ID   TALB_ECO1E              Reviewed;         317 AA.
AC   K0BE10;
DT   18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2012, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Transaldolase;
DE            EC=2.2.1.2;
GN   Name=talB; OrderedLocusNames=O3O_03880;
OS   Escherichia coli O104:H4 (strain 2009EL-2071).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=1133853;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2009EL-2071;
RX   PubMed=23133618; DOI=10.1371/journal.pone.0048228;
RA   Ahmed S.A., Awosika J., Baldwin C., Bishop-Lilly K.A., Biswas B.,
RA   Broomall S., Chain P.S., Chertkov O., Chokoshvili O., Coyne S.,
RA   Davenport K., Detter J.C., Dorman W., Erkkila T.H., Folster J.P.,
RA   Frey K.G., George M., Gleasner C., Henry M., Hill K.K., Hubbard K.,
RA   Insalaco J., Johnson S., Kitzmiller A., Krepps M., Lo C.C., Luu T.,
RA   McNew L.A., Minogue T., Munk C.A., Osborne B., Patel M., Reitenga K.G.,
RA   Rosenzweig C.N., Shea A., Shen X., Strockbine N., Tarr C., Teshima H.,
RA   van Gieson E., Verratti K., Wolcott M., Xie G., Sozhamannan S.,
RA   Gibbons H.S.;
RT   "Genomic comparison of Escherichia coli O104:H4 isolates from 2009 and 2011
RT   reveals plasmid, and prophage heterogeneity, including Shiga toxin encoding
RT   phage stx2.";
RL   PLoS ONE 7:E48228-E48228(2012).
CC   -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC       the pentose-phosphate pathway. {ECO:0000250|UniProtKB:P0A870}.
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:0000250|UniProtKB:P0A870};
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.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0A870}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A870}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP003301; AFS84550.1; -; Genomic_DNA.
DR   RefSeq; WP_000130189.1; NC_018661.1.
DR   AlphaFoldDB; K0BE10; -.
DR   SMR; K0BE10; -.
DR   KEGG; eso:O3O_03880; -.
DR   PATRIC; fig|1133853.3.peg.4527; -.
DR   HOGENOM; CLU_047470_0_1_6; -.
DR   OMA; KFGYKTL; -.
DR   UniPathway; UPA00115; UER00414.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004801; F:transaldolase activity; IDA: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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..317
FT                   /note="Transaldolase"
FT                   /id="PRO_0000423396"
FT   ACT_SITE        132
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   317 AA;  35249 MW;  6CE02C751E57705D CRC64;
     MTDKLTSLRQ YTTVVADTGD IAAMKLYQPQ DATTNPSLIL NAAQIPEYRK LIDDAVAWAK
     QQSNDRAQQI VDATDKLAVN IGLEILKLVP GRISTEVDAR LSYDTEASIA KAKRLIKLYN
     DAGISNDRIL IKLASTWQGI RAAEQLEKEG INCNLTLLFS FAQARACAEA GVFLISPFVG
     RILDWYKANT DKKEYAPAED PGVVSVSEIY QYYKEHGYET VVMGASFRNI GEILELAGCD
     RLTIAPTLLK ELAESEGAIE RKLSYTGEVK ARPARITESE FLWQHNQDPM AVDKLAEGIR
     KFAIDQEKLE KMIGDLL