ID   TPIS2_LISMO             Reviewed;         254 AA.
AC   Q8YA20;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Probable triosephosphate isomerase 2 {ECO:0000250|UniProtKB:P9WG43};
DE            Short=TIM 2 {ECO:0000250|UniProtKB:P9WG43};
DE            Short=TPI 2 {ECO:0000250|UniProtKB:P9WG43};
DE            EC=5.3.1.1 {ECO:0000250|UniProtKB:P9WG43};
DE   AltName: Full=Triose-phosphate isomerase 2 {ECO:0000250|UniProtKB:P9WG43};
GN   Name=tpiA2 {ECO:0000250|UniProtKB:P9WG43}; OrderedLocusNames=lmo0346;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
CC   -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes stereospecifically
CC       the conversion of dihydroxyacetone phosphate (DHAP) to D-
CC       glyceraldehyde-3-phosphate (G3P). {ECO:0000250|UniProtKB:P9WG43}.
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:0000250|UniProtKB:P9WG43};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000250|UniProtKB:P9WG43}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate from glycerone phosphate: step 1/1.
CC       {ECO:0000250|UniProtKB:P9WG43}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WG43}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WG43}.
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; AL591975; CAC98425.1; -; Genomic_DNA.
DR   PIR; AC1118; AC1118.
DR   RefSeq; NP_463876.1; NC_003210.1.
DR   RefSeq; WP_010989434.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q8YA20; -.
DR   SMR; Q8YA20; -.
DR   STRING; 169963.lmo0346; -.
DR   PaxDb; Q8YA20; -.
DR   EnsemblBacteria; CAC98425; CAC98425; CAC98425.
DR   GeneID; 987587; -.
DR   KEGG; lmo:lmo0346; -.
DR   PATRIC; fig|169963.11.peg.356; -.
DR   eggNOG; COG0149; Bacteria.
DR   HOGENOM; CLU_024251_2_3_9; -.
DR   OMA; IEKNGTM; -.
DR   PhylomeDB; Q8YA20; -.
DR   BioCyc; LMON169963:LMO0346-MON; -.
DR   UniPathway; UPA00109; UER00189.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000817; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004807; F:triose-phosphate isomerase activity; IBA:GO_Central.
DR   GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR   GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0019563; P:glycerol catabolic process; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   CDD; cd00311; TIM; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR035990; TIM_sf.
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   PROSITE; PS00171; TIM_1; 1.
DR   PROSITE; PS51440; TIM_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT   CHAIN           1..254
FT                   /note="Probable triosephosphate isomerase 2"
FT                   /id="PRO_0000090243"
FT   ACT_SITE        96
FT                   /note="Electrophile"
FT                   /evidence="ECO:0000250|UniProtKB:P9WG43"
FT   ACT_SITE        168
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WG43"
FT   BINDING         9..11
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WG43"
FT   BINDING         174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WG43"
FT   BINDING         212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WG43"
SQ   SEQUENCE   254 AA;  27918 MW;  BB0A97C4420147CC CRC64;
     MRKPLVGINM KNYINTRAQT SEWLEATIPL LGNFSDVDTF IFPSMGTLET TANLLAGTSF
     GFGPQNMAPE KSGPLTGEFS VESIIDLSAN YVEIGHAERK NLFHEKTSEI AKKIQLALDE
     KITPVVCVGE GIRANDTNEL KNALKKQIEA LFDTIQVTQF KNVVLAYEPE WAIGKANSAD
     TDYIESAHQA LREIIRELGG DETLVRIIYG GSVSKENAAE IVRQKNVDGL FVGRFGHKPQ
     NFADIVSIVS KTKG