FSAA_ECOLI
ID FSAA_ECOLI Reviewed; 220 AA.
AC P78055; P77855; Q9R3X3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Fructose-6-phosphate aldolase 1;
DE EC=4.1.2.-;
DE AltName: Full=Fructose-6-phosphate aldolase A;
DE Short=FSAA;
GN Name=fsaA; Synonyms=fsa, mipB, ybiZ; OrderedLocusNames=b0825, JW5109;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RA Isomura M., Ogino T., Mizuno T.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MASS
RP SPECTROMETRY, SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF LYS-85.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11120740; DOI=10.1074/jbc.m008061200;
RA Schuermann M., Sprenger G.A.;
RT "Fructose-6-phosphate aldolase is a novel class I aldolase from Escherichia
RT coli and is related to a novel group of bacterial transaldolases.";
RL J. Biol. Chem. 276:11055-11061(2001).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOTECHNOLOGY.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RA Schuermann M., Schuermann M., Sprenger G.A.;
RT "Fructose-6-phosphate aldolase and 1-deoxy-D-xylulose 5-phosphate synthase
RT from Escherichia coli as tools in enzymatic synthesis of 1-deoxysugars.";
RL J. Mol. Catal., B Enzym. 19:247-252(2002).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS,
RP AND BIOTECHNOLOGY.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=17985886; DOI=10.1021/ja073911i;
RA Sugiyama M., Hong Z., Liang P.H., Dean S.M., Whalen L.J., Greenberg W.A.,
RA Wong C.H.;
RT "D-Fructose-6-phosphate aldolase-catalyzed one-pot synthesis of
RT iminocyclitols.";
RL J. Am. Chem. Soc. 129:14811-14817(2007).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS,
RP AND BIOTECHNOLOGY.
RX PubMed=19554584; DOI=10.1002/anie.200902065;
RA Garrabou X., Castillo J.A., Guerard-Helaine C., Parella T., Joglar J.,
RA Lemaire M., Clapes P.;
RT "Asymmetric self- and cross-aldol reactions of glycolaldehyde catalyzed by
RT D-fructose-6-phosphate aldolase.";
RL Angew. Chem. Int. Ed. 48:5521-5525(2009).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS), ACTIVE SITE, AND SUBUNIT.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12051943; DOI=10.1016/s0022-2836(02)00258-9;
RA Thorell S., Schurmann M., Sprenger G.A., Schneider G.;
RT "Crystal structure of decameric fructose-6-phosphate aldolase from
RT Escherichia coli reveals inter-subunit helix swapping as a structural basis
RT for assembly differences in the transaldolase family.";
RL J. Mol. Biol. 319:161-171(2002).
CC -!- FUNCTION: Catalyzes the reversible formation of fructose 6-phosphate
CC from dihydroxyacetone (DHA) and D-glyceraldehyde 3-phosphate via an
CC aldolization reaction. Can utilize several aldehydes as acceptor
CC compounds in vitro, and hydroxyacetone (HA) or 1-hydroxy-butan-2-one as
CC alternative donor substrate. Is also able to catalyze the direct
CC stereoselective self-aldol addition of glycolaldehyde to furnish D-(-)-
CC threose, and cross-aldol reactions of glycolaldehyde to other aldehyde
CC acceptors. Is not able to cleave fructose, fructose 1-phosphate,
CC glucose 6-phosphate, sedoheptulose 1,7-bisphosphate, xylulose 5-
CC phosphate, ribulose 5-phosphate, and fructose 1,6-bisphosphate; cannot
CC use dihydroxyacetone phosphate as donor compound nor D-glyceraldehyde
CC as acceptor. Does not display transaldolase activity.
CC {ECO:0000269|PubMed:11120740, ECO:0000269|PubMed:17985886,
CC ECO:0000269|PubMed:19554584, ECO:0000269|Ref.6}.
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 Evidence={ECO:0000269|PubMed:11120740, ECO:0000269|PubMed:17985886,
CC ECO:0000269|PubMed:19554584, ECO:0000269|Ref.6};
CC -!- ACTIVITY REGULATION: Inhibited by glycerol, inorganic phosphate and
CC arabinose 5-phosphate. {ECO:0000269|PubMed:11120740}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9 mM for D-fructose 6-phosphate (at 30 degrees Celsius and pH 8.5)
CC {ECO:0000269|PubMed:11120740};
CC KM=35 mM for dihydroxyacetone (at 30 degrees Celsius and pH 8.5)
CC {ECO:0000269|PubMed:11120740};
CC KM=0.8 mM for glyceraldehyde 3-phosphate (at 30 degrees Celsius and
CC pH 8.5) {ECO:0000269|PubMed:11120740};
CC KM=40 mM for dihydroxyacetone (at 25 degrees Celsius and pH 8.5)
CC {ECO:0000269|PubMed:17985886};
CC KM=11 mM for hydroxyacetone (at 25 degrees Celsius and pH 8.5)
CC {ECO:0000269|PubMed:17985886};
CC KM=32 mM for 1-hydroxy-butan-2-one (at 25 degrees Celsius and pH 8.5)
CC {ECO:0000269|PubMed:17985886};
CC KM=32 mM for dihydroxyacetone {ECO:0000269|PubMed:19554584};
CC KM=17.4 mM for hydroxyacetone {ECO:0000269|PubMed:19554584};
CC KM=0.197 mM for glycolaldehyde (as donor substrate in the self-aldol
CC addition of glycolaldehyde) {ECO:0000269|PubMed:19554584};
CC KM=62.8 mM for glycolaldehyde (as acceptor substrate in the self-
CC aldol addition of glycolaldehyde) {ECO:0000269|PubMed:19554584};
CC KM=0.286 mM for D-threose {ECO:0000269|PubMed:19554584};
CC KM=0.561 mM for D-arabinose-5-P {ECO:0000269|PubMed:19554584};
CC Vmax=45 umol/min/mg enzyme for the aldolization reaction leading to
CC D-fructose 6-phosphate (at 30 degrees Celsius and pH 8.5)
CC {ECO:0000269|PubMed:11120740};
CC Vmax=7 umol/min/mg enzyme for D-fructose 6-phosphate cleavage (at 30
CC degrees Celsius and pH 8.5) {ECO:0000269|PubMed:11120740};
CC Vmax=1.46 umol/min/mg enzyme for the aldol reaction with DHA and D,L-
CC glyceraldehyde 3-phosphate as substrates
CC {ECO:0000269|PubMed:19554584};
CC Vmax=33.7 umol/min/mg enzyme for the aldol reaction with HA and D,L-
CC glyceraldehyde 3-phosphate as substrates
CC {ECO:0000269|PubMed:19554584};
CC Vmax=0.22 umol/min/mg enzyme for the self-aldol addition of
CC glycolaldehyde {ECO:0000269|PubMed:19554584};
CC Vmax=0.34 umol/min/mg enzyme for D-fructose 6-phosphate cleavage
CC {ECO:0000269|PubMed:19554584};
CC Vmax=0.160 umol/min/mg enzyme for D-arabinose-5-P cleavage
CC {ECO:0000269|PubMed:19554584};
CC Note=kcat is 1.31 sec(-1), 0.82 sec(-1) and 0.63 sec(-1) using
CC glyceraldehyde 3-phosphate as acceptor substrate, and
CC dihydroxyacetone, hydroxyacetone or 1-hydroxy-butan-2-one as donor
CC substrate, respectively (at 25 degrees Celsius and pH 8.5).
CC {ECO:0000269|PubMed:17985886};
CC pH dependence:
CC Optimum pH is about 8.5. Active from pH 6 to 12.
CC {ECO:0000269|PubMed:11120740};
CC Temperature dependence:
CC Displays a broad temperature optimum and is active in the range from
CC 20 to 75 degrees Celsius. Although no significant loss of activity is
CC detected after 600 hours of incubation at 45 degrees Celsius (at pH
CC 8.0), the respective half-lives of the enzyme are 200 hours at 55
CC degrees Celsius, 30 hours at 65 degrees Celsius, and 16 hours at 75
CC degrees Celsius. {ECO:0000269|PubMed:11120740};
CC -!- SUBUNIT: Homodecamer. Five subunits are arranged as a pentamer, and two
CC ring-like pentamers pack like a donut to form the decamer.
CC {ECO:0000269|PubMed:11120740, ECO:0000269|PubMed:12051943}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MASS SPECTROMETRY: Mass=22998; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11120740};
CC -!- BIOTECHNOLOGY: Is an interesting tool in chemoenzymatic synthesis for
CC the construction of chiral complex polyhydroxylated sugar-type
CC structures. The use of hydroxyacetone (acetol) as a donor compound
CC allows access to various 1-deoxysugars. Can also be used for the
CC synthesis of a broad range of iminocyclitols, that are potent
CC glycosidase and glycosyltransferase inhibitors, from dihydroxyacetone,
CC hydroxyacetone or 1-hydroxy-butan-2-one as donor substrate, and a range
CC of acceptor substrates. {ECO:0000269|PubMed:17985886,
CC ECO:0000269|PubMed:19554584, ECO:0000269|Ref.6}.
CC -!- MISCELLANEOUS: Is not inhibited by EDTA which points to a metal-
CC independent mode of action. {ECO:0000305|PubMed:11120740}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 3A subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D88188; BAA13552.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73912.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA35513.2; -; Genomic_DNA.
DR PIR; A64820; A64820.
DR RefSeq; NP_415346.4; NC_000913.3.
DR RefSeq; WP_001336208.1; NZ_SSZK01000002.1.
DR PDB; 1L6W; X-ray; 1.93 A; A/B/C/D/E/F/G/H/I/J=1-220.
DR PDB; 4RXF; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J=2-220.
DR PDB; 4RXG; X-ray; 2.15 A; A/B/C/D/E/F/G/H/I/J=1-220.
DR PDB; 4RZ4; X-ray; 1.75 A; A/B/C/D/E/F/G/H/I/J=2-220.
DR PDB; 4S1F; X-ray; 2.24 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=2-220.
DR PDB; 5ZOL; X-ray; 2.17 A; A/B/C/D/E/F/G/H/I/J=1-220.
DR PDBsum; 1L6W; -.
DR PDBsum; 4RXF; -.
DR PDBsum; 4RXG; -.
DR PDBsum; 4RZ4; -.
DR PDBsum; 4S1F; -.
DR PDBsum; 5ZOL; -.
DR AlphaFoldDB; P78055; -.
DR SMR; P78055; -.
DR BioGRID; 4263503; 3.
DR DIP; DIP-10218N; -.
DR IntAct; P78055; 1.
DR STRING; 511145.b0825; -.
DR jPOST; P78055; -.
DR PaxDb; P78055; -.
DR PRIDE; P78055; -.
DR EnsemblBacteria; AAC73912; AAC73912; b0825.
DR EnsemblBacteria; BAA35513; BAA35513; BAA35513.
DR GeneID; 945449; -.
DR KEGG; ecj:JW5109; -.
DR KEGG; eco:b0825; -.
DR PATRIC; fig|1411691.4.peg.1453; -.
DR EchoBASE; EB3244; -.
DR eggNOG; COG0176; Bacteria.
DR HOGENOM; CLU_079764_2_0_6; -.
DR InParanoid; P78055; -.
DR OMA; VRHPMHV; -.
DR PhylomeDB; P78055; -.
DR BioCyc; EcoCyc:G6428-MON; -.
DR BioCyc; MetaCyc:G6428-MON; -.
DR SABIO-RK; P78055; -.
DR EvolutionaryTrace; P78055; -.
DR PRO; PR:P78055; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097023; F:fructose 6-phosphate aldolase activity; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm;
KW Direct protein sequencing; Lyase; Reference proteome; Schiff base.
FT CHAIN 1..220
FT /note="Fructose-6-phosphate aldolase 1"
FT /id="PRO_0000173643"
FT ACT_SITE 85
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000269|PubMed:11120740,
FT ECO:0000269|PubMed:12051943"
FT MUTAGEN 85
FT /note="K->R: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11120740"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:4RZ4"
FT HELIX 10..17
FT /evidence="ECO:0007829|PDB:4RZ4"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:4RZ4"
FT HELIX 29..35
FT /evidence="ECO:0007829|PDB:4RZ4"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:4RZ4"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:4RZ4"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:4RZ4"
FT HELIX 65..78
FT /evidence="ECO:0007829|PDB:4RZ4"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:4RZ4"
FT HELIX 90..101
FT /evidence="ECO:0007829|PDB:4RZ4"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:4RZ4"
FT HELIX 114..123
FT /evidence="ECO:0007829|PDB:4RZ4"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:4RZ4"
FT HELIX 132..137
FT /evidence="ECO:0007829|PDB:4RZ4"
FT HELIX 142..156
FT /evidence="ECO:0007829|PDB:4RZ4"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:4RZ4"
FT HELIX 170..178
FT /evidence="ECO:0007829|PDB:4RZ4"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:4RZ4"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:4RZ4"
FT HELIX 198..215
FT /evidence="ECO:0007829|PDB:4RZ4"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:4RZ4"
SQ SEQUENCE 220 AA; 22997 MW; 317B9A06CD19C587 CRC64;
MELYLDTSDV VAVKALSRIF PLAGVTTNPS IIAAGKKPLD VVLPQLHEAM GGQGRLFAQV
MATTAEGMVN DALKLRSIIA DIVVKVPVTA EGLAAIKMLK AEGIPTLGTA VYGAAQGLLS
ALAGAEYVAP YVNRIDAQGG SGIQTVTDLH QLLKMHAPQA KVLAASFKTP RQALDCLLAG
CESITLPLDV AQQMISYPAV DAAVAKFEQD WQGAFGRTSI
