Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Sitei60Transition state stabilizer1
Active sitei64Proton acceptor1
Metal bindingi65Calcium 11
Metal bindingi68Calcium 1; via carbonyl oxygen1
Metal bindingi70Calcium 1; via carbonyl oxygen1
Metal bindingi72Calcium 11
Metal bindingi74Calcium 11
Metal bindingi191Iron (heme axial ligand)1
Metal bindingi192Calcium 21
Metal bindingi236Calcium 21
Metal bindingi239Calcium 21
Metal bindingi242Calcium 2; via carbonyl oxygen1
Metal bindingi244Calcium 21

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
ChainiPRO_000002374623 – 316Cationic peroxidase 1Add BLAST294

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei23Pyrrolidone carboxylic acid1
Disulfide bondi33 ↔ 113
Disulfide bondi66 ↔ 71
Glycosylationi82N-linked (GlcNAc...)1
Disulfide bondi119 ↔ 312
GlycosylationiCAR_000185166N-linked (GlcNAc...)1
Disulfide bondi198 ↔ 223

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PRIDEiP22195.

PTM databases

UniCarbKBiP22195.

Structurei

Secondary structure

1316
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni26 – 32Combined sources7
Helixi36 – 50Combined sources15
Helixi53 – 66Combined sources14
Turni67 – 69Combined sources3
Beta strandi70 – 73Combined sources4
Helixi74 – 76Combined sources3
Turni90 – 95Combined sources6
Helixi99 – 112Combined sources14
Turni114 – 116Combined sources3
Helixi119 – 133Combined sources15
Helixi153 – 159Combined sources7
Helixi167 – 175Combined sources9
Turni176 – 178Combined sources3
Helixi181 – 188Combined sources8
Helixi189 – 192Combined sources4
Beta strandi195 – 197Combined sources3
Helixi198 – 207Combined sources10
Beta strandi209 – 211Combined sources3
Helixi213 – 220Combined sources8
Beta strandi225 – 227Combined sources3
Beta strandi232 – 235Combined sources4
Beta strandi237 – 239Combined sources3
Helixi246 – 252Combined sources7
Helixi259 – 263Combined sources5
Beta strandi265 – 268Combined sources4
Helixi271 – 279Combined sources9
Helixi281 – 295Combined sources15
Beta strandi305 – 307Combined sources3

3D structure databases

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

CDDicd00693. secretory_peroxidase. 1 hit.
InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
IPR033905. Secretory_peroxidase.
[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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SCHX-ray2.56A/B24-316[»]
ProteinModelPortaliP22195.
SMRiP22195.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

PeroxiBasei102. AhPrx04.

PTM databases

UniCarbKBiP22195.

Proteomic databases

PRIDEiP22195.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP22195.

Family and domain databases

CDDicd00693. secretory_peroxidase. 1 hit.
InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
IPR033905. Secretory_peroxidase.
[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...

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: November 30, 2016
This is version 103 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.