ID   FSAA_ECOL6              Reviewed;         220 AA.
AC   Q8FJL3;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 2.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Fructose-6-phosphate aldolase 1;
DE            EC=4.1.2.-;
GN   Name=fsaA; Synonyms=fsa, mipB; OrderedLocusNames=c0910;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Catalyzes the reversible formation of fructose 6-phosphate
CC       from dihydroxyacetone and D-glyceraldehyde 3-phosphate via an
CC       aldolization reaction. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 6-phosphate = D-glyceraldehyde 3-phosphate +
CC         dihydroxyacetone; Xref=Rhea:RHEA:28002, ChEBI:CHEBI:16016,
CC         ChEBI:CHEBI:57634, ChEBI:CHEBI:59776;
CC   -!- SUBUNIT: Homodecamer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 3A subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN79383.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN79383.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001298570.1; NC_004431.1.
DR   AlphaFoldDB; Q8FJL3; -.
DR   SMR; Q8FJL3; -.
DR   STRING; 199310.c0910; -.
DR   EnsemblBacteria; AAN79383; AAN79383; c0910.
DR   KEGG; ecc:c0910; -.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_079764_2_0_6; -.
DR   OMA; VRHPMHV; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097023; F:fructose 6-phosphate aldolase activity; IEA:RHEA.
DR   GO; GO:0006000; P:fructose metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00956; Transaldolase_FSA; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00496; F6P_aldolase; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR023001; F6P_aldolase.
DR   InterPro; IPR001585; TAL/FSA.
DR   InterPro; IPR004731; Transaldolase_3B/F6P_aldolase.
DR   InterPro; IPR018225; Transaldolase_AS.
DR   InterPro; IPR033919; TSA/FSA_arc/bac.
DR   PANTHER; PTHR10683; PTHR10683; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   TIGRFAMs; TIGR00875; fsa_talC_mipB; 1.
DR   PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR   PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Lyase; Schiff base.
FT   CHAIN           1..220
FT                   /note="Fructose-6-phosphate aldolase 1"
FT                   /id="PRO_0000173644"
FT   ACT_SITE        85
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   220 AA;  23012 MW;  80AFBD95C850CB8B CRC64;
     MELYLDTSDV VAVTALSRIF PLAGVTTNPS IIAAGKKPLE VVLPQLHEAM GGQGRLFAQV
     MATTAEGMVN DARKLRSIIA DIVVKVPVTA EGLAAIKMLK AEGIPTLGTA VYGAAQGLLS
     ALAGAEYVAP YVNRIDAQGG SGIQTVTDLH QLLKMHAPQA KVLAASFKTP RQALDCLLAG
     CESITLPLDV AQQMISYPAV DAAVAKFEQD WLGAFGRTSI