ID   TPIS_CHLL3              Reviewed;         250 AA.
AC   Q3B2V8;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=Plut_1464;
OS   Chlorobium luteolum (strain DSM 273 / BCRC 81028 / 2530) (Pelodictyon
OS   luteolum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Pelodictyon.
OX   NCBI_TaxID=319225;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 273 / BCRC 81028 / 2530;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Pelodictyon luteolum DSM 273.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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: Homodimer. {ECO:0000255|HAMAP-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; CP000096; ABB24323.1; -; Genomic_DNA.
DR   RefSeq; WP_011358195.1; NC_007512.1.
DR   AlphaFoldDB; Q3B2V8; -.
DR   SMR; Q3B2V8; -.
DR   STRING; 319225.Plut_1464; -.
DR   EnsemblBacteria; ABB24323; ABB24323; Plut_1464.
DR   KEGG; plt:Plut_1464; -.
DR   eggNOG; COG0149; Bacteria.
DR   HOGENOM; CLU_024251_2_3_10; -.
DR   OMA; QEVCGAI; -.
DR   OrthoDB; 1266295at2; -.
DR   UniPathway; UPA00109; UER00189.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000002709; 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_B; TIM_B; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR035990; TIM_sf.
DR   InterPro; IPR022896; TrioseP_Isoase_bac/euk.
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   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..250
FT                   /note="Triosephosphate isomerase"
FT                   /id="PRO_0000307522"
FT   ACT_SITE        96
FT                   /note="Electrophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT   ACT_SITE        166
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         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT   BINDING         212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT   BINDING         233..234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
SQ   SEQUENCE   250 AA;  26051 MW;  58BD05A57B34712D CRC64;
     MRRKIVVGNW KMNKTVAEST ALATAVIAAL GDGCSACEAG IAPTYPALDA VGRALEGSGI
     ALVAQNCHYE DDGAYTGEVS TGMLKAVGCS YVIIGHSERR QYFGETDETV NLRIKKVLAS
     GMKVILCVGE TLAEREEGVT GTVVSRQVTE GLKGVADITD LVIAYEPVWA IGTGKTASSD
     QAQEVHRLIR DTVKGMYGAE VSEAVRIQYG GSVKASNAEE LFAMPDIDGG LIGGASLNAA
     DFAAIVKAGC