{PDOC00395}
{PS00437; CATALASE_1}
{PS00438; CATALASE_2}
{PS51402; CATALASE_3}
{BEGIN}
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* Catalase signatures and profile *
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Catalase  (EC  1.11.1.6)  [1,2,3]  or more correctly, hydroperoxidase [4] is a
heme-containing enzyme, present in all aerobic cells, that decomposes hydrogen
peroxide  to molecular oxygen and water. Its main function is to protect cells
from  the  toxic  effects of hydrogen peroxide. In eukaryotic organisms and in
some  prokaryotes  catalase is a molecule composed of four identical subunits.
Each of the subunits binds one protoheme IX group.

The  typical core catalase is composed of a heme-containing active site deeply
buried  in a beta-barrel structure with two or three channels providing access
to  the  heme  (see  <PDB:1A4E>)  [5]. A conserved tyrosine serves as the heme
proximal  side  ligand. We have used the region around this residue as a first
signature  pattern; it also includes a conserved arginine that participates in
heme-binding.  A  conserved  histidine  has been shown to be important for the
catalytic mechanism of the enzyme. We have used the region around this residue
as  a  second  signature pattern. We also developed a profile which covers the
whole conserved region.

-Consensus pattern: R-[LIVMFSTAN]-F-[GASTNP]-Y-x-D-[AST]-[QEH]
                    [Y is the proximal heme-binding ligand]
-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: [IF]-x-[RH]-x(4)-[EQ]-R-x(2)-H-x(2)-[GAS]-[GASTFY]-[GAST]
                    [H is an active site residue]
-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

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

-Note:  Some  prokaryotic  catalases  belong to the non-animal heme peroxidase
 family (see <PDOC00394>).

-Last update: August 2008 / Profile added and text revised.

[ 1] Murthy M.R.N., Reid T.J. III, Sicignano A., Tanaka N., Rossmann M.G.
     "Structure of beef liver catalase."
     J. Mol. Biol. 152:465-499(1981).
     PubMed=7328661
[ 2] Melik-Adamyan W.R., Barynin V.V., Vagin A.A., Borisov V.V.,
     Vainshtein B.K., Fita I., Murthy M.R.N., Rossmann M.G.
     J. Mol. Biol. 188:63-72(1986).
[ 3] von Ossowki I., Hausner G., Loewen P.C.
     J. Mol. Evol. 37:71-76(1993).
[ 4] Chelikani P., Fita I., Loewen P.C.
     "Diversity of structures and properties among catalases."
     Cell. Mol. Life Sci. 61:192-208(2004).
     PubMed=14745498; DOI=10.1007/s00018-003-3206-5
[ 5] Mate M.J., Zamocky M., Nykyri L.M., Herzog C., Alzari P.M., Betzel C.,
     Koller F., Fita I.
     "Structure of catalase-A from Saccharomyces cerevisiae."
     J. Mol. Biol. 286:135-149(1999).
     PubMed=9931255; DOI=10.1006/jmbi.1998.2453

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