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   16-JUN-2009, entry version 32.
DE   RecName: Full=Fructose-bisphosphate aldolase class 1;
DE            EC=4.1.2.13;
DE   AltName: Full=Fructose-biphosphate aldolase class I;
DE            Short=FBP aldolase;
GN   Name=fbaB; Synonyms=dhnA; OrderedLocusNames=b2097, JW5344;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
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   MEDLINE=97426617; 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.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(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
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-10, CHARACTERIZATION, AND MASS SPECTROMETRY.
RX   MEDLINE=98198380; PubMed=9531482;
RA   Thomson G.J., Howlett G.J., Ashcroft A.E., Berry A.;
RT   "The dhnA gene of Escherichia coli encodes a class I fructose
RT   bisphosphate aldolase.";
RL   Biochem. J. 331:437-445(1998).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-208 AND LYS-262, AND MASS
RP   SPECTROMETRY.
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   -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone
CC       phosphate + D-glyceraldehyde 3-phosphate.
CC   -!- ENZYME REGULATION: Activated by citrate.
CC   -!- SUBUNIT: Homooctamer or homodecamer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- MASS SPECTROMETRY: Mass=37979.3; Method=MALDI; Range=2-350;
CC       Source=PubMed:9531482;
CC   -!- SIMILARITY: Belongs to the deoC/fbaB aldolase family. FbaB
CC       subfamily.
CC   -!- CAUTION: Was originally (Ref.1) thought to be a dehydrin.
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DR   EMBL; U73760; AAB18249.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC75158.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP009048; BAE76584.1; -; Genomic_DNA.
DR   RefSeq; AP_002695.1; -.
DR   RefSeq; NP_416600.4; -.
DR   GeneID; 946632; -.
DR   GenomeReviews; AP009048_GR; JW5344.
DR   GenomeReviews; U00096_GR; b2097.
DR   KEGG; ecj:JW5344; -.
DR   KEGG; eco:b2097; -.
DR   EchoBASE; EB3815; -.
DR   EcoGene; EG14062; fbaB.
DR   HOGENOM; P0A991; -.
DR   OMA; P0A991; FTIYPGS.
DR   BioCyc; EcoCyc:FRUCBISALD-CLASSI-MON; -.
DR   BioCyc; MetaCyc:FRUCBISALD-CLASSI-MON; -.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002915; DeoC/AroFGH_arch.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   Pfam; PF01791; DeoC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Glycolysis; Lyase; Schiff base.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    350       Fructose-bisphosphate aldolase class 1.
FT                                /FTId=PRO_0000138939.
FT   ACT_SITE    237    237       Schiff-base intermediate with
FT                                dihydroxyacetone-P.
FT   MOD_RES     208    208       N6-acetyllysine.
FT   MOD_RES     262    262       N6-acetyllysine.
FT   MUTAGEN     237    237       K->A: Loss of activity.
FT   MUTAGEN     239    239       K->A: No change in activity.
FT   CONFLICT    192    192       L -> V (in Ref. 1; AAB18249).
FT   CONFLICT    309    309       N -> I (in Ref. 1; AAB18249).
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
//