., Vaughn R., Weber M.J., Wooten L.L.;
RT   "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas
RT   denitrificans.";
RL   Appl. Environ. Microbiol. 74:1145-1156(2008).
CC   -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes stereospecifically
CC       the conversion of dihydroxyacetone phosphate (DHAP) to D-
CC       glyceraldehyde-3-phosphate (G3P). {ECO:0000250|UniProtKB:P9WG43}.
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:0000250|UniProtKB:P9WG43};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000250|UniProtKB:P9WG43}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate from glycerone phosphate: step 1/1.
CC       {ECO:0000250|UniProtKB:P9WG43}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WG43}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WG43}.
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000153; ABB45026.1; -; Genomic_DNA.
DR   RefSeq; WP_011373367.1; NC_007575.1.
DR   AlphaFoldDB; Q30PQ5; -.
DR   SMR; Q30PQ5; -.
DR   STRING; 326298.Suden_1752; -.
DR   EnsemblBacteria; ABB45026; ABB45026; Suden_1752.
DR   KEGG; tdn:Suden_1752; -.
DR   eggNOG; COG0149; Bacteria.
DR   HOGENOM; CLU_024251_2_3_7; -.
DR   OMA; QEVCGAI; -.
DR   OrthoDB; 1266295at2; -.
DR   UniPathway; UPA00109; UER00189.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000002714; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00311; TIM; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR035990; TIM_sf.
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   PROSITE; PS00171; TIM_1; 1.
DR   PROSITE; PS51440; TIM_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT   CHAIN           1..240
FT                   /note="Triosephosphate isomerase"
FT                   /id="PRO_1000009860"
FT   ACT_SITE        88
FT                   /note="Electrophile"
FT                   /evidence="ECO:0000250|UniProtKB:P9WG43"
FT   ACT_SITE        157
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WG43"
FT   BINDING         6..8
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WG43"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WG43"
FT   BINDING         193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WG43"
SQ   SEQUENCE   240 AA;  26649 MW;  EBE2AA50E07275A7 CRC64;
     MIIAANLKTN LTREKTAKYI KEVESFLNQH NISQEVFVFP AISNLISSSA NVVVGAQNAY
     PTQNGAFTGE IGNEQLEEFG IKTILIGHSE RRHVIGETQD SLIVKFNFYK NLGFKIIYCV
     GEPLHIREMG HEKMMEYISA QYVGIDAAYE NLIIAYEPVW AIGTGLTPTL EDIKMIHKEL
     KAKSTAPLLY GGSVKVTNVE EVLALDGVDG VLVGSAALYV EHFCTMCEYA QNIDKKNKKL