ID ALF1_ECOLI Reviewed; 350 AA.
AC P0A991; P71295; P76416; Q2MAX2;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=Fructose-bisphosphate aldolase class 1;
DE EC=4.1.2.13 {ECO:0000269|PubMed:9278503};
DE AltName: Full=Fructose-bisphosphate aldolase class I;
DE Short=FBP aldolase;
GN Name=fbaB; Synonyms=dhnA; OrderedLocusNames=b2097, JW5344;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Close T.J., Choi D.W.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
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 PROTEIN SEQUENCE OF 2-10, MASS SPECTROMETRY, SUBUNIT, CATALYTIC ACTIVITY,
RP FUNCTION, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP LYS-237 AND LYS-239.
RX PubMed=9531482; DOI=10.1042/bj3310437;
RA Thomson G.J., Howlett G.J., Ashcroft A.E., Berry A.;
RT "The dhnA gene of Escherichia coli encodes a class I fructose bisphosphate
RT aldolase.";
RL Biochem. J. 331:437-445(1998).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-208 AND LYS-262, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
CC -!- FUNCTION: Catalyzes the reversible aldol condensation/cleavage reaction
CC between glyceraldehyde 3-phosphate and dihydroxyacetone phosphate
CC (DHAP) to yield fructose-bisphosphate (FBP).
CC {ECO:0000269|PubMed:9531482}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13;
CC Evidence={ECO:0000269|PubMed:9531482};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14730;
CC Evidence={ECO:0000269|PubMed:9531482};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14731;
CC Evidence={ECO:0000269|PubMed:9531482};
CC -!- ACTIVITY REGULATION: Activated by citrate.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20 uM for FBP {ECO:0000269|PubMed:9531482};
CC -!- SUBUNIT: Homooctamer or homodecamer. {ECO:0000269|PubMed:9531482}.
CC -!- INTERACTION:
CC P0A991; P0A991: fbaB; NbExp=2; IntAct=EBI-545269, EBI-545269;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=37979.3; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9531482};
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. FbaB subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally (Ref.1) thought to be a dehydrin.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18249.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U73760; AAB18249.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75158.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76584.1; -; Genomic_DNA.
DR RefSeq; NP_416600.4; NC_000913.3.
DR RefSeq; WP_000129551.1; NZ_STEB01000002.1.
DR AlphaFoldDB; P0A991; -.
DR SMR; P0A991; -.
DR BioGRID; 4261525; 6.
DR DIP; DIP-36197N; -.
DR IntAct; P0A991; 5.
DR STRING; 511145.b2097; -.
DR iPTMnet; P0A991; -.
DR jPOST; P0A991; -.
DR PaxDb; 511145-b2097; -.
DR EnsemblBacteria; AAC75158; AAC75158; b2097.
DR GeneID; 75205967; -.
DR GeneID; 946632; -.
DR KEGG; ecj:JW5344; -.
DR KEGG; eco:b2097; -.
DR PATRIC; fig|1411691.4.peg.150; -.
DR EchoBASE; EB3815; -.
DR eggNOG; COG1830; Bacteria.
DR HOGENOM; CLU_057069_0_0_6; -.
DR InParanoid; P0A991; -.
DR OMA; RYQVLNC; -.
DR OrthoDB; 9769559at2; -.
DR PhylomeDB; P0A991; -.
DR BioCyc; EcoCyc:FRUCBISALD-CLASSI-MONOMER; -.
DR BioCyc; MetaCyc:FRUCBISALD-CLASSI-MONOMER; -.
DR SABIO-RK; P0A991; -.
DR PRO; PR:P0A991; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR CDD; cd00958; DhnA; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR InterPro; IPR041720; FbaB-like.
DR PANTHER; PTHR47916:SF1; 3-HYDROXY-5-PHOSPHONOOXYPENTANE-2,4-DIONE THIOLASE-RELATED; 1.
DR PANTHER; PTHR47916; FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 1; 1.
DR Pfam; PF01791; DeoC; 1.
DR SMART; SM01133; DeoC; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Glycolysis; Lyase;
KW Reference proteome; Schiff base.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9531482"
FT CHAIN 2..350
FT /note="Fructose-bisphosphate aldolase class 1"
FT /id="PRO_0000138939"
FT ACT_SITE 237
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000269|PubMed:9531482"
FT MOD_RES 208
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 262
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MUTAGEN 237
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9531482"
FT MUTAGEN 239
FT /note="K->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:9531482"
FT CONFLICT 192
FT /note="L -> V (in Ref. 1; AAB18249)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="N -> I (in Ref. 1; AAB18249)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 38109 MW; 462341BE2459E587 CRC64;
MTDIAQLLGK DADNLLQHRC MTIPSDQLYL PGHDYVDRVM IDNNRPPAVL RNMQTLYNTG
RLAGTGYLSI LPVDQGVEHS AGASFAANPL YFDPKNIVEL AIEAGCNCVA STYGVLASVS
RRYAHRIPFL VKLNHNETLS YPNTYDQTLY ASVEQAFNMG AVAVGATIYF GSEESRRQIE
EISAAFERAH ELGMVTVLWA YLRNSAFKKD GVDYHVSADL TGQANHLAAT IGADIVKQKM
AENNGGYKAI NYGYTDDRVY SKLTSENPID LVRYQLANCY MGRAGLINSG GAAGGETDLS
DAVRTAVINK RAGGMGLILG RKAFKKSMAD GVKLINAVQD VYLDSKITIA
//
