ID   ALF1_STAAB              Reviewed;         296 AA.
AC   Q2YWF3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 93.
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=SAB2479;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI82167.1; -; Genomic_DNA.
DR   RefSeq; WP_001031398.1; NC_007622.1.
DR   AlphaFoldDB; Q2YWF3; -.
DR   SMR; Q2YWF3; -.
DR   KEGG; sab:SAB2479; -.
DR   HOGENOM; CLU_081560_0_0_9; -.
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; Aldolase class I; 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; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR   PANTHER; PTHR11627:SF80; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR   Pfam; PF00274; Glycolytic; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Glycolysis; Lyase; Schiff base.
FT   CHAIN           1..296
FT                   /note="Fructose-bisphosphate aldolase class 1"
FT                   /id="PRO_1000045919"
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;  32927 MW;  CB103A2A63539181 CRC64;
     MNKEQLEKMK NGKGFIAALD QSGGSTPKAL KEYGINEDQY SNEDEMFQLV HDMRTRVVTS
     PSFSPDKILG AILFEQTMDR EVEGKYTADY LADKGVVPFL KVDKGLAEEQ NGVQLMKPID
     NLDSLLDRAN ERHIFGTKMR SNILELNEQG IKDVVEQQFE VAKQIIAKGL VPIIEPEVNI
     NAKDKAEIEK VLKAELKKGL DSLNADQLVM LKLTIPTEAN LYKDLAEHPN VVRIVVLSGG
     YSREKANELL KDNAELIASF SRALASDLRA GQSKEEFDKA LGDAVESIYD ASVNKN
//