ID   TPIS2_LISIN             Reviewed;         254 AA.
AC   Q92EU4;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Triosephosphate isomerase 2 {ECO:0000303|PubMed:22773791};
DE            Short=TIM 2 {ECO:0000250|UniProtKB:P9WG43};
DE            Short=TPI 2 {ECO:0000303|PubMed:22773791};
DE            EC=5.3.1.1 {ECO:0000269|PubMed:22773791};
DE   AltName: Full=Triose-phosphate isomerase 2 {ECO:0000250|UniProtKB:P9WG43};
GN   Name=tpi-2 {ECO:0000303|PubMed:22773791}; Synonyms=tpiA2 {ECO:0000305};
GN   OrderedLocusNames=lin0364;
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
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).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, INDUCTION, SUBCELLULAR LOCATION, AND PATHWAY.
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
RX   PubMed=22773791; DOI=10.1128/jb.00801-12;
RA   Monniot C., Zebre A.C., Ake F.M., Deutscher J., Milohanic E.;
RT   "Novel listerial glycerol dehydrogenase- and phosphoenolpyruvate-dependent
RT   dihydroxyacetone kinase system connected to the pentose phosphate
RT   pathway.";
RL   J. Bacteriol. 194:4972-4982(2012).
CC   -!- FUNCTION: Involved in the glycerol metabolism. Catalyzes
CC       stereospecifically the conversion of dihydroxyacetone phosphate (DHAP)
CC       to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000269|PubMed:22773791}.
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:0000269|PubMed:22773791};
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation.
CC       {ECO:0000305|PubMed:22773791}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WG43}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:22773791}.
CC   -!- INDUCTION: Repressed by GolR. {ECO:0000269|PubMed:22773791}.
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; AL596164; CAC95597.1; -; Genomic_DNA.
DR   PIR; AE1478; AE1478.
DR   RefSeq; WP_010990359.1; NC_003212.1.
DR   AlphaFoldDB; Q92EU4; -.
DR   SMR; Q92EU4; -.
DR   STRING; 272626.lin0364; -.
DR   EnsemblBacteria; CAC95597; CAC95597; CAC95597.
DR   KEGG; lin:lin0364; -.
DR   eggNOG; COG0149; Bacteria.
DR   HOGENOM; CLU_024251_2_3_9; -.
DR   OMA; IEKNGTM; -.
DR   OrthoDB; 1266295at2; -.
DR   UniPathway; UPA00616; -.
DR   Proteomes; UP000002513; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR   GO; GO:0004807; F:triose-phosphate isomerase activity; IDA:UniProtKB.
DR   GO; GO:0006094; P:gluconeogenesis; TAS:UniProtKB.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006096; P:glycolytic process; TAS:UniProtKB.
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   1: Evidence at protein level;
KW   Cytoplasm; Glycerol metabolism; Isomerase.
FT   CHAIN           1..254
FT                   /note="Triosephosphate isomerase 2"
FT                   /id="PRO_0000090239"
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;  28065 MW;  F99CA128F50DE71C CRC64;
     MRKPLVGINM KNYINTRAQT SEWLEATIPL LENFSDVDTF IFPSMGTLET TANLLAGTSF
     GFGPQNMAPE KSGPLTGEFS VESIIDLNAN YVEIGHAERK NLFHEKTSEI AKKIKLALDE
     KITPVVCVGE EVHANDTNEL KNALKKQIEA LFQTINLAQW ENVVLAYEPE WAIGKASSAE
     TNYIESAHQA LREIIRELGG DETLVRIIYG GSVSKENAAE IVRQKNVDGL FVGRFGHKPQ
     NFADIVSIVS KTKG