ID   TPIS2_LISMF             Reviewed;         254 AA.
AC   Q723V9;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=LMOf2365_0366;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA   Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA   White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA   Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA   Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA   Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA   Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT   pathogen Listeria monocytogenes reveal new insights into the core genome
RT   components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
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; AE017262; AAT03152.1; -; Genomic_DNA.
DR   RefSeq; WP_003724277.1; NC_002973.6.
DR   AlphaFoldDB; Q723V9; -.
DR   SMR; Q723V9; -.
DR   KEGG; lmf:LMOf2365_0366; -.
DR   HOGENOM; CLU_024251_2_3_9; -.
DR   OMA; IEKNGTM; -.
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.
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.
FT   CHAIN           1..254
FT                   /note="Probable triosephosphate isomerase 2"
FT                   /id="PRO_0000090241"
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;  28083 MW;  142D35B5BD7963C0 CRC64;
     MRKPLVGINM KNYINTRAQT SEWLEATIPL LKNFSDVDTF IFPSMGTLET TANLLAGTSF
     GFGPQNMAPE KSGPLTGEFS VESIIDLNAN YVEIGHAERK NLFHEKTSEI AKKIKLALDE
     KITPVVCVGE EVRANDTNEL KNALKKQIEA LFQTINLAQW ENVVLAYEPE WAIGKASSAE
     TNYIESAHQA LREIIRELGG DETLVRIIYG GSVSKENAAE IVRQKNVDGL FVGRFGHKPQ
     NFADIVSIVS KTKG