ID   FSA_SALHS               Reviewed;         220 AA.
AC   B4TCP9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Fructose-6-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00496};
DE            EC=4.1.2.- {ECO:0000255|HAMAP-Rule:MF_00496};
GN   Name=fsa {ECO:0000255|HAMAP-Rule:MF_00496}; OrderedLocusNames=SeHA_C4444;
OS   Salmonella heidelberg (strain SL476).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=454169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL476;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
CC   -!- FUNCTION: Catalyzes the reversible formation of fructose 6-phosphate
CC       from dihydroxyacetone and D-glyceraldehyde 3-phosphate via an
CC       aldolization reaction. {ECO:0000255|HAMAP-Rule:MF_00496}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00496};
CC   -!- SUBUNIT: Homodecamer. {ECO:0000255|HAMAP-Rule:MF_00496}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00496}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 3A subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00496}.
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DR   EMBL; CP001120; ACF66675.1; -; Genomic_DNA.
DR   RefSeq; WP_000424826.1; NC_011083.1.
DR   AlphaFoldDB; B4TCP9; -.
DR   SMR; B4TCP9; -.
DR   KEGG; seh:SeHA_C4444; -.
DR   HOGENOM; CLU_079764_2_0_6; -.
DR   OMA; QQMLGTP; -.
DR   Proteomes; UP000001866; 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"
FT                   /id="PRO_1000126377"
FT   ACT_SITE        85
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00496"
SQ   SEQUENCE   220 AA;  23506 MW;  F349F789FE8B1733 CRC64;
     MELYLDTANV AEVERLAHIF PIAGVTTNPS IVAASKESIW DVLPRLQNAI GEEGTLFAQT
     MSRDAKGMVE EAKRLNNAIP GIVVKIPVTA EGLAAIKLLK KEGIVTLGTA VYSASQGLLA
     ALAGAKYVAP YVNRVDAQGG DGIRMVQELQ TLLEHHAPDS MVLAASFKTP RQALDCLLAG
     CQAITLPLDV AQQMLNTPAV ESAIEKFEQD WKNAFGNLNL