ID   ALF1_STAAM              Reviewed;         296 AA.
AC   P67472; Q99R31;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Fructose-bisphosphate aldolase class 1;
DE            EC=4.1.2.13;
DE   AltName: Full=Fructose-bisphosphate aldolase class I;
DE            Short=FBP aldolase;
GN   Name=fda; OrderedLocusNames=SAV2606;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 4/4.
CC   -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC       family. {ECO:0000305}.
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DR   EMBL; BA000017; BAB58768.1; -; Genomic_DNA.
DR   RefSeq; WP_001031409.1; NC_002758.2.
DR   AlphaFoldDB; P67472; -.
DR   SMR; P67472; -.
DR   World-2DPAGE; 0002:P67472; -.
DR   PaxDb; P67472; -.
DR   EnsemblBacteria; BAB58768; BAB58768; SAV2606.
DR   KEGG; sav:SAV2606; -.
DR   HOGENOM; CLU_081560_0_0_9; -.
DR   OMA; GVFGTKM; -.
DR   PhylomeDB; P67472; -.
DR   BioCyc; SAUR158878:SAV_RS14210-MON; -.
DR   UniPathway; UPA00109; UER00183.
DR   Proteomes; UP000002481; Chromosome.
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_0000216904"
FT   ACT_SITE        175
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        212
FT                   /note="Schiff-base intermediate with dihydroxyacetone-P"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   296 AA;  33042 MW;  D63B1A3C7646725B CRC64;
     MNKEQLEKMK NGKGFIAALD QSGGSTPKAL KEYGVNEDQY SNEDEMFQLV HDMRTRVVTS
     PSFSPDKILG AILFEQTMDR EVEGKYTADY LADKGVVPFL KVDKGLAEEQ NGVQLMKPID
     NLDSLLDRAN ERHIFGTKMR SNILELNEQG IKDVVEQQFE VAKQIIAKGL VPIIEPEVNI
     NAKDKAEIEK VLKAELKKGL DSLNADQLVM LKLTIPTEPN LYKELAEHPN VVRVVVLSGG
     YSREKANELL KDNDELIASF SRALASDLRA DQSKEEFDKA LGDAVESIYD ASVNKN