ID   ALF_ECOLI      STANDARD;      PRT;   358 AA.
AC   P11604;
DT   01-OCT-1989 (Rel. 12, Created)
DT   01-JAN-1990 (Rel. 13, Last sequence update)
DT   15-JUN-2002 (Rel. 41, Last annotation update)
DE   Fructose-bisphosphate aldolase class II (EC 4.1.2.13) (FBP aldolase).
GN   FBAA OR FBA OR FDA OR B2925 OR Z4263 OR ECS3796.
OS   Escherichia coli, and
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae;
OC   Escherichia.
OX   NCBI_TaxID=562, 83334;
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12 / CS520;
RX   MEDLINE=89313302; PubMed=2546007;
RA   Alefounder P.R., Baldwin S.A., Perham S.A., Short N.J.;
RT   "Identification, molecular cloning and sequence analysis of a gene
RT   cluster encoding the class II fructose 1,6-bisphosphate aldolase, 3-
RT   phosphoglycerate kinase and a putative second glyceraldehyde 3-
RT   phosphate dehydrogenase of Escherichia coli.";
RL   Mol. Microbiol. 3:723-732(1989).
RN   [2]
RP   SEQUENCE FROM N.A., AND SEQUENCE OF 1-26.
RX   MEDLINE=89193446; PubMed=2649077;
RA   Alefounder P.R., Baldwin S.A., Perham R.N., Short N.J.;
RT   "Cloning, sequence analysis and over-expression of the gene for the
RT   class II fructose 1,6-bisphosphate aldolase of Escherichia coli.";
RL   Biochem. J. 257:529-534(1989).
RN   [3]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12 / MG1655;
RX   MEDLINE=97426617; PubMed=9278503;
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   [4]
RP   SEQUENCE FROM N.A.
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927;
RX   MEDLINE=21074935; PubMed=11206551;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [5]
RP   SEQUENCE FROM N.A.
RC   STRAIN=O157:H7 / RIMD 0509952;
RX   MEDLINE=21156231; PubMed=11258796;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
RN   [6]
RP   SEQUENCE OF 1-12.
RC   STRAIN=K12 / EMG2;
RX   MEDLINE=97443975; PubMed=9298646;
RA   Link A.J., Robison K., Church G.M.;
RT   "Comparing the predicted and observed properties of proteins encoded
RT   in the genome of Escherichia coli K-12.";
RL   Electrophoresis 18:1259-1313(1997).
RN   [7]
RP   ZINC-LIGANDS, AND MUTAGENESIS.
RX   MEDLINE=93170474; PubMed=8436219;
RA   Berry A., Marshall K.E.;
RT   "Identification of zinc-binding ligands in the class II fructose-1,6-
RT   bisphosphate aldolase of Escherichia coli.";
RL   FEBS Lett. 318:11-16(1993).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS).
RX   MEDLINE=96433074; PubMed=8836102;
RA   Blom N.S., Tetreault S., Coulombe R., Sygusch J.;
RT   "Novel active site in Escherichia coli fructose 1,6-bisphosphate
RT   aldolase.";
RL   Nat. Struct. Biol. 3:856-862(1996).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   MEDLINE=97094986; PubMed=8939754;
RA   Cooper S.J., Leonard G.A., McSweeney S.M., Thompson A.W.,
RA   Naismith J.H., Qamar S., Plater A., Berry A., Hunter W.N.;
RT   "The crystal structure of a class II fructose-1,6-bisphosphate
RT   aldolase shows a novel binuclear metal-binding active site embedded
RT   in a familiar fold.";
RL   Structure 4:1303-1315(1996).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   MEDLINE=99182425; PubMed=10080900;
RA   Hall D.R., Leonard G.A., Reed C.D., Watt C.I., Berry A., Hunter W.N.;
RT   "The crystal structure of Escherichia coli class II fructose-1,
RT   6-bisphosphate aldolase in complex with phosphoglycolohydroxamate
RT   reveals details of mechanism and specificity.";
RL   J. Mol. Biol. 287:383-394(1999).
CC   -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone
CC       phosphate + D-glyceraldehyde 3-phosphate.
CC   -!- COFACTOR: ZINC.
CC   -!- PATHWAY: Glycolysis; sixth step.
CC   -!- SUBUNIT: HOMODIMER.
CC   -!- SIMILARITY: BELONGS TO CLASS II FRUCTOSE-BISPHOSPHATE ALDOLASE
CC       FAMILY.
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DR   EMBL; X14436; CAA32605.1; -.
DR   EMBL; U28377; AAA69092.1; -.
DR   EMBL; AE000376; AAC75962.1; -.
DR   EMBL; AE005522; AAG58051.1; ALT_INIT.
DR   EMBL; AP002563; BAB37219.1; -.
DR   PIR; S02177; ADEC2A.
DR   PDB; 1DOS; 07-JUL-97.
DR   PDB; 1ZEN; 07-JUL-97.
DR   PDB; 1B57; 07-JAN-00.
DR   SWISS-2DPAGE; P11604; COLI.
DR   EcoGene; EG10282; fbaA.
DR   InterPro; IPR000771; F_bP_aldolase.
DR   Pfam; PF01116; F_bP_aldolase; 1.
DR   ProDom; PD002376; F_bP_aldolase; 1.
DR   TIGRFAMs; TIGR00167; cbbA; 1.
DR   PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1.
DR   PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
KW   Lyase; Glycolysis; Zinc; 3D-structure; Complete proteome.
FT   INIT_MET      0      0
FT   METAL       107    107       ZINC.
FT   METAL       110    110       ZINC.
FT   MUTAGEN     107    107       H->A: LOSS OF ACTIVITY.
FT   MUTAGEN     110    110       H->A: LOSS OF ACTIVITY.
FT   MUTAGEN     111    111       C->A: PARTIAL LOSS OF ACTIVITY.
SQ   SEQUENCE   358 AA;  39016 MW;  ED5A0FDC66246031 CRC64;
     SKIFDFVKPG VITGDDVQKV FQVAKENNFA LPAVNCVGTD SINAVLETAA KVKAPVIVQF
     SNGGASFIAG KGVKSDVPQG AAILGAISGA HHVHQMAEHY GVPVILHTDH CAKKLLPWID
     GLLDAGEKHF AATGKPLFSS HMIDLSEESL QENIEICSKY LERMSKIGMT LEIELGCTGG
     EEDGVDNSHM DASALYTQPE DVDYAYTELS KISPRFTIAA SFGNVHGVYK PGNVVLTPTI
     LRDSQEYVSK KHNLPHNSLN FVFHGGSGST AQEIKDSVSY GVVKMNIDTD TQWATWEGVL
     NYYKANEAYL QGQLGNPKGE DQPNKKYYDP RVWLRAGQTS MIARLEKAFQ ELNAIDVL
//