FSAB_ECOLI
ID FSAB_ECOLI Reviewed; 220 AA.
AC P32669; Q2M8P2;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Fructose-6-phosphate aldolase 2;
DE EC=4.1.2.-;
DE AltName: Full=Fructose-6-phosphate aldolase B;
DE Short=FSAB;
GN Name=fsaB; Synonyms=talC, yijG; OrderedLocusNames=b3946, JW3918;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [2]
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 [3]
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 [4]
RP DISCUSSION OF SEQUENCE.
RX PubMed=7773398; DOI=10.1099/13500872-141-4-961;
RA Reizer J., Reizer A., Saier M.H. Jr.;
RT "Novel phosphotransferase system genes revealed by bacterial genome
RT analysis -- a gene cluster encoding a unique Enzyme I and the proteins of a
RT fructose-like permease system.";
RL Microbiology 141:961-971(1995).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND 3D-STRUCTURE MODELING.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX DOI=10.1016/j.molcatb.2012.02.010;
RA Sanchez-Moreno I., Nauton L., Thery V., Pinet A., Petit J.-L.,
RA de Berardinis V., Samland A.K., Guerard-Helaine C., Lemaire M.;
RT "FSAB: A new fructose-6-phosphate aldolase from Escherichia coli. Cloning,
RT over-expression and comparative kinetic characterization with FSAA.";
RL J. Mol. Catal., B Enzym. 84:9-14(2012).
CC -!- FUNCTION: Catalyzes the reversible formation of fructose 6-phosphate
CC from dihydroxyacetone and D-glyceraldehyde 3-phosphate via an
CC aldolization reaction. Can utilize hydroxyacetone as an alternative
CC donor substrate. Is also able to catalyze the direct self-aldol
CC addition of glycolaldehyde. Is less catalytically efficient than the
CC isozyme FsaA. Does not display transaldolase activity.
CC {ECO:0000269|PubMed:11120740, 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|Ref.6};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=27 mM for dihydroxyacetone {ECO:0000269|Ref.6};
CC KM=15 mM for hydroxyacetone {ECO:0000269|Ref.6};
CC KM=0.28 mM for glycolaldehyde (as donor substrate in the self-aldol
CC addition of glycolaldehyde) {ECO:0000269|Ref.6};
CC KM=65 mM for glycolaldehyde (as acceptor substrate in the self-aldol
CC addition of glycolaldehyde) {ECO:0000269|Ref.6};
CC KM=0.65 mM for D,L-glyceraldehyde 3-phosphate {ECO:0000269|Ref.6};
CC KM=6.70 mM for D-fructose 6-phosphate {ECO:0000269|Ref.6};
CC KM=210 mM for D-fructose {ECO:0000269|Ref.6};
CC KM=271 mM for D-sorbose {ECO:0000269|Ref.6};
CC Note=Catalytic efficiency is 28-fold higher using glyceraldehyde 3-
CC phosphate as acceptor substrate and hydroxyacetone as donor substrate
CC than with dihydroxyacetone as the donor.;
CC pH dependence:
CC Optimum pH is 8.5 for the retroaldol activity on F6P.
CC {ECO:0000269|Ref.6};
CC Temperature dependence:
CC Is not thermally stable at temperatures higher than 60 degrees
CC Celsius. Is less thermostable than the isozyme FsaA.
CC {ECO:0000269|Ref.6};
CC -!- SUBUNIT: Homodecamer. {ECO:0000269|Ref.6}.
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; U00006; AAC43052.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76928.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77364.1; -; Genomic_DNA.
DR PIR; E65201; E65201.
DR RefSeq; NP_418381.1; NC_000913.3.
DR RefSeq; WP_000424840.1; NZ_SSZK01000014.1.
DR AlphaFoldDB; P32669; -.
DR SMR; P32669; -.
DR BioGRID; 4263139; 18.
DR BioGRID; 852736; 3.
DR IntAct; P32669; 5.
DR STRING; 511145.b3946; -.
DR PaxDb; P32669; -.
DR PRIDE; P32669; -.
DR EnsemblBacteria; AAC76928; AAC76928; b3946.
DR EnsemblBacteria; BAE77364; BAE77364; BAE77364.
DR GeneID; 58461015; -.
DR GeneID; 948439; -.
DR KEGG; ecj:JW3918; -.
DR KEGG; eco:b3946; -.
DR PATRIC; fig|1411691.4.peg.2758; -.
DR EchoBASE; EB1850; -.
DR eggNOG; COG0176; Bacteria.
DR HOGENOM; CLU_079764_2_0_6; -.
DR InParanoid; P32669; -.
DR OMA; QQMLGTP; -.
DR PhylomeDB; P32669; -.
DR BioCyc; EcoCyc:EG11905-MON; -.
DR BioCyc; MetaCyc:EG11905-MON; -.
DR PRO; PR:P32669; -.
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 Carbohydrate metabolism; Cytoplasm; Lyase; Reference proteome; Schiff base.
FT CHAIN 1..220
FT /note="Fructose-6-phosphate aldolase 2"
FT /id="PRO_0000173646"
FT ACT_SITE 85
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 220 AA; 23555 MW; 95D72DFD475BDE7B CRC64;
MELYLDTANV AEVERLARIF PIAGVTTNPS IIAASKESIW EVLPRLQKAI GDEGILFAQT
MSRDAQGMVE EAKRLRDAIP GIVVKIPVTS EGLAAIKILK KEGITTLGTA VYSAAQGLLA
ALAGAKYVAP YVNRVDAQGG DGIRTVQELQ TLLEMHAPES MVLAASFKTP RQALDCLLAG
CESITLPLDV AQQMLNTPAV ESAIEKFEHD WNAAFGTTHL
