ID   FSAB_ECO57              Reviewed;         220 AA.
AC   P58424;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Fructose-6-phosphate aldolase 2;
DE            EC=4.1.2.-;
GN   Name=fsaB; Synonyms=talC; OrderedLocusNames=Z5501, ECs4875;
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   -!- PATHWAY: Carbohydrate metabolism; fructose metabolism.
CC   -!- SUBUNIT: Homodecamer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 3A subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE005174; AAG59147.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB38298.1; -; Genomic_DNA.
DR   PIR; C91238; C91238.
DR   PIR; G86085; G86085.
DR   RefSeq; NP_312902.1; NC_002695.1.
DR   RefSeq; WP_000424823.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P58424; -.
DR   SMR; P58424; -.
DR   STRING; 155864.EDL933_5282; -.
DR   EnsemblBacteria; AAG59147; AAG59147; Z5501.
DR   EnsemblBacteria; BAB38298; BAB38298; ECs_4875.
DR   GeneID; 915012; -.
DR   KEGG; ece:Z5501; -.
DR   KEGG; ecs:ECs_4875; -.
DR   PATRIC; fig|386585.9.peg.5099; -.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_079764_2_0_6; -.
DR   OMA; QQMLGTP; -.
DR   UniPathway; UPA00202; -.
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 2"
FT                   /id="PRO_0000173648"
FT   ACT_SITE        85
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   220 AA;  23506 MW;  45B6FAA9D97F045F CRC64;
     MELYLDTANV AEVERLAHIF PIAGVTTNPS IIAASKESIW EVLPRLQKAI GDEGILFAQT
     MSRDAQGMVE EAKRLRDAIP GIVVKIPVTS EGLAAIKILK KEGITTLGTA VYSAAQGLLA
     ALAGAKYVAP YVNRVDAQGG DGIRTVQELQ ALLEMHAPES MVLAASFKTP RQALDCLLAG
     CESITLPLDV AQQMLNTPAV ESAIEKFEHD WNAAFGTTHL