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Protein

Peroxidase

Gene
N/A
Organism
Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

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.UniRule annotation
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.SAAS annotation

Catalytic activityi

2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O.UniRule annotationSAAS annotation

Cofactori

Protein has several cofactor binding sites:
  • Ca2+UniRule annotationNote: Binds 2 calcium ions per subunit.UniRule annotation
  • heme bUniRule annotationNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxideUniRule annotation

Keywords - Ligandi

CalciumUniRule annotation, HemeUniRule annotationSAAS annotation, Iron, Metal-binding

Protein family/group databases

PeroxiBasei911. PtPrx11_Trichobel.

Names & Taxonomyi

Protein namesi
Recommended name:
PeroxidaseUniRule annotationSAAS annotation (EC:1.11.1.7UniRule annotationSAAS annotation)
OrganismiPopulus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa)Imported
Taxonomic identifieri3694 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesSalicaceaeSaliceaePopulus

Subcellular locationi

  • Secreted UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

SecretedUniRule annotation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222UniRule annotationAdd
BLAST
Chaini23 – 343321PeroxidaseUniRule annotationPRO_5005143307Add
BLAST

Keywords - PTMi

Disulfide bondSAAS annotation

Structurei

3D structure databases

ProteinModelPortaliQ43099.
SMRiQ43099. Positions 25-331.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 329305PEROXIDASE_4InterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.UniRule annotationSAAS annotation

Keywords - Domaini

SignalUniRule annotation

Family and domain databases

InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00458. PEROXIDASE.
PR00461. PLPEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q43099-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHLSKAIVAA FFFVVLLGGT LAHGQLTPTF YDQTCPNVSS IIRNVITETL
60 70 80 90 100
VCDRRIGGSL IRLHFHDCFV NGCDGSLLLD NTDTIESEKE AAGNNNSARG
110 120 130 140 150
FEVVDRMKAL LESACPATVS CADILTIAAE ESVVLAGGPN WTVPLGRRDS
160 170 180 190 200
TTASRAAANA SLPAPFLTLD QLRESFTNVG LNNNTDLVAL SGAHTFGRAK
210 220 230 240 250
CSTFNFRLYD FNGTGAPDPT LDPPFLAALQ ELCPQGGNDS VITDLDLTTP
260 270 280 290 300
DAFDSNYYSN LQCNRGLLQT DQELFSTPGA DDVIALVNAF SANQTAFFES
310 320 330 340
FVESMIRMGN LSPLTGTEGE IRLNCSVVNA NLAGPDSMLV SSI
Length:343
Mass (Da):36,576
Last modified:November 1, 1996 - v1
Checksum:iAB5C26E00627FC95
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97348 mRNA. Translation: CAA66034.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97348 mRNA. Translation: CAA66034.1.

3D structure databases

ProteinModelPortaliQ43099.
SMRiQ43099. Positions 25-331.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

PeroxiBasei911. PtPrx11_Trichobel.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00458. PEROXIDASE.
PR00461. PLPEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The syringaldazine-oxidizing peroxidase PXP 3-4 from poplar xylem: cDNA isolation, characterization and expression."
    Christensen J.H., Overney S., Rohde A., Diaz W.A., Bauw G., Simon P., Van Montagu M., Boerjan W.
    Plant Mol. Biol. 47:581-593(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: XylemImported.

Entry informationi

Entry nameiQ43099_POPTR
AccessioniPrimary (citable) accession number: Q43099
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.