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Database: UniProt/SWISS-PROT
Entry: TPIS_THEP3
LinkDB: TPIS_THEP3
Original site: TPIS_THEP3 
ID   TPIS_THEP3              Reviewed;         248 AA.
AC   B0K880;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   23-MAY-2018, entry version 73.
DE   RecName: Full=Triosephosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147};
DE            Short=TIM {ECO:0000255|HAMAP-Rule:MF_00147};
DE            Short=TPI {ECO:0000255|HAMAP-Rule:MF_00147};
DE            EC=5.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00147};
DE   AltName: Full=Triose-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147};
GN   Name=tpiA {ECO:0000255|HAMAP-Rule:MF_00147};
GN   OrderedLocusNames=Teth39_0733;
OS   Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E)
OS   (Clostridium thermohydrosulfuricum).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=340099;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33223 / 39E;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E.,
RA   Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z.,
RA   Zhou J., Richardson P.;
RT   "Complete sequence of Thermoanaerobacter pseudethanolicus 39E.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes
CC       stereospecifically the conversion of dihydroxyacetone phosphate
CC       (DHAP) to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000255|HAMAP-
CC       Rule:MF_00147}.
CC   -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate = glycerone
CC       phosphate. {ECO:0000255|HAMAP-Rule:MF_00147}.
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00147}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate from glycerone phosphate: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_00147}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00147}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00147}.
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00147}.
DR   EMBL; CP000924; ABY94393.1; -; Genomic_DNA.
DR   ProteinModelPortal; B0K880; -.
DR   SMR; B0K880; -.
DR   STRING; 340099.Teth39_0733; -.
DR   PRIDE; B0K880; -.
DR   EnsemblBacteria; ABY94393; ABY94393; Teth39_0733.
DR   KEGG; tpd:Teth39_0733; -.
DR   eggNOG; ENOG4105CP7; Bacteria.
DR   eggNOG; COG0149; LUCA.
DR   HOGENOM; HOG000226412; -.
DR   KO; K01803; -.
DR   OMA; LCVGEGL; -.
DR   UniPathway; UPA00109; UER00189.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000002156; Chromosome.
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   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   PANTHER; PTHR21139; PTHR21139; 1.
DR   Pfam; PF00121; TIM; 1.
DR   SUPFAM; SSF51351; SSF51351; 1.
DR   TIGRFAMs; TIGR00419; tim; 1.
DR   PROSITE; PS00171; TIM_1; 1.
DR   PROSITE; PS51440; TIM_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase;
KW   Reference proteome.
FT   CHAIN         1    248       Triosephosphate isomerase.
FT                                /FTId=PRO_1000096542.
FT   REGION        9     11       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00147}.
FT   REGION      233    234       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00147}.
FT   ACT_SITE     94     94       Electrophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_00147}.
FT   ACT_SITE    166    166       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00147}.
FT   BINDING     172    172       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00147}.
FT   BINDING     212    212       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00147}.
SQ   SEQUENCE   248 AA;  27042 MW;  C98DBAFE020F5643 CRC64;
     MRRPIIAGNW KMHMTPSEAV KLVEELIPQV KDAKAEVVVI PPFVDLTEVN KVIQGTNILL
     GAQDMFWEEK GAYTGEISPL MLKEIGVKYV VIGHSERRQY FGETDEMVNK KVLSALSHGL
     SPIVCVGESL SQREEGKTFE VVLNQTKEAL KGVSHDDIVN VVIAYEPIWA IGTGKTATAK
     DANEVIKALR NTIASLYGKE KASLVRIQYG GSVKPENISE LMAESDIDGA LVGGASLVAS
     DFAKIVNY
//
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