ID   ALF1_STAHJ              Reviewed;         296 AA.
AC   Q4L9B6;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Fructose-bisphosphate aldolase class 1;
DE            EC=4.1.2.13;
DE   AltName: Full=Fructose-biphosphate aldolase class I;
DE            Short=FBP aldolase;
GN   Name=fda; OrderedLocusNames=SH0450;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S.,
RA   Lee J.C., Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
CC   -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone
CC       phosphate + D-glyceraldehyde 3-phosphate.
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.
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DR   EMBL; AP006716; BAE03759.1; -; Genomic_DNA.
DR   RefSeq; YP_252365.1; -.
DR   GeneID; 3484099; -.
DR   GenomeReviews; AP006716_GR; SH0450.
DR   KEGG; sha:SH0450; -.
DR   NMPDR; fig|279808.3.peg.540; -.
DR   HOGENOM; Q4L9B6; -.
DR   OMA; Q4L9B6; GTKMRSV.
DR   BioCyc; SHAE279808:SH0450-MON; -.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:HAMAP.
DR   GO; GO:0006096; P:glycolysis; IEA:HAMAP.
DR   HAMAP; MF_00729; -; 1.
DR   InterPro; IPR000741; Aldolase_I.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   PANTHER; PTHR11627; Aldolase_I; 1.
DR   Pfam; PF00274; Glycolytic; 1.
DR   ProDom; PD001128; Aldolase_I; 1.
DR   PROSITE; PS00158; ALDOLASE_CLASS_I; FALSE_NEG.
PE   3: Inferred from homology;
KW   Complete proteome; Glycolysis; Lyase; Schiff base.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    296       Fructose-bisphosphate aldolase class 1.
FT                                /FTId=PRO_0000216912.
FT   ACT_SITE    175    175       Proton acceptor (By similarity).
FT   ACT_SITE    212    212       Schiff-base intermediate with
FT                                dihydroxyacetone-P (By similarity).
SQ   SEQUENCE   296 AA;  32968 MW;  619D6086BE604E71 CRC64;
     MNKEQLEKMT NGKGFIAALD QSGGSTPKAL KEYGVNEDEY SNDDEMFQLV HDMRTRVVTS
     PSFSPDKILG AILFEQTMDR EVEGKYTGDY LADKGVVPFL KVDKGLAEQQ NGVQLMKPID
     DLDDTLDRAV ERHIFGTKMR SNILELNEQG IKDVVEQQFE FAKKIIAKGL VPIIEPEVNI
     NAKDKAEIEE VLKAELKKGL DALNDDQLVM LKLTIPTKAN LYKELADHPN VVRVVVLSGG
     YSRDEANKLL KDNDELIASF SRALASDLRA SQSQEEFDKA LGDAVDSIYD ASVNKN
//