ID   FSA_SALPB               Reviewed;         220 AA.
AC   A9N0F4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=SPAB_05092;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000886; ABX70383.1; -; Genomic_DNA.
DR   RefSeq; WP_000424866.1; NC_010102.1.
DR   AlphaFoldDB; A9N0F4; -.
DR   SMR; A9N0F4; -.
DR   KEGG; spq:SPAB_05092; -.
DR   PATRIC; fig|1016998.12.peg.4779; -.
DR   HOGENOM; CLU_079764_2_0_6; -.
DR   OMA; QQMLGTP; -.
DR   BioCyc; SENT1016998:SPAB_RS20720-MON; -.
DR   Proteomes; UP000008556; 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_1000081411"
FT   ACT_SITE        85
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00496"
SQ   SEQUENCE   220 AA;  23525 MW;  333921DD60B3A167 CRC64;
     MELYLDTANV AEVERLARIF PIAGVTTNPS IVAASKESIW DVLPRLQNAI GEEGTLFAQT
     MSRDAKGMVE EAKRLNNAIP GIVVKIPVTA EGLAAIKLLK KEGIVTLGTA VYSASQGLLA
     ALAGAKYVAP YVNRVDAQGG DGIRMVQELQ TLLEHHAPDS MVLAASFKTP RQALDCLLAG
     CQAITLPLDV AQQMLNTPAV ESAIEKFEQD WKNAFGNLNL