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Protein

Cationic peroxidase 1

Gene

PNC1

Organism
Arachis hypogaea (Peanut)
Status
Reviewed-Annotation score: Annotation score: 5 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. These functions might be dependent on each isozyme/isoform in each plant tissue.

Catalytic activityi

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

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei60 – 601Transition state stabilizer
Active sitei64 – 641Proton acceptor
Metal bindingi65 – 651Calcium 1
Metal bindingi68 – 681Calcium 1; via carbonyl oxygen
Metal bindingi70 – 701Calcium 1; via carbonyl oxygen
Metal bindingi72 – 721Calcium 1
Metal bindingi74 – 741Calcium 1
Metal bindingi191 – 1911Iron (heme axial ligand)
Metal bindingi192 – 1921Calcium 2
Metal bindingi236 – 2361Calcium 2
Metal bindingi239 – 2391Calcium 2
Metal bindingi242 – 2421Calcium 2; via carbonyl oxygen
Metal bindingi244 – 2441Calcium 2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding

Protein family/group databases

PeroxiBasei102. AhPrx04.

Names & Taxonomyi

Protein namesi
Recommended name:
Cationic peroxidase 1 (EC:1.11.1.7)
Alternative name(s):
PNPC1
Gene namesi
Name:PNC1
OrganismiArachis hypogaea (Peanut)
Taxonomic identifieri3818 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeDalbergieaeArachis

Subcellular locationi

  • Secreted PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Chaini23 – 316294Cationic peroxidase 1PRO_0000023746Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231Pyrrolidone carboxylic acid
Disulfide bondi33 ↔ 113
Disulfide bondi66 ↔ 71
Glycosylationi82 – 821N-linked (GlcNAc...)
Disulfide bondi119 ↔ 312
Glycosylationi166 – 1661N-linked (GlcNAc...)CAR_000185
Disulfide bondi198 ↔ 223

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

PTM databases

UniCarbKBiP22195.

Structurei

Secondary structure

1
316
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni26 – 327Combined sources
Helixi36 – 5015Combined sources
Helixi53 – 6614Combined sources
Turni67 – 693Combined sources
Beta strandi70 – 734Combined sources
Helixi74 – 763Combined sources
Turni90 – 956Combined sources
Helixi99 – 11214Combined sources
Turni114 – 1163Combined sources
Helixi119 – 13315Combined sources
Helixi153 – 1597Combined sources
Helixi167 – 1759Combined sources
Turni176 – 1783Combined sources
Helixi181 – 1888Combined sources
Helixi189 – 1924Combined sources
Beta strandi195 – 1973Combined sources
Helixi198 – 20710Combined sources
Beta strandi209 – 2113Combined sources
Helixi213 – 2208Combined sources
Beta strandi225 – 2273Combined sources
Beta strandi232 – 2354Combined sources
Beta strandi237 – 2393Combined sources
Helixi246 – 2527Combined sources
Helixi259 – 2635Combined sources
Beta strandi265 – 2684Combined sources
Helixi271 – 2799Combined sources
Helixi281 – 29515Combined sources
Beta strandi305 – 3073Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SCHX-ray2.56A/B24-316[»]
ProteinModelPortaliP22195.
SMRiP22195. Positions 23-316.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22195.

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Signal

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.

P22195-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALPISKVDF LIFMCLIGLG SAQLSSNFYA TKCPNALSTI KSAVNSAVAK
60 70 80 90 100
EARMGASLLR LHFHDCFVQG CDASVLLDDT SNFTGEKTAG PNANSIRGFE
110 120 130 140 150
VIDTIKSQVE SLCPGVVSCA DILAVAARDS VVALGGASWN VLLGRRDSTT
160 170 180 190 200
ASLSSANSDL PAPFFNLSGL ISAFSNKGFT TKELVTLSGA HTIGQAQCTA
210 220 230 240 250
FRTRIYNESN IDPTYAKSLQ ANCPSVGGDT NLSPFDVTTP NKFDNAYYIN
260 270 280 290 300
LRNKKGLLHS DQQLFNGVST DSQVTAYSNN AATFNTDFGN AMIKMGNLSP
310
LTGTSGQIRT NCRKTN
Length:316
Mass (Da):33,518
Last modified:July 15, 1999 - v2
Checksum:i2CC271F8E8B8C9F0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M37636 mRNA. Translation: AAB06183.1.
PIRiA38265.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M37636 mRNA. Translation: AAB06183.1.
PIRiA38265.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SCHX-ray2.56A/B24-316[»]
ProteinModelPortaliP22195.
SMRiP22195. Positions 23-316.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

PeroxiBasei102. AhPrx04.

PTM databases

UniCarbKBiP22195.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP22195.

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. "Molecular cloning of complementary DNAs encoding two cationic peroxidases from cultivated peanut cells."
    Buffard D., Breda C., van Huystee R.B., Asemota O., Pierre M., Dang Ha D.B., Esnault R.
    Proc. Natl. Acad. Sci. U.S.A. 87:8874-8878(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Esnault R.
    Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 47.
  3. Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).

Entry informationi

Entry nameiPER1_ARAHY
AccessioniPrimary (citable) accession number: P22195
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: July 15, 1999
Last modified: October 14, 2015
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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.