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class II fructose-bisphosphate aldolase [Listeria monocytogenes].


LOCUS       WP_010989903             284 aa            linear   BCT 21-JAN-2025
ACCESSION   WP_010989903
VERSION     WP_010989903.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10097223
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..284
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=30878
     Region          5..281
                     /region_name="TBP_aldolase_IIB"
                     /note="Tagatose-1,6-bisphosphate (TBP) aldolase and
                     related Type B Class II aldolases. TBP aldolase is a
                     tetrameric class II aldolase that catalyzes the reversible
                     condensation of dihydroxyacetone phosphate with
                     glyceraldehyde 3-phsophate to produce tagatose 1; cd00947"
                     /db_xref="CDD:238477"
     Site            order(26..28,31,51,54,56..57,61,65,68..69,142,233..234,
                     236..237,240,244,247)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238477"
     Site            order(82..83,177..179,181,208..209,211,230,232..233)
                     /site_type="active"
                     /db_xref="CDD:238477"
     Site            order(83,178,208)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238477"
     Site            order(177,179,181,209,211)
                     /site_type="other"
                     /note="Na+ binding site [ion binding]"
                     /db_xref="CDD:238477"
ORIGIN      
        1 myvsmkgmle rankehyavm aincfnleta ravidaaqel rapiiidllq dhltshlgsr
       61 fltkpiikma eeasvevain ldhghdvaiv kqcladgfss vmmdassfpy eenvaitkkm
      121 vefaevyhas veaevgniga vtgdnytnqe mytdpkvaid fakrtgidal aisygsshgd
      181 ypegftpafq fdivreiksa tnmplvlhgg sgcgaenire svrlginkin vgsdfmkaqv
      241 nqiktnlkes pavnyvdlih etikagtkav kyyihlsgst gksl