{PDOC00394}
{PS00435; PEROXIDASE_1}
{PS00436; PEROXIDASE_2}
{PS50292; PEROXIDASE_3}
{PS50873; PEROXIDASE_4}
{BEGIN}
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* Heme peroxidase signatures and profiles *
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Heme-binding peroxidases (EC 1.11.1.-) [1] carry out a variety of biosynthetic
and  degradative  functions  using hydrogen peroxide as the electron acceptor.
The  heme  prosthetic  group  is protoporphyrin IX and the fifth ligand of the
heme iron is a histidine (known as the proximal histidine). An other histidine
residue (the distal histidine) serves as an acid-base catalyst in the reaction
between  hydrogen peroxide and the enzyme. The regions around these two active
site residues are more or less conserved in a majority of peroxidases [2,3].

Heme  peroxidases  are  widely distributed throughout bacteria, fungi, plants,
and  vertebrates. On the basis of structural properties they can be devided in
two large superfamilies.

The plant peroxidase superfamily (can be grouped in three classes):

 Class I. Peroxidase of prokaryotic origin:
 - Plant  ascorbate  peroxidases.  They  play  a key role in hydrogen peroxide
   removal in the chloroplasts and cytosol of higher plants.
 - Yeast cytochrome c peroxidase (EC 1.11.1.5).
 - Prokaryotic catalase-peroxidases.  Some  bacterial  species produce enzymes
   that exhibit both catalase  and  broad-spectrum  peroxidase activities [4].
   Examples  of  such  enzymes are:  catalase HP I from Escherichia coli (gene
   katG) and perA from Bacillus stearothermophilus.

 Class II. Secreted fungal peroxidases:
 - Fungal ligninases. Ligninase catalyzes the first step in the degradation of
   lignin. It depolymerizes lignin by catalyzing the C(alpha)-C(beta) cleavage
   of the propyl side chains of lignin.

 Class III. Classical secretory plant peroxidases:
 - Plant peroxidases (EC 1.11.1.7).  Plants express a large number of isozymes
   of  peroxidases.   Some  of  them  play  a   role  in  cell-suberization by
   catalyzing the deposition of the  aromatic residues  of suberin on the cell
   wall, some are expressed as a defense response toward  wounding, others are
   involved in the metabolism of auxin and the biosynthesis of lignin.

The animal peroxidase superfamily:

 - Myeloperoxidase (EC 1.11.1.7)  (MPO).  MPO  is  found  in  granulocytes and
   monocytes and  plays  a  major  role  in  the oxygen-dependent microbicidal
   system of neutrophils.
 - Lactoperoxidase (EC 1.11.1.7) (LPO). LPO is a milk protein which acts as an
   antimicrobial agent.
 - Eosinophil  peroxidase  (EC 1.11.1.7)  (EPO).   An   enzyme  found  in  the
   cytoplasmic granules of eosinophils.
 - Thyroid peroxidase (EC 1.11.1.8) (TPO).  TPO  plays  a  central role in the
   biosynthesis of thyroid hormones. It  catalyzes the iodination and coupling
   of  the  hormonogenic  tyrosines in  thyroglobulin  to  yield  the  thyroid
   hormones T3 and T4.

The  two patterns we developed recognize both superfamilies. Our first pattern
recognizes   the   proximal  heme-binding  site  whereas  the  second  pattern
surrounded  the  distal  active  site.  We  also  developed  two profiles, one
specific  for  the animal peroxidases superfamily and one directed against the
plant peroxidase superfamily.

-Consensus pattern: [DET]-[LIVMTA]-{NSYL}-{RPFC}-[LIVM]-[LIVMSTAG]-[SAG]-
                    [LIVMSTAG]-H-[STA]-[LIVMFY]
                    [H is the proximal heme-binding ligand]
-Sequences known to belong to this class detected by the profile: ALL.
 for ligninase III from Phlebia radiata, and LPO.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: [SGATV]-{D}-x(2)-[LIVMA]-R-[LIVMA]-x-[FW]-H-{V}-[SAC]
                    [H is an active site residue]
-Sequences known to belong to this class detected by the profile: ALL.
 for vertebrate peroxidases (MPO, TPO, LPO, and EPO).
-Other sequence(s) detected in Swiss-Prot: NONE.

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

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

-Last update: April 2006 / Pattern revised.

[ 1] Dawson J.H.
     "Probing structure-function relations in heme-containing oxygenases
     and peroxidases."
     Science 240:433-439(1988).
     PubMed=3358128
[ 2] Kimura S., Ikeda-Saito M.
     "Human myeloperoxidase and thyroid peroxidase, two enzymes with
     separate and distinct physiological functions, are evolutionarily
     related members of the same gene family."
     Proteins 3:113-120(1988).
     PubMed=2840655
[ 3] Henrissat B., Saloheimo M., Lavaitte S., Knowles J.K.C.
     "Structural homology among the peroxidase enzyme family revealed by
     hydrophobic cluster analysis."
     Proteins 8:251-257(1990).
     PubMed=2177893
[ 4] Welinder K.G.
     "Bacterial catalase-peroxidases are gene duplicated members of the
     plant peroxidase superfamily."
     Biochim. Biophys. Acta 1080:215-220(1991).
     PubMed=1954228

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