ID   FSA_STRPJ               Reviewed;         222 AA.
AC   B8ZKS3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Probable 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=SPN23F02420;
OS   Streptococcus pneumoniae (strain ATCC 700669 / Spain 23F-1).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=561276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700669 / Spain 23F-1;
RX   PubMed=19114491; DOI=10.1128/jb.01343-08;
RA   Croucher N.J., Walker D., Romero P., Lennard N., Paterson G.K., Bason N.C.,
RA   Mitchell A.M., Quail M.A., Andrew P.W., Parkhill J., Bentley S.D.,
RA   Mitchell T.J.;
RT   "Role of conjugative elements in the evolution of the multidrug-resistant
RT   pandemic clone Streptococcus pneumoniae Spain23F ST81.";
RL   J. Bacteriol. 191:1480-1489(2009).
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   -!- 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; FM211187; CAR68102.1; -; Genomic_DNA.
DR   RefSeq; WP_000395437.1; NC_011900.1.
DR   AlphaFoldDB; B8ZKS3; -.
DR   SMR; B8ZKS3; -.
DR   PRIDE; B8ZKS3; -.
DR   KEGG; sne:SPN23F02420; -.
DR   HOGENOM; CLU_079764_2_0_9; -.
DR   OMA; QQMLGTP; -.
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; IPR018225; Transaldolase_AS.
DR   InterPro; IPR033919; TSA/FSA_arc/bac.
DR   PANTHER; PTHR10683; PTHR10683; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Lyase; Schiff base.
FT   CHAIN           1..222
FT                   /note="Probable fructose-6-phosphate aldolase"
FT                   /id="PRO_1000198462"
FT   ACT_SITE        87
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00496"
SQ   SEQUENCE   222 AA;  24374 MW;  AF21B55217E084B6 CRC64;
     MEFMLDTLNL DEIKKWSEIL PLAGVTSNPT IAKREGSINF FERIKDVREL IGSTPSIHVQ
     VISQDFEGIL KDAHKIRRQA GDDIFIKVPV TPAGLRAIKA LKKEGYHITA TAIYTVIQGL
     LAIEAGADYL APYYNRMENL NIDSNSVIRQ LALAIDRQNS PSKILAASFK NVAQVNNALA
     AGAHAVTAGA DVFESAFAMP SIQKAVDDFS DDWFVIQNSR SI