GenomeNet

Database: PROSITE(DOC)
Entry: PDOC00794
LinkDB: PDOC00794
Original site: PDOC00794 
{PDOC00794}
{PS01034; GH16_1}
{PS51762; GH16_2}
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* Glycosyl hydrolases family 16 (GH16) signature and domain profile *
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The glycosyl   hydrolases   family  16  (GH16)  [1,E1]  contains  functionally
heterogeneous members,   including   beta-agarases,   endo-1,3-beta-glucanases
(laminarinases), endo-beta-1,3-1,4-glucanases       (lichenases),       kappa-
carrageenases, endo-beta-galactosidases and xyloglucan endotransferases. These
enzymes share  a  common  ancestor  and  have  diverged significantly in their
primary sequence.

The GH16  catalytic domain has a classical sandwich-like beta-jelly roll fold,
formed by  two  main,  closely  packed  and  curved  antiparallel beta sheets,
creating a  deep  channel  harboring the catalytic machinery (see <PDB:1DYP>).
Even though  the GH16 domains have now diverged significantly in their primary
sequences, they  all  feature  a  common  catalytic  motif,  E-[ILV]-D-[IVAF]-
[VILMF](0,1)-E. The  two glutamic acid residues in the conserved motif are the
nucleophile and  the  general base involved in catalysis, whereas the aspartic
acid residue  is  important  in  maintaining  the  relative  position of these
catalytic amino acids [2,3].

Some proteins known to contain a GH16 domain are listed below:

 - Bacterial beta-1,3-1,4-glucanases, or lichenases, (EC 3.2.1.73) mainly from
   Bacillus but  also  from  Clostridium thermocellum (gene licB), Fibrobacter
   succinogenes and Rhodothermus marinus (gene bglA).
 - Bacillus circulans beta-1,3-glucanase A1 (EC 3.2.1.39) (gene glcA).
 - Alteromonas carrageenovora kappa-carrageenase (EC 3.2.1.83) (gene cgkA).
 - Rhizobium meliloti endo-1,3-1,4-beta-glycanase exoK.
 - Streptomyces coelicolor agarase (EC 3.2.1.81) (gene dagA).
 - Zobellia galactanivorans beta-agarase A (EC 3.2.1.81) (gene agaA).
 - Zobellia galactanivorans beta-agarase B (EC 3.2.1.81) (gene agaB).
 - Saccharophagus sp. AG21 beta-agarase (gene agy1), includes a GH16 domain
   and two CBM6 (carbohydrate binding type-6) domain (see <PDOC51175>).
 - Microbulbifer thermotolerans agarase (agaA).
 - Thermotoga maritima laminarinase.
 - Saccharomyces cerevisiae beta-glucan synthesis-associated protein SKN1 [5].
 - Saccharomyces cerevisiae beta-glucan synthesis-associated protein KRE6 [5].

Two closely  clustered conserved glutamates have been shown [6] to be involved
in the  catalytic  activity  of Bacillus licheniformis lichenase.  We used the
region that  contains  these  residues  as  a  signature pattern. We have also
developed a profile that covers the entire GH16 domain.

-Consensus pattern: E-[LIV]-D-[LIVF]-x(0,1)-E-x(2)-[GQ]-[KRNF]-x-[PSTA]
                    [The 2 E's are active site residues]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: 4.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

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

-Last update: June 2015 / Text revised; profile added.

[ 1] Henrissat B.
     "A classification of glycosyl hydrolases based on amino acid sequence
     similarities."
     Biochem. J. 280:309-316(1991).
     PubMed=1747104
[ 2] Allouch J., Jam M., Helbert W., Barbeyron T., Kloareg B.,
     Henrissat B., Czjzek M.
     "The three-dimensional structures of two beta-agarases."
     J. Biol. Chem. 278:47171-47180(2003).
     PubMed=12970344; DOI=10.1074/jbc.M308313200
[ 3] Michel G., Chantalat L., Duee E., Barbeyron T., Henrissat B.,
     Kloareg B., Dideberg O.
     "The kappa-carrageenase of P. carrageenovora features a tunnel-shaped
     active site: a novel insight in the evolution of Clan-B glycoside
     hydrolases."
     Structure 9:513-525(2001).
     PubMed=11435116
[ 4] Thevissen K., Idkowiak-Baldys J., Im Y.-J., Takemoto J.,
     Francois I.E.J.A., Ferket K.K.A., Aerts A.M., Meert E.M.K.,
     Winderickx J., Roosen J., Cammue B.P.A.
     "SKN1, a novel plant defensin-sensitivity gene in Saccharomyces
     cerevisiae, is implicated in sphingolipid biosynthesis."
     FEBS Lett. 579:1973-1977(2005).
     PubMed=15792805; DOI=10.1016/j.febslet.2005.02.043
[ 5] Montijn R.C., Vink E., Mueller W.H., Verkleij A.J., Van Den Ende H.,
     Henrissat B., Klis F.M.
     "Localization of synthesis of beta1,6-glucan in Saccharomyces
     cerevisiae."
     J. Bacteriol. 181:7414-7420(1999).
     PubMed=10601196
[ 6] Juncosa M., Pons J., Dot T., Querol E., Planas A.
     "Identification of active site carboxylic residues in Bacillus
     licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase by
     site-directed mutagenesis."
     J. Biol. Chem. 269:14530-14535(1994).
     PubMed=8182059
[E1] http://www.cazy.org/GH16.html
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