{PDOC00532}
{PS00609; GLYCOSYL_HYDROL_F32}
{BEGIN}
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* Glycosyl hydrolases family 32 active site *
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It has  been  shown  [1,2]  that  the  following  glycosyl  hydrolases  can be
classified into a single family on the basis of sequence similarities:

 - Inulinase (EC 3.2.1.7) (or inulase) from the fungi Kluyveromyces marxianus.
 - Beta-fructofuranosidase (EC 3.2.1.26), commonly known as invertase in fungi
   and plants and as sucrase in bacteria (gene sacA or scrB).
 - Raffinose invertase (EC 3.2.1.26) (gene rafD) from Escherichia coli plasmid
   pRSD2.
 - Levanase (EC 3.2.1.65) (gene sacC) from Bacillus subtilis.

One of the  conserved regions in  these  enzymes is  located in the N-terminal
section and contains an  aspartic acid  residue which  has been  shown [3], in
yeast invertase to be important for the catalytic mechanism. We have used this
region as a signature pattern.

-Consensus pattern: H-x(2)-[PV]-x(4)-[LIVMA]-N-D-P-N-[GA]
                    [D is the active site residue]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Expert(s) to contact by email:
           Henrissat B.; bernie@afmb.cnrs-mrs.fr

-Last update: April 2006 / Pattern revised.

[ 1] Henrissat B.
     "A classification of glycosyl hydrolases based on amino acid sequence
     similarities."
     Biochem. J. 280:309-316(1991).
     PubMed=1747104
[ 2] Gunasekaran P., Karunakaran T., Cami B., Mukundan A.G., Preziosi L.,
     Baratti J.
     "Cloning and sequencing of the sacA gene: characterization of a
     sucrase from Zymomonas mobilis."
     J. Bacteriol. 172:6727-6735(1990).
     PubMed=2254250
[ 3] Reddy V.A., Maley F.
     "Identification of an active-site residue in yeast invertase by
     affinity labeling and site-directed mutagenesis."
     J. Biol. Chem. 265:10817-10820(1990).
     PubMed=2113524

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