ID   ALF2_STAAS              Reviewed;         286 AA.
AC   Q6G7I5;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=Fructose-bisphosphate aldolase;
DE            Short=FBP aldolase;
DE            Short=FBPA;
DE            EC=4.1.2.13;
DE   AltName: Full=Fructose-1,6-bisphosphate aldolase;
GN   Name=fba; Synonyms=fbaA; OrderedLocusNames=SAS2028;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T.,
RA   Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
RA   Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
RA   James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
RA   Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
RA   Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
RA   Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains:
RT   evidence for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Catalyzes the aldol condensation of dihydroxyacetone
CC       phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-
CC       phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in
CC       gluconeogenesis and the reverse reaction in glycolysis (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone
CC       phosphate + D-glyceraldehyde 3-phosphate.
CC   -!- COFACTOR: Binds 2 zinc ions per subunit. One is catalytic and the
CC       other provides a structural contribution (By similarity).
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 4/4.
CC   -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC       family.
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DR   EMBL; BX571857; CAG43836.1; -; Genomic_DNA.
DR   RefSeq; YP_044139.1; -.
DR   GeneID; 2862268; -.
DR   GenomeReviews; BX571857_GR; SAS2028.
DR   KEGG; sas:SAS2028; -.
DR   HOGENOM; Q6G7I5; -.
DR   OMA; Q6G7I5; IGKMREF.
DR   BioCyc; SAUR282459:SAS2028-MON; -.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011289; Fruc_bis_ald_.
DR   InterPro; IPR000771; Ketose_bisP_aldolase_II.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   Pfam; PF01116; F_bP_aldolase; 1.
DR   PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR   ProDom; PD002376; K_bP_aldolase; 1.
DR   TIGRFAMs; TIGR00167; cbbA; 1.
DR   TIGRFAMs; TIGR01859; fruc_bis_ald_; 1.
DR   PROSITE; PS00602; ALDOLASE_CLASS_II_1; FALSE_NEG.
DR   PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glycolysis; Lyase; Metal-binding; Zinc.
FT   CHAIN         1    286       Fructose-bisphosphate aldolase.
FT                                /FTId=PRO_0000178739.
FT   REGION      210    212       Dihydroxyacetone phosphate binding (By
FT                                similarity).
FT   REGION      231    234       Dihydroxyacetone phosphate binding (By
FT                                similarity).
FT   ACT_SITE     85     85       Proton donor (By similarity).
FT   METAL        86     86       Zinc 1; catalytic (By similarity).
FT   METAL       107    107       Zinc 2 (By similarity).
FT   METAL       137    137       Zinc 2 (By similarity).
FT   METAL       181    181       Zinc 1; catalytic (By similarity).
FT   METAL       209    209       Zinc 1; catalytic (By similarity).
FT   BINDING      50     50       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     182    182       Dihydroxyacetone phosphate; via amide
FT                                nitrogen (By similarity).
SQ   SEQUENCE   286 AA;  30836 MW;  7A5FD0EBD48283D9 CRC64;
     MPLVSMKEML IDAKENGYAV GQYNINNLEF TQAILEASQE ENAPVILGVS EGAARYMSGF
     YTIVKMVEGL MHDLNITIPV AIHLDHGSSF EKCKEAIDAG FTSVMIDASH SPFEENVATT
     KKVVEYAHEK GVSVEAELGT VGGQEDDVVA DGIIYADPKE CQELVEKTGI DALAPALGSV
     HGPYKGEPKL GFKEMEEIGL STGLPLVLHG GTGIPTKDIQ KAIPFGTAKI NVNTENQIAS
     AKAVRDVLNN DKEVYDPRKY LGPAREAIKE TVKGKIKEFG TSNRAK
//