ID   FSAA_ECO57              Reviewed;         220 AA.
AC   P58423;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Fructose-6-phosphate aldolase 1;
DE            EC=4.1.2.-;
GN   Name=fsaA; Synonyms=fsa, mipB; OrderedLocusNames=Z1048, ECs0903;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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=AAG55198.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB34326.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE005174; AAG55198.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BA000007; BAB34326.1; ALT_INIT; Genomic_DNA.
DR   PIR; B85592; B85592.
DR   PIR; G90741; G90741.
DR   RefSeq; NP_308930.3; NC_002695.1.
DR   RefSeq; WP_000424894.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P58423; -.
DR   SMR; P58423; -.
DR   STRING; 155864.EDL933_0949; -.
DR   EnsemblBacteria; AAG55198; AAG55198; Z1048.
DR   EnsemblBacteria; BAB34326; BAB34326; ECs_0903.
DR   GeneID; 917642; -.
DR   KEGG; ece:Z1048; -.
DR   KEGG; ecs:ECs_0903; -.
DR   PATRIC; fig|386585.9.peg.1018; -.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_079764_2_0_6; -.
DR   OMA; VRHPMHV; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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; Reference proteome; Schiff base.
FT   CHAIN           1..220
FT                   /note="Fructose-6-phosphate aldolase 1"
FT                   /id="PRO_0000173645"
FT   ACT_SITE        85
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   220 AA;  23113 MW;  B5D2B38FF13EDC5C CRC64;
     MELYLDTSDV VAVKALSRIF PLAGVTTNPS IIAAGKKPLE VVLPELHEAM GGQGRLFAQV
     MATTAEGMVN DARKLRSIIA DIVVKVPVTT EGLAAIKMLK AEGIPTLGTA VYGAAQGLLS
     ALAGAEYVAP YVNRIDAQGG SGIQTVTDLH QLLKMHAPRA KVLAASFKTP RQALDCLLAG
     CESITLPLDV AQQMISYPAV DAAVAKFEQD WQGAFGRTSI