General rule information
[?]
Accession |
PRU00297 |
Dates |
12-DEC-2003 (Created) 19-NOV-2022 (Last updated, Version 37) |
Predictors |
PROSITE; PS50873; PEROXIDASE_4
|
Name |
Plant heme peroxidase |
Function |
Removal of H(2)O(2), oxidation of toxic reductants |
Propagated annotation
[?]
case <FTGroup:1> and <FTGroup:2> and <FTGroup:3> and <FTTag:viacarbo>
Function |
Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. |
Catalytic activity |
RHEA:30275: AH2 + H2O2 = A + 2 H2O
|
Cofactor |
heme b Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. |
|
Ca(2+) Note: Binds 2 calcium ions per subunit. |
Subcellular location |
Secreted. |
Similarity |
Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily. |
end case
case <FT:12>
end case
case <FT:11>
end case
case <FTGroup:1> and <FTGroup:2> and <FTGroup:3> and <FTTag:viacarbo>
GO:0016491; Molecular function: oxidoreductase activity.
GO:0004601; Molecular function: peroxidase activity.
GO:0009055; Molecular function: electron transfer activity.
GO:0006979; Biological process: response to oxidative stress.
GO:0042744; Biological process: hydrogen peroxide catabolic process.
end case
case <FT:12>
end case
case <FT:17>
end case
case <FTGroup:1> or <FTGroup:2>
GO:0005509; Molecular function: calcium ion binding.
end case
case <FT:12> or <FTGroup:1> or <FTGroup:2>
end case
case <FTTag:disulf>
end case
From: PS50873 |
Key
|
|
From
|
|
To
|
|
Description
|
|
Tag
|
|
Condition
|
|
FTGroup
|
BINDING
|
|
43
|
|
43
|
|
/ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="#1
|
|
|
|
[DE]
|
|
1
|
BINDING
|
|
46
|
|
46
|
|
/ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="#1
|
|
|
|
[VI]
|
|
1
|
BINDING
|
|
48
|
|
48
|
|
/ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="#1
|
|
|
|
G
|
|
1
|
BINDING
|
|
50
|
|
50
|
|
/ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="#1
|
|
|
|
[DE]
|
|
1
|
BINDING
|
|
52
|
|
52
|
|
/ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="#1
|
|
|
|
[ST]
|
|
1
|
BINDING
|
|
169
|
|
169
|
|
/ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="#2
|
|
|
|
[TS]
|
|
2
|
BINDING
|
|
222
|
|
222
|
|
/ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="#2
|
|
|
|
[DE]
|
|
2
|
BINDING
|
|
225
|
|
225
|
|
/ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="#2
|
|
|
|
[TS]
|
|
2
|
BINDING
|
|
230
|
|
230
|
|
/ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="#2
|
|
|
|
[DE]
|
|
2
|
SITE
|
|
38
|
|
38
|
|
Transition state stabilizer
|
|
|
|
R
|
|
3
|
ACT_SITE
|
|
42
|
|
42
|
|
Proton acceptor
|
|
|
|
H
|
|
3
|
BINDING
|
|
168
|
|
168
|
|
/ligand="heme b" /ligand_id="ChEBI:CHEBI:60344" /ligand_part="Fe" /ligand_part_id="ChEBI:CHEBI:18248" /note="axial binding residue
|
|
|
|
H
|
|
3
|
DISULFID
|
|
11
|
|
90
|
|
|
|
disulf
|
|
C-x*-C
|
|
|
DISULFID
|
|
44
|
|
49
|
|
|
|
disulf
|
|
C-x*-C
|
|
|
DISULFID
|
|
96
|
|
298
|
|
|
|
disulf
|
|
C-x*-C
|
|
|
DISULFID
|
|
175
|
|
207
|
|
|
|
disulf
|
|
C-x*-C
|
|
|
MOD_RES
|
|
1
|
|
1
|
|
Pyrrolidone carboxylic acid
|
|
|
|
Q
|
|
|
case <FTTag:viacarbo>
BINDING
|
|
138
|
|
138
|
|
/ligand="substrate
|
|
|
|
P
|
|
|
end case
Additional information
[?]
Size range |
250-384 amino acids |
Related rules |
None |
Repeats |
1 |
Topology |
Undefined |
Examples |
P0DI10 (PER1_ARATH); Q67Z07 (PER2_ARATH): [Recover all] |
Scope |
Eukaryota |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and
distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives
(CC BY-NC-ND 4.0) License, see
prosite_license.html.
UniProtKB rule member sequences
[?]