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 16-JUN-2009, entry version 31. 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=SAS2491; OS Staphylococcus aureus (strain MSSA476). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=282459; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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., RA Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L., RA Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., RA James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., RA Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., RA Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., RA Spratt B.G., Parkhill J.; RT "Complete genomes of two clinical Staphylococcus aureus strains: RT evidence for the rapid evolution of virulence and drug resistance."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004). 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX571857; CAG44307.1; -; Genomic_DNA. DR RefSeq; YP_044604.1; -. DR GeneID; 2864245; -. DR GenomeReviews; BX571857_GR; SAS2491. DR KEGG; sas:SAS2491; -. DR HOGENOM; Q6G670; -. DR OMA; Q6G670; GTKMRSV. DR BioCyc; SAUR282459:SAS2491-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_0000216907. 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; 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 //