ID   ALF1_STAAS              Reviewed;         296 AA.
AC   Q6G670;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Fructose-bisphosphate aldolase class 1 {ECO:0000255|HAMAP-Rule:MF_00729};
DE            EC=4.1.2.13 {ECO:0000255|HAMAP-Rule:MF_00729};
DE   AltName: Full=Fructose-bisphosphate aldolase class I;
DE            Short=FBP aldolase {ECO:0000255|HAMAP-Rule:MF_00729};
GN   Name=fda {ECO:0000255|HAMAP-Rule:MF_00729}; OrderedLocusNames=SAS2491;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
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., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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:0000255|HAMAP-Rule:MF_00729};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 4/4.
CC       {ECO:0000255|HAMAP-Rule:MF_00729}.
CC   -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00729}.
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DR   EMBL; BX571857; CAG44307.1; -; Genomic_DNA.
DR   RefSeq; WP_001031405.1; NC_002953.3.
DR   AlphaFoldDB; Q6G670; -.
DR   SMR; Q6G670; -.
DR   KEGG; sas:SAS2491; -.
DR   HOGENOM; CLU_081560_0_0_9; -.
DR   OMA; GVFGTKM; -.
DR   UniPathway; UPA00109; UER00183.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00729; FBP_aldolase_1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000741; FBA_I.
DR   InterPro; IPR023014; FBA_I_Gram+-type.
DR   PANTHER; PTHR11627; PTHR11627; 1.
DR   Pfam; PF00274; Glycolytic; 1.
PE   3: Inferred from homology;
KW   Glycolysis; Lyase; Schiff base.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..296
FT                   /note="Fructose-bisphosphate aldolase class 1"
FT                   /id="PRO_0000216907"
FT   ACT_SITE        175
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00729"
FT   ACT_SITE        212
FT                   /note="Schiff-base intermediate with dihydroxyacetone-P"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00729"
SQ   SEQUENCE   296 AA;  32967 MW;  C6D620FBD9F76E96 CRC64;
     MNKEQLEKMK NGKGFIAALD QSGGSTPKAL KEYGVNEDQY SNEDEMFQLV HDMRTRVVTS
     PSFSPDKILG AILFEQTMDR EVEGKYTADY LADKGVVPFL KVDKGLAEEQ NGVQLMKPID
     NLDSLLDRAN ERHIFGTKMR SNILELNEQG IKDVVEQQFE VAKQIIAKGL VPIIEPEVNI
     NAKDKAEIEK VLKAELKKGL DNLNADQLVM LKLTIPTEPN LYKELAEHPN VVRVVVLSGG
     YSREKANELL KDNAELIASF SRALASDLRA GQSKEEFDKA LGDAVESIYD ASVNKN