(data stored in ACNUC10821 zone)

SWISSPROT: TPIS2_LISMF

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   08-MAY-2019, entry version 86.
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};
GN   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.,
RA   Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T.,
RA   Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J.,
RA   Brinkac L.M., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R.,
RA   Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N.,
RA   Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A.,
RA   Bayles D.O., Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-
RT   borne pathogen Listeria monocytogenes reveal new insights into the
RT   core genome components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
CC   -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes
CC       stereospecifically the conversion of dihydroxyacetone phosphate
CC       (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
CC       {ECO:0000250|UniProtKB:P9WG43}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone
CC         phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642,
CC         ChEBI:CHEBI:59776; EC=5.3.1.1;
CC         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}.
DR   EMBL; AE017262; AAT03152.1; -; Genomic_DNA.
DR   RefSeq; WP_003724277.1; NC_002973.6.
DR   SMR; Q723V9; -.
DR   EnsemblBacteria; AAT03152; AAT03152; LMOf2365_0366.
DR   KEGG; lmf:LMOf2365_0366; -.
DR   HOGENOM; HOG000226413; -.
DR   KO; K01803; -.
DR   OMA; IADCFGT; -.
DR   BioCyc; LMON265669:G1G0V-383-MONOMER; -.
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;
DR   PRODOM; Q723V9.
DR   SWISS-2DPAGE; Q723V9.
KW   Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase.
FT   CHAIN         1    254       Probable triosephosphate isomerase 2.
FT                                /FTId=PRO_0000090241.
FT   REGION        9     11       Substrate binding.
FT                                {ECO:0000250|UniProtKB:P9WG43}.
FT   ACT_SITE     96     96       Electrophile.
FT                                {ECO:0000250|UniProtKB:P9WG43}.
FT   ACT_SITE    168    168       Proton acceptor.
FT                                {ECO:0000250|UniProtKB:P9WG43}.
FT   BINDING     174    174       Substrate; via amide nitrogen.
FT                                {ECO:0000250|UniProtKB:P9WG43}.
FT   BINDING     212    212       Substrate.
FT                                {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
//

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