TAL_YERP3
ID TAL_YERP3 Reviewed; 317 AA.
AC A7FME9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Transaldolase {ECO:0000255|HAMAP-Rule:MF_00492};
DE EC=2.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00492};
GN Name=tal {ECO:0000255|HAMAP-Rule:MF_00492};
GN OrderedLocusNames=YpsIP31758_3472;
OS Yersinia pseudotuberculosis serotype O:1b (strain IP 31758).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP 31758;
RX PubMed=17784789; DOI=10.1371/journal.pgen.0030142;
RA Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G.,
RA Fayolle C., Lindler L.E., Carniel E., Ravel J.;
RT "The complete genome sequence of Yersinia pseudotuberculosis IP31758, the
RT causative agent of Far East scarlet-like fever.";
RL PLoS Genet. 3:1508-1523(2007).
CC -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC the pentose-phosphate pathway. {ECO:0000255|HAMAP-Rule:MF_00492}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC beta-D-fructose 6-phosphate + D-erythrose 4-phosphate;
CC Xref=Rhea:RHEA:17053, ChEBI:CHEBI:16897, ChEBI:CHEBI:57483,
CC ChEBI:CHEBI:57634, ChEBI:CHEBI:59776; EC=2.2.1.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00492};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-
CC ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage):
CC step 2/3. {ECO:0000255|HAMAP-Rule:MF_00492}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00492}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00492}.
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DR EMBL; CP000720; ABS47615.1; -; Genomic_DNA.
DR RefSeq; WP_002209241.1; NC_009708.1.
DR AlphaFoldDB; A7FME9; -.
DR SMR; A7FME9; -.
DR EnsemblBacteria; ABS47615; ABS47615; YpsIP31758_3472.
DR GeneID; 57974146; -.
DR KEGG; ypi:YpsIP31758_3472; -.
DR HOGENOM; CLU_047470_0_1_6; -.
DR OMA; KFGYKTL; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000002412; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004801; F:transaldolase activity; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule.
DR CDD; cd00957; Transaldolase_TalAB; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00492; Transaldolase_1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001585; TAL/FSA.
DR InterPro; IPR004730; Transaldolase_1.
DR InterPro; IPR018225; Transaldolase_AS.
DR PANTHER; PTHR10683; PTHR10683; 1.
DR PANTHER; PTHR10683:SF18; PTHR10683:SF18; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR TIGRFAMs; TIGR00874; talAB; 1.
DR PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Pentose shunt; Schiff base; Transferase.
FT CHAIN 1..317
FT /note="Transaldolase"
FT /id="PRO_1000060452"
FT ACT_SITE 132
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
SQ SEQUENCE 317 AA; 35049 MW; 3576DDDAD0C693A8 CRC64;
MTDKLTSLRQ ITTVVADTGD IAAMKLYQPQ DATTNPSIIL NAAQIPEYRK LIDEAIAWAR
EQSSDHAQQI VDATDKLAVN IGLEILKLIP GRISTEVDAR LSYDTVASVA KAKRLIKLYN
EAGISNDRIL IKLASTWQGI RAAEQLEKEG INCNLTLLFS FAQARACAEA GVFLISPFVG
RILDWYKANG DQKEFAPSED PGVVSVTEIY QYYKKHGYKT VVMGASFRNL GEIIELAGCD
RLTIAPSLLK ELAESEGPVE RKLAYTGEIQ AKPAPLTEAE FYWQHNQDPM AVDKLADGIR
KFAIDQGKLE KMISDLL
