AC   MF_00147;
DC   Protein; auto
c?   <OC:Bacteria>
TR   HAMAP; MF_00147_B; -; 1; level=0
c?   <OC:Archaea>
TR   HAMAP; MF_00147_A; -; 1; level=0
XX
Names: TIM
XX
ID   TPIS
DE   RecName: Full=Triosephosphate isomerase;
DE            Short=TIM;
DE            Short=TPI;
DE            EC=5.3.1.1;
DE   AltName: Full=Triose-phosphate isomerase;
GN   Name=tpiA;
XX
CC   -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes stereospecifically
CC       the conversion of dihydroxyacetone phosphate (DHAP) to D-
CC       glyceraldehyde-3-phosphate (G3P).
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;
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate from glycerone phosphate: step 1/1.
case <OC:Archaea>
CC   -!- SUBUNIT: Homotetramer; dimer of dimers.
end case
case not <OC:Archaea>
CC   -!- SUBUNIT: Homodimer.
end case
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
XX
DR   Pfam; PF00121; TIM; 1; trigger=no
DR   NCBIfam; TIGR00419; Tim; 1; trigger=no
DR   PROSITE; PS00171; TIM_1; 1; trigger=no
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KW   Cytoplasm
KW   Isomerase
KW   Glycolysis
KW   Gluconeogenesis
case <FT:7>
KW   Phosphoprotein
end case
XX
GO   GO:0004807; F:triose-phosphate isomerase activity
GO   GO:0006094; P:gluconeogenesis
GO   GO:0006096; P:glycolytic process
GO   GO:0005737; C:cytoplasm
XX
FT   From: TPIS_MYCTU (P9WG43)
case <OC:Bacteria>
FT   BINDING         10..12
FT                   /ligand="substrate"
FT   Condition: N-x-K
FT   BINDING         239..240
FT                   /ligand="substrate"
FT   Condition: G-G
FT   ACT_SITE        100
FT                   /note="Electrophile"
FT   Condition: H
FT   ACT_SITE        172
FT                   /note="Proton acceptor"
FT   Condition: E
FT   BINDING         178
FT                   /ligand="substrate"
FT   Condition: G
FT   BINDING         218
FT                   /ligand="substrate"
FT   Condition: S
end case
FT   From: TPIS_BACSU (P27876)
case <OC:Bacillaceae>
FT   MOD_RES         213
FT                   /note="Phosphoserine"
FT   Condition: S
end case
FT   From: TPIS_PYRWO (P62003)
case <OC:Archaea>
FT   BINDING         12..14
FT                   /ligand="substrate"
FT   Condition: N-x-K
FT   BINDING         205..206
FT                   /ligand="substrate"
FT   Condition: A-S
FT   ACT_SITE        96
FT                   /note="Electrophile"
FT   Condition: H
FT   ACT_SITE        144
FT                   /note="Proton acceptor"
FT   Condition: E
FT   BINDING         149
FT                   /ligand="substrate"
FT   Condition: I
FT   BINDING         184
FT                   /ligand="substrate"
FT   Condition: G
end case
XX
case <OC:Bacteria>
Size: 223-293;
end case
case <OC:Archaea>
Size: 213-231;
end case
Related: None;
Template: P9WG43; P00943; P0A858; Q6GIL6; P50921; P56076; P62003; Q58923; O74025; Q8NKN9;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: MF_00145 (pgk)
 Cter: None
Duplicate: in BRUME, BRUSU, LISIN, LISMO, RHILO, RHIME
Plasmid: None
Comments: Probable wrong start in CHLTR
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# Revision 1.45 2023/06/01
//