ID   ALF1_STAES              Reviewed;         296 AA.
AC   Q8CMY5;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 103.
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=SE_2156;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO05798.1; -; Genomic_DNA.
DR   RefSeq; NP_765711.1; NC_004461.1.
DR   RefSeq; WP_001830665.1; NZ_WBME01000005.1.
DR   AlphaFoldDB; Q8CMY5; -.
DR   SMR; Q8CMY5; -.
DR   STRING; 176280.SE_2156; -.
DR   EnsemblBacteria; AAO05798; AAO05798; SE_2156.
DR   GeneID; 50017768; -.
DR   KEGG; sep:SE_2156; -.
DR   PATRIC; fig|176280.10.peg.2106; -.
DR   eggNOG; COG3588; Bacteria.
DR   HOGENOM; CLU_081560_0_0_9; -.
DR   OMA; GVFGTKM; -.
DR   UniPathway; UPA00109; UER00183.
DR   Proteomes; UP000001411; 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_0000216910"
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;  33052 MW;  13258473A6438CE9 CRC64;
     MNKEQLEKMT HGKGFIAALD QSGGSTPKAL KEYGVNEDQY SNEDEMFQLV HDMRTRVVTS
     PSFSPDKILG AILFEQTMDR EVEGKYTGDY LADKGVVPFL KVDKGLAEEK NGVQLMKPID
     DLDETLDRAN ERHIFGTKMR SNILELNEQG IKDVVEQQFE FAKKIIAKGL VPIIEPEVNI
     NAKDKSEIEK VLKAEIKKGL DSLNDDQLVM LKLTIPTEAN LYKDLADHPN VVRVVVLSGG
     YSRDEANKLL KDNDELIASF SRALASDLRA SQSQEEFDKA LGDAVDSIYD ASVNKN