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Triosephosphate isomerase (TIM) (TPI) (EC 5.3.1.1) (Triose-phosphate isomerase)

 TPIS_FRATF              Reviewed;         253 AA.
A7NEF8;
20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
26-FEB-2008, sequence version 2.
23-MAY-2018, entry version 71.
RecName: Full=Triosephosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147};
Short=TIM {ECO:0000255|HAMAP-Rule:MF_00147};
Short=TPI {ECO:0000255|HAMAP-Rule:MF_00147};
EC=5.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00147};
AltName: Full=Triose-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147};
Name=tpiA {ECO:0000255|HAMAP-Rule:MF_00147};
OrderedLocusNames=FTA_1886;
Francisella tularensis subsp. holarctica (strain FTNF002-00 / FTA).
Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
Francisellaceae; Francisella.
NCBI_TaxID=458234;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=FTNF002-00 / FTA;
PubMed=19756146; DOI=10.1371/journal.pone.0007041;
Barabote R.D., Xie G., Brettin T.S., Hinrichs S.H., Fey P.D.,
Jay J.J., Engle J.L., Godbole S.D., Noronha J.M., Scheuermann R.H.,
Zhou L.W., Lion C., Dempsey M.P.;
"Complete genome sequence of Francisella tularensis subspecies
holarctica FTNF002-00.";
PLoS ONE 4:E7041-E7041(2009).
-!- FUNCTION: Involved in the gluconeogenesis. Catalyzes
stereospecifically the conversion of dihydroxyacetone phosphate
(DHAP) to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000255|HAMAP-
Rule:MF_00147}.
-!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate = glycerone
phosphate. {ECO:0000255|HAMAP-Rule:MF_00147}.
-!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
{ECO:0000255|HAMAP-Rule:MF_00147}.
-!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
phosphate from glycerone phosphate: step 1/1. {ECO:0000255|HAMAP-
Rule:MF_00147}.
-!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00147}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00147}.
-!- SIMILARITY: Belongs to the triosephosphate isomerase family.
{ECO:0000255|HAMAP-Rule:MF_00147}.
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EMBL; CP000803; ABU62361.2; -; Genomic_DNA.
RefSeq; WP_003017307.1; NC_009749.1.
ProteinModelPortal; A7NEF8; -.
SMR; A7NEF8; -.
PRIDE; A7NEF8; -.
EnsemblBacteria; ABU62361; ABU62361; FTA_1886.
KEGG; fta:FTA_1886; -.
HOGENOM; HOG000226413; -.
KO; K01803; -.
OMA; LCVGEGL; -.
UniPathway; UPA00109; UER00189.
UniPathway; UPA00138; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:UniProtKB-EC.
GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
CDD; cd00311; TIM; 1.
Gene3D; 3.20.20.70; -; 1.
HAMAP; MF_00147_B; TIM_B; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR035990; TIM_sf.
InterPro; IPR022896; TrioseP_Isoase_bac/euk.
InterPro; IPR000652; Triosephosphate_isomerase.
InterPro; IPR020861; Triosephosphate_isomerase_AS.
PANTHER; PTHR21139; PTHR21139; 1.
Pfam; PF00121; TIM; 1.
SUPFAM; SSF51351; SSF51351; 1.
TIGRFAMs; TIGR00419; tim; 1.
PROSITE; PS00171; TIM_1; 1.
PROSITE; PS51440; TIM_2; 1.
3: Inferred from homology;
Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase.
CHAIN 1 253 Triosephosphate isomerase.
/FTId=PRO_1000076647.
REGION 8 10 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_00147}.
REGION 231 232 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_00147}.
ACT_SITE 93 93 Electrophile. {ECO:0000255|HAMAP-
Rule:MF_00147}.
ACT_SITE 165 165 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_00147}.
BINDING 171 171 Substrate; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_00147}.
BINDING 210 210 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00147}.
SEQUENCE 253 AA; 27656 MW; 78566DD0CE374D37 CRC64;
MQKLIMGNWK MNGNSTSIKE LCSGISQVQY DTSRVAIAVF PSSVYVKEVI SQLPEKVGVG
LQNITFYDDG AYTGEISARM LEDIGCDYLL IGHSERRSLF AESDEDVFKK LNKIIDTTIT
PVVCIGESLD DRKSGKLKQV LATQLSLILE NLSVEQLAKV VIAYEPVWAI GTGVVASLEQ
IQETHQFIRS LLAKVDERLA KNIKIVYGGS LKAENAKDIL SLPDVDGGLI GGASLKAAEF
NEIINQANKI CTE


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