FSA_SALTI
ID FSA_SALTI Reviewed; 220 AA.
AC Q8Z305;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 114.
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}; Synonyms=talC;
GN OrderedLocusNames=STY3758, t3508;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD09513.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO71016.1; -; Genomic_DNA.
DR RefSeq; NP_457943.1; NC_003198.1.
DR RefSeq; WP_000424865.1; NZ_WSUR01000010.1.
DR AlphaFoldDB; Q8Z305; -.
DR SMR; Q8Z305; -.
DR STRING; 220341.16504630; -.
DR EnsemblBacteria; AAO71016; AAO71016; t3508.
DR KEGG; stt:t3508; -.
DR KEGG; sty:STY3758; -.
DR PATRIC; fig|220341.7.peg.3832; -.
DR eggNOG; COG0176; Bacteria.
DR HOGENOM; CLU_079764_2_0_6; -.
DR OMA; QQMLGTP; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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_0000173649"
FT ACT_SITE 85
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00496"
SQ SEQUENCE 220 AA; 23510 MW; 332312F47A808867 CRC64;
MELYLDTANV AEVERLARIF PIAGVTTNPS IVAASKESIW DVLPRLQNAI GEEGTLFAQT
MSRDAKGMVE EAKRLNNAIP GIVVKIPVTA EGLAAIKLLK KEGIVTLGTA VYSASQGLLA
ALAGAKYVAP YVNRVDAQGG DGIRMVLELQ TLLEHHAPDS MVLAASFKTP RQALDCLLAG
CQAITLPLDV AQQMLNTPAV ESAIEKFEQD WKNAFGNLNL