ID FSA_STRPN Reviewed; 222 AA.
AC Q97SS2;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=Probable fructose-6-phosphate aldolase;
DE EC=4.1.2.-;
GN Name=fsa; OrderedLocusNames=SP_0252;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 3A subfamily.
CC {ECO:0000305}.
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DR EMBL; AE005672; AAK74431.1; -; Genomic_DNA.
DR PIR; F95029; F95029.
DR RefSeq; WP_000395437.1; NZ_CP089948.1.
DR AlphaFoldDB; Q97SS2; -.
DR SMR; Q97SS2; -.
DR PaxDb; 170187-SP_0252; -.
DR EnsemblBacteria; AAK74431; AAK74431; SP_0252.
DR KEGG; spn:SP_0252; -.
DR eggNOG; COG0176; Bacteria.
DR PhylomeDB; Q97SS2; -.
DR BioCyc; SPNE170187:G1FZB-258-MONOMER; -.
DR Proteomes; UP000000585; 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; Aldolase class I; 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; TRANSALDOLASE; 1.
DR PANTHER; PTHR10683:SF28; TRANSALDOLASE C; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cytoplasm; Lyase; Reference proteome; Schiff base.
FT CHAIN 1..222
FT /note="Probable fructose-6-phosphate aldolase"
FT /id="PRO_0000173651"
FT ACT_SITE 87
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
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
//
