ID   TPIS_CLOPA              Reviewed;          19 AA.
AC   P81348;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Triosephosphate isomerase;
DE            Short=TIM;
DE            EC=5.3.1.1;
DE   AltName: Full=CP 25;
DE   AltName: Full=Triose-phosphate isomerase;
DE   Flags: Fragment;
GN   Name=tpiA; Synonyms=tpi;
OS   Clostridium pasteurianum.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1501;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=ATCC 6013 / DSM 525 / NCIB 9486 / VKM B-1774 / W5;
RX   PubMed=9629918; DOI=10.1002/elps.1150190533;
RA   Flengsrud R., Skjeldal L.;
RT   "Two-dimensional gel electrophoresis separation and N-terminal sequence
RT   analysis of proteins from Clostridium pasteurianum W5.";
RL   Electrophoresis 19:802-806(1998).
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|PROSITE-ProRule:PRU10127};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|PROSITE-ProRule:PRU10127}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate from glycerone phosphate: step 1/1. {ECO:0000255|PROSITE-
CC       ProRule:PRU10127}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|PROSITE-ProRule:PRU10127}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU10127}.
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU10127}.
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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-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Gluconeogenesis; Glycolysis;
KW   Isomerase.
FT   CHAIN           1..>19
FT                   /note="Triosephosphate isomerase"
FT                   /id="PRO_0000090210"
FT   BINDING         9
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT   BINDING         11
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT   VARIANT         1
FT                   /note="M -> S"
FT   VARIANT         3
FT                   /note="T -> Y"
FT   NON_TER         19
SQ   SEQUENCE   19 AA;  2055 MW;  288C0350BAFB25AF CRC64;
     MITPIIAGNX KLVNTISEE