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};
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; 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
//