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Protein

Peroxidase

Gene

Prx5

Organism
Hordeum vulgare (Barley)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi207 – 2071Iron (heme axial ligand); via tele nitrogenCombined sources
Metal bindingi208 – 2081CalciumCombined sources
Metal bindingi253 – 2531CalciumCombined sources
Metal bindingi256 – 2561CalciumCombined sources
Metal bindingi259 – 2591Calcium; via carbonyl oxygenCombined sources
Metal bindingi261 – 2611CalciumCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxideUniRule annotation

Keywords - Ligandi

CalciumUniRule annotationCombined sources, HemeUniRule annotationCombined sourcesSAAS annotation, Iron, Metal-binding

Protein family/group databases

PeroxiBasei68. HvPrx101.

Names & Taxonomyi

Protein namesi
Recommended name:
PeroxidaseUniRule annotationSAAS annotation (EC:1.11.1.7UniRule annotationSAAS annotation)
Gene namesi
Name:Prx5Imported
OrganismiHordeum vulgare (Barley)Imported
Taxonomic identifieri4513 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeHordeinaeHordeum

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 – 2828UniRule annotationAdd
BLAST
Chaini29 – 359331PeroxidaseUniRule annotationPRO_5005143295Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 127Combined sources
Disulfide bondi79 ↔ 84Combined sources
Disulfide bondi134 ↔ 329Combined sources
Disulfide bondi214 ↔ 241Combined sources

Keywords - PTMi

Disulfide bondSAAS annotation

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BGPX-ray1.90A29-337[»]
ProteinModelPortaliQ40069.
SMRiQ40069. Positions 29-337.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ40069.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 333298PEROXIDASE_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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q40069-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARVPLLAAL VVAMAVLVAS SLGPRASAAE PPVAPGLSFD FYRRTCPRAE
60 70 80 90 100
SIVREFVQEA VRKDIGLAAG LLRLHFHDCF VQGCDASVLL DGSATGPGEQ
110 120 130 140 150
QAPPNLTLRP SAFKAVNDIR DRLERECRGA VVSCSDILAL AARDSVVVSG
160 170 180 190 200
GPDYRVPLGR RDSRSFASTQ DVLSDLPGPS SNVQSLLALL GRLGLDATDL
210 220 230 240 250
VTISGGHTIG LAHCSSFEDR LFPRPDPTIS PTFLSRLKRT CPVKGTDRRT
260 270 280 290 300
VLDVRTPNVF DNKYYIDLVN REGLFVSDQD LFTNAITRPI VERFARSQQD
310 320 330 340 350
FFEQFGVSIG KMGQMRVRTS DQGEVRRNCS VRNPGPGADA LQWPSLVQTI

VDEAAGSIG
Length:359
Mass (Da):38,820
Last modified:November 1, 1996 - v1
Checksum:iAD94411156C2C767
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73234 mRNA. Translation: AAA32973.1.
PIRiS22505.
UniGeneiHv.519.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73234 mRNA. Translation: AAA32973.1.
PIRiS22505.
UniGeneiHv.519.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BGPX-ray1.90A29-337[»]
ProteinModelPortaliQ40069.
SMRiQ40069. Positions 29-337.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

PeroxiBasei68. HvPrx101.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ40069.

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. "cDNA cloning, characterization and expression of an endosperm-specific barley peroxidase."
    Rasmussen S.K., Welinder K.G., Hejgaard J.
    Plant Mol. Biol. 16:317-327(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: SeedImported.
  2. "cDNA, amino acid and carbohydrate sequence of barley seed-specific peroxidase BP 1."
    Johansson A., Rasmussen S.K., Harthill J.E., Welinder K.G.
    Plant Mol. Biol. 18:1151-1161(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: SeedImported.
  3. "Structure of barley grain peroxidase refined at 1.9-A resolution. A plant peroxidase reversibly inactivated at neutral pH."
    Henriksen A., Welinder K.G., Gajhede M.
    J. Biol. Chem. 273:2241-2248(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 29-337 IN COMPLEX WITH CALCIUM AND HEME, DISULFIDE BONDS.

Entry informationi

Entry nameiQ40069_HORVU
AccessioniPrimary (citable) accession number: Q40069
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.