ID   Q1MGC2_RHIJ3            Unreviewed;       256 AA.
AC   Q1MGC2;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   02-SEP-2026, entry version 121.
DE   RecName: Full=Triosephosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013};
DE            Short=TIM {ECO:0000256|HAMAP-Rule:MF_00147};
DE            Short=TPI {ECO:0000256|HAMAP-Rule:MF_00147};
DE            EC=5.3.1.1 {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013};
DE   AltName: Full=Triose-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00147};
GN   Name=tpiA {ECO:0000256|HAMAP-Rule:MF_00147,
GN   ECO:0000313|EMBL:CAK08001.1};
GN   OrderedLocusNames=RL2513 {ECO:0000313|EMBL:CAK08001.1};
OS   Rhizobium johnstonii (strain DSM 114642 / LMG 32736 / 3841) (Rhizobium
OS   leguminosarum bv. viciae).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium;
OC   Rhizobium johnstonii.
OX   NCBI_TaxID=216596 {ECO:0000313|EMBL:CAK08001.1, ECO:0000313|Proteomes:UP000006575};
RN   [1] {ECO:0000313|EMBL:CAK08001.1, ECO:0000313|Proteomes:UP000006575}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 114642 / LMG 32736 / 3841
RC   {ECO:0000313|Proteomes:UP000006575};
RX   PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA   Young J.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA   Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA   East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach A.,
RA   Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT   components.";
RL   Genome Biol. 7:R34.1-R34.20(2006).
CC   -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes stereospecifically
CC       the conversion of dihydroxyacetone phosphate (DHAP) to D-
CC       glyceraldehyde-3-phosphate (G3P). {ECO:0000256|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:0000256|HAMAP-Rule:MF_00147,
CC         ECO:0000256|RuleBase:RU363013};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-erythrulose 1-phosphate = D-erythrulose 4-phosphate;
CC         Xref=Rhea:RHEA:49588, ChEBI:CHEBI:58002, ChEBI:CHEBI:90796;
CC         EC=5.3.1.33; Evidence={ECO:0000256|ARBA:ARBA00000148};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate from glycerone phosphate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004680, ECO:0000256|HAMAP-Rule:MF_00147,
CC       ECO:0000256|RuleBase:RU363013}.
CC   -!- PATHWAY: Carbohydrate metabolism; erythritol degradation.
CC       {ECO:0000256|ARBA:ARBA00004939}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00147,
CC       ECO:0000256|RuleBase:RU363013}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00147,
CC       ECO:0000256|RuleBase:RU363013}.
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC       {ECO:0000256|ARBA:ARBA00007422, ECO:0000256|HAMAP-Rule:MF_00147,
CC       ECO:0000256|PROSITE-ProRule:PRU10127, ECO:0000256|RuleBase:RU363013}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM236080; CAK08001.1; -; Genomic_DNA.
DR   RefSeq; WP_011652070.1; NC_008380.1.
DR   AlphaFoldDB; Q1MGC2; -.
DR   EnsemblBacteria; CAK08001; CAK08001; RL2513.
DR   GeneID; 303207506; -.
DR   KEGG; rle:RL2513; -.
DR   eggNOG; COG0149; Bacteria.
DR   HOGENOM; CLU_024251_2_1_5; -.
DR   UniPathway; UPA00109; UER00189.
DR   UniPathway; UPA00138; -.
DR   UniPathway; UPA01066; -.
DR   Proteomes; UP000006575; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; IEA:TreeGrafter.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:TreeGrafter.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00311; TIM; 1.
DR   FunFam; 3.20.20.70:FF:000016; Triosephosphate isomerase; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 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   NCBIfam; TIGR00419; tim; 1.
DR   PANTHER; PTHR21139; TRIOSEPHOSPHATE ISOMERASE; 1.
DR   PANTHER; PTHR21139:SF42; TRIOSEPHOSPHATE ISOMERASE; 1.
DR   Pfam; PF00121; TIM; 1.
DR   SUPFAM; SSF51351; Triosephosphate isomerase (TIM); 1.
DR   PROSITE; PS00171; TIM_1; 1.
DR   PROSITE; PS51440; TIM_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00147};
KW   Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432, ECO:0000256|HAMAP-
KW   Rule:MF_00147};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW   Rule:MF_00147};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00147};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006575}.
FT   ACT_SITE        99
FT                   /note="Electrophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00147,
FT                   ECO:0000256|PROSITE-ProRule:PRU10127"
FT   ACT_SITE        169
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00147,
FT                   ECO:0000256|PROSITE-ProRule:PRU10127"
FT   BINDING         12..14
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00147"
FT   BINDING         12
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10127"
FT   BINDING         14
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10127"
FT   BINDING         175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00147"
FT   BINDING         214
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00147"
FT   BINDING         235..236
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00147"
SQ   SEQUENCE   256 AA;  26972 MW;  06A6642D604A065D CRC64;
     MTPDVRPLVA GNWKMNGMRA SLDQIKTIAE GVRPPLADKV EALICPPATL LYVATALCTD
     SPLAIGAQDC HQNPSGAHTG DISAEMIADC FGTYVIVGHS ERRTDHAETD HLVRAKAEAA
     FAAGLTAIIC IGETADERRT GQALDVIKRQ LSASVPDCAT AESTVIAYEP IWAIGTGVTP
     TSGDVEKAHA FMRAELAVRF GDEGRKMRLL YGGSVKPANA HELMGIANVD GALIGGASLK
     AADFLAIYRA YEALLA
//