Reviewed, UniProtKB/Swiss-Prot Q4W1I9 (PER2_ZINEL)

Names and origin

Protein names

Recommended name:
    Basic peroxidase
    EC=1.11.1.7
Alternative name(s):
    ZePrx33.44
    ZePrx34.70

Gene names

Name:	POD3
AND
Name:	POD4

Organism

Zinnia elegans (Zinnia)

Taxonomic identifier

34245 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › campanulids › Asterales › Asteraceae › Asteroideae › Heliantheae › Zinnia

Protein attributes

Sequence length	321 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Removal of H2O2, 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. Involved in the synthesis of highly polymerized lignins.
Catalytic activity	Donor + H2O2 = oxidized donor + 2 H2O. Ref.1
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity. Binds 2 calcium ions per subunit By similarity.
Subcellular location	Secreted By similarity.
Tissue specificity	Expressed in tracheary elements, roots, young and old hypocotyls, and stems in the partially glycosylated form and in roots and young hypocotyls in the fully glycosylated form. None of the isoforms is significantly expressed in leaves or cotyledons. Ref.1
Post-translational modification	N-glycosylated.
Sequence similarities	Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.
Caution	Four genes are encoding the same mature protein that may have different glycosylation degree. The two precursors produced differ by only one amino acid located in the signal peptide.
biophysicochemical properties	Kinetic parameters: The full glycosylation reduces the affinity of the enzyme for both p-coumaryl and coniferyl, but not sinapyl, alcohol. KM=241 µM for p-coumaryl alcohol (in the presence of 10.2 µM H2O2, for a partially glycosylated enzyme) KM=432 µM for p-coumaryl alcohol (in the presence of 10.2 µM H2O2, for a fully glycosylated enzyme) KM=83 µM for coniferyl alcohol (in the presence of 10.2 µM H2O2, for a partially glycosylated enzyme) KM=124 µM for coniferyl alcohol (in the presence of 10.2 µM H2O2, for a fully glycosylated enzyme) KM=15 µM for sinapyl alcohol (in the presence of 10.2 µM H2O2, for a partially glycosylated enzyme) KM=13 µM for sinapyl alcohol (in the presence of 10.2 µM H2O2, for a fully glycosylated enzyme)
Mass spectrometry	Molecular mass is 31460 Da from positions 30 - 321. Determined by MALDI. Deglycosylated form. Ref.1 Molecular mass is 33440 Da from positions 30 - 321. Determined by MALDI. Partially glycosylated form. Ref.1 Molecular mass is 34700 Da from positions 30 - 321. Determined by MALDI. Fully glycosylated form. Ref.1

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 30	30	Ref.1
	Chain	31 – 321	291	Basic peroxidase		PRO_0000042697
Sites
	Active site	72	1	Proton acceptor
	Metal binding	73	1	Calcium 1 By similarity
	Metal binding	76	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	78	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	80	1	Calcium 1 By similarity
	Metal binding	82	1	Calcium 1 By similarity
	Metal binding	195	1	Iron (heme axial ligand)
	Metal binding	196	1	Calcium 2 By similarity
	Metal binding	241	1	Calcium 2 By similarity
	Metal binding	244	1	Calcium 2 By similarity
	Metal binding	249	1	Calcium 2 By similarity
	Binding site	165	1	Substrate; via carbonyl oxygen By similarity
	Site	68	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	31	1	Pyrrolidone carboxylic acid
	Glycosylation	211	1	N-linked (GlcNAc...) Potential
	Glycosylation	221	1	N-linked (GlcNAc...) Potential
	Disulfide bond	41 ↔ 117		By similarity
	Disulfide bond	74 ↔ 79		By similarity
	Disulfide bond	123 ↔ 317		By similarity
	Disulfide bond	202 ↔ 228		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4W1I9-1 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: 620A21D02479F7F3	FASTA	321	34,233
	10 20 30 40 50 60 MSYHKSSGTT LMVPLFMLLI SVNYFMSCNA QLSTTFYDTT CPTALSTIRT SIRSSVSSNR 70 80 90 100 110 120 RNAALVIRLL FHDCFVQGCD ASLLLSGAGS ERASPANDGV LGYEVIDAAK AAVERVCPGV 130 140 150 160 170 180 VSCADILAVA ARDASVAVGG PSWTVRLGRR DSTTSNAAQA ATDLPRGNMV LSQLISNFAN 190 200 210 220 230 240 KGLNTREMVA LSGSHTLGQA RCIRFRGRIY NSTLRIEPNF NRSLSQACPP TGNDATLRPL 250 260 270 280 290 300 DLVTPNSFDN NYYRNLVTSR GLLISDQVLF NADSTDSIVT EYVNNPATFA ADFAAAMVKM 310 320 SEIGVVTGTS GIVRTLCGNP S

References

[1]

"Cloning and molecular characterization of the basic peroxidase isoenzyme from Zinnia elegans, an enzyme involved in lignin biosynthesis." Gabaldon C., Lopez-Serrano M., Pedreno M.A., Barcelo A.R. Plant Physiol. 139:1138-1154(2005) [PubMed: 16258008] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-43; 133-146; 186-201 AND 297-313, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PYROGLUTAMATE FORMATION AT GLN-31, MASS SPECTROMETRY. Strain: cv. Envy. Tissue: Callus.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ880394 mRNA. Translation: CAI54301.1. AJ880392 mRNA. Translation: CAI54299.1.
3D structure databases
ModBase	Search...
Protein family/group databases
PeroxiBase	2625. ZePrx14.
Enzyme and pathway databases
BRENDA	1.11.1.7. 228834.
Family and domain databases
InterPro	IPR002016. Haem_peroxidase_pln/fun/bac. IPR000823. Peroxidase_pln. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view]
Pfam	PF00141. peroxidase. 1 hit. [Graphical view]
PRINTS	PR00458. PEROXIDASE. PR00461. PLPEROXIDASE.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PER2_ZINEL

Accession

Primary (citable) accession number: Q4W1I9
Secondary accession number(s): P84332, P84333

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	July 5, 2005
Last modified:	June 16, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)