FSAB_ECOL6
ID FSAB_ECOL6 Reviewed; 220 AA.
AC Q8FBA7;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Fructose-6-phosphate aldolase 2;
DE EC=4.1.2.-;
GN Name=fsaB; Synonyms=talC; OrderedLocusNames=c4905;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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 -!- SUBUNIT: Homodecamer. {ECO:0000250}.
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; AE014075; AAN83333.1; -; Genomic_DNA.
DR RefSeq; WP_000424855.1; NC_004431.1.
DR AlphaFoldDB; Q8FBA7; -.
DR SMR; Q8FBA7; -.
DR STRING; 199310.c4905; -.
DR EnsemblBacteria; AAN83333; AAN83333; c4905.
DR KEGG; ecc:c4905; -.
DR eggNOG; COG0176; Bacteria.
DR HOGENOM; CLU_079764_2_0_6; -.
DR OMA; QQMLGTP; -.
DR BioCyc; ECOL199310:C4905-MON; -.
DR Proteomes; UP000001410; 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 2"
FT /id="PRO_0000173647"
FT ACT_SITE 85
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 220 AA; 23523 MW; F2677146877D38EB CRC64;
MELYLDTANV AEVERLARIF PIAGVTTNPS IIAASKESIW EVLPRLQKAI GDEGILFAQT
MSRDAQGMVK EAKHLRDAIP GIVVKIPVTS EGLAAIKMLK KEGITTLGTA VYSAAQGLLA
ALAGAKYVAP YVNRVDAQGG DGIRTVQELQ ALLEMHAPES MVLAASFKTP RQALDCLLAG
CESITLPLDV AQQMLNTPAV ESAIEKFEHD WNAAFGTTHL