{PDOC51759}
{PS51759; CBM15}
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* Carbohydrate-binding module 15 (CBM15) domain profile *
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Microbial plant  cell  wall hydrolases are often modular proteins comprising a
catalytic module  linked  via  a  highly  flexible  sequence  to  one  or more
carbohydrate-binding modules  (CBMs). CBMs bind to a range of plant structural
polysaccharides that  include  both  crystalline  cellulose and noncrystalline
beta-1,4-glucan, xylan,   mannan,   beta-1,3-glucan,  and  glucomannan.  Their
primary function  is  to  increase  the  catalytic efficiency of these enzymes
against their  soluble  substrates  by  bringing  the  catalytic  module  into
prolonged and intimate contact with its substrate. CBMs have been grouped into
approximately 30 families based on amino acid sequence similarities.

The family  15  CBM (CBM15) binds both soluble xylan and xylooligosaccharides.
The structure  of  the  CBM15  domain  forms  a  classic beta-jelly roll fold,
predominantly consisting  of  five major anti-parallel beta-strands on the two
faces (see  <PDB:1GNY>).  The  CBM15  domain  displays a single disulfide bond
linking the  two  beta-sheets  that  form  the  jelly  roll.  The CBM15 domain
contains a deep cleft that runs along the concave face of the beta-sheet which
forms the binding site for the target ligands [1,2,E1].

Protein known to contain a CBM15 domain:

 - Pseudomonas  cellulosa  xylanase Xyn10C, comprised of a C-terminal xylanase
   GH10 catalytic  module  with an N-terminal carbohydrate-binding module that
   belongs to family 15 (CBM15).

The profile we developed covers the entire CBM15 domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: June 2015 / First entry.

[ 1] Szabo L., Jamal S., Xie H., Charnock S.J., Bolam D.N., Gilbert H.J.,
     Davies G.J.
     "Structure of a family 15 carbohydrate-binding module in complex with
     xylopentaose. Evidence that xylan binds in an approximate 3-fold
     helical conformation."
     J. Biol. Chem. 276:49061-49065(2001).
     PubMed=11598143; DOI=10.1074/jbc.M109558200
[ 2] Pell G., Szabo L., Charnock S.J., Xie H., Gloster T.M., Davies G.J.,
     Gilbert H.J.
     "Structural and biochemical analysis of Cellvibrio japonicus xylanase
     10C: how variation in substrate-binding cleft influences the catalytic
     profile of family GH-10 xylanases."
     J. Biol. Chem. 279:11777-11788(2004).
     PubMed=14670951; DOI=10.1074/jbc.M311947200
[E1] http://www.cazy.org/CBM15.html

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