ID   TPIS_PROM9              Reviewed;         241 AA.
AC   Q31AR4;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
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};
GN   OrderedLocusNames=PMT9312_0971;
OS   Prochlorococcus marinus (strain MIT 9312).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9312;
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., Thiel J., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
RL   Submitted (JUL-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; CP000111; ABB50031.1; -; Genomic_DNA.
DR   RefSeq; WP_011376523.1; NC_007577.1.
DR   AlphaFoldDB; Q31AR4; -.
DR   SMR; Q31AR4; -.
DR   STRING; 74546.PMT9312_0971; -.
DR   EnsemblBacteria; ABB50031; ABB50031; PMT9312_0971.
DR   KEGG; pmi:PMT9312_0971; -.
DR   eggNOG; COG0149; Bacteria.
DR   HOGENOM; CLU_024251_2_3_3; -.
DR   OMA; QEVCGAI; -.
DR   OrthoDB; 1266295at2; -.
DR   UniPathway; UPA00109; UER00189.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000002715; 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..241
FT                   /note="Triosephosphate isomerase"
FT                   /id="PRO_0000307526"
FT   ACT_SITE        96
FT                   /note="Electrophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT   ACT_SITE        165
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         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT   BINDING         204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT   BINDING         225..226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
SQ   SEQUENCE   241 AA;  26808 MW;  97268284F836D4DF CRC64;
     MRKSVIAGNW KMHMTCAEAK SYLEEFIPLI KNIRDDRKVV IAPPFTAIST FSKHSDFDYL
     DISSQNIHWE DEGAFTAEIS PKMLIEHGVS YAIVGHSEPR KYFSESDEQI NKRAVFAQCS
     GLTPIVCVGE TLEQRERGEA DRVITRQVEQ GLENTDPSNL IVAYEPIWAI GTGKTCEAKD
     ANNICSLIRK LIGFDDVIIQ YGGSVKPNNI DEIMSMSDID GVLVGGASLD PNSFARIANY
     Q