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Protein

Peroxidase C1A

Gene

PRXC1A

Organism
Armoracia rusticana (Horseradish) (Armoracia laphatifolia)
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
Sitei68Transition state stabilizer1
Active sitei72Proton acceptor1
Metal bindingi73Calcium 11
Metal bindingi76Calcium 1; via carbonyl oxygen1
Metal bindingi78Calcium 1; via carbonyl oxygen1
Metal bindingi80Calcium 11
Metal bindingi82Calcium 11
Metal bindingi94Calcium 11
Binding sitei169Substrate; via carbonyl oxygen1
Metal bindingi200Iron (heme axial ligand)1
Metal bindingi201Calcium 21
Metal bindingi252Calcium 21
Metal bindingi255Calcium 21
Metal bindingi260Calcium 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

Enzyme and pathway databases

BRENDAi1.11.1.7. 429.
SABIO-RKP00433.

Protein family/group databases

PeroxiBasei90. AruPrx01-1.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxidase C1A (EC:1.11.1.7)
Gene namesi
Name:PRXC1A
Synonyms:HPRC1
OrganismiArmoracia rusticana (Horseradish) (Armoracia laphatifolia)
Taxonomic identifieri3704 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCardamineaeArmoracia

Subcellular locationi

  • Secreted Curated
  • Vacuole Curated

  • Note: Carboxy-terminal extension appears to target the protein to vacuoles.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 301 PublicationAdd BLAST30
ChainiPRO_000002373931 – 338Peroxidase C1A1 PublicationAdd BLAST308
PropeptideiPRO_0000023740339 – 353Add BLAST15

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei31Pyrrolidone carboxylic acidPROSITE-ProRule annotation1 Publication1
Disulfide bondi41 ↔ 121PROSITE-ProRule annotation1 Publication
Glycosylationi43N-linked (GlcNAc...)1 Publication1
Disulfide bondi74 ↔ 79PROSITE-ProRule annotation1 Publication
Glycosylationi87N-linked (GlcNAc...)1 Publication1
Disulfide bondi127 ↔ 331
Glycosylationi188N-linked (GlcNAc...)1
Disulfide bondi207 ↔ 239
Glycosylationi216N-linked (GlcNAc...)1
Glycosylationi228N-linked (GlcNAc...)1
Glycosylationi244N-linked (GlcNAc...)1
Glycosylationi285N-linked (GlcNAc...)1
Glycosylationi298N-linked (GlcNAc...)1

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

PTM databases

UniCarbKBiP00433.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1353
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni34 – 40Combined sources7
Helixi44 – 58Combined sources15
Helixi62 – 74Combined sources13
Turni75 – 77Combined sources3
Beta strandi78 – 81Combined sources4
Helixi82 – 84Combined sources3
Beta strandi89 – 91Combined sources3
Helixi94 – 96Combined sources3
Turni98 – 103Combined sources6
Helixi107 – 120Combined sources14
Turni122 – 124Combined sources3
Helixi127 – 141Combined sources15
Helixi161 – 167Combined sources7
Helixi175 – 184Combined sources10
Helixi190 – 197Combined sources8
Helixi198 – 201Combined sources4
Beta strandi204 – 206Combined sources3
Helixi207 – 210Combined sources4
Helixi211 – 215Combined sources5
Helixi217 – 219Combined sources3
Beta strandi220 – 222Combined sources3
Helixi229 – 238Combined sources10
Beta strandi248 – 251Combined sources4
Beta strandi253 – 255Combined sources3
Helixi262 – 268Combined sources7
Helixi275 – 282Combined sources8
Turni284 – 288Combined sources5
Helixi289 – 298Combined sources10
Helixi300 – 314Combined sources15
Beta strandi324 – 326Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ATJX-ray2.15A/B/C/D/E/F31-336[»]
1GW2X-ray2.15A31-338[»]
1GWOX-ray2.07A31-338[»]
1GWTX-ray1.70A31-338[»]
1GWUX-ray1.31A31-338[»]
1GX2X-ray2.20A/B31-338[»]
1H55X-ray1.61A31-338[»]
1H57X-ray1.60A31-338[»]
1H58X-ray1.70A31-338[»]
1H5AX-ray1.60A31-338[»]
1H5CX-ray1.62A31-338[»]
1H5DX-ray1.60A31-338[»]
1H5EX-ray1.60A31-338[»]
1H5FX-ray1.60A31-338[»]
1H5GX-ray1.57A31-338[»]
1H5HX-ray1.60A31-338[»]
1H5IX-ray1.60A31-338[»]
1H5JX-ray1.60A31-338[»]
1H5KX-ray1.60A31-338[»]
1H5LX-ray1.60A31-338[»]
1H5MX-ray1.57A31-338[»]
1HCHX-ray1.57A31-336[»]
1KZMX-ray2.00A31-338[»]
1W4WX-ray1.55A31-353[»]
1W4YX-ray1.60A31-353[»]
2ATJX-ray2.00A/B31-337[»]
2YLJX-ray1.69A31-336[»]
3ATJX-ray2.20A/B31-338[»]
4ATJX-ray2.50A/B31-338[»]
6ATJX-ray2.00A31-338[»]
7ATJX-ray1.47A31-338[»]
ProteinModelPortaliP00433.
SMRiP00433.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00433.

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.

P00433-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHFSSSSTLF TCITLIPLVC LILHASLSDA QLTPTFYDNS CPNVSNIVRD
60 70 80 90 100
TIVNELRSDP RIAASILRLH FHDCFVNGCD ASILLDNTTS FRTEKDAFGN
110 120 130 140 150
ANSARGFPVI DRMKAAVESA CPRTVSCADL LTIAAQQSVT LAGGPSWRVP
160 170 180 190 200
LGRRDSLQAF LDLANANLPA PFFTLPQLKD SFRNVGLNRS SDLVALSGGH
210 220 230 240 250
TFGKNQCRFI MDRLYNFSNT GLPDPTLNTT YLQTLRGLCP LNGNLSALVD
260 270 280 290 300
FDLRTPTIFD NKYYVNLEEQ KGLIQSDQEL FSSPNATDTI PLVRSFANST
310 320 330 340 350
QTFFNAFVEA MDRMGNITPL TGTQGQIRLN CRVVNSNSLL HDMVEVVDFV

SSM
Length:353
Mass (Da):38,825
Last modified:April 1, 1990 - v2
Checksum:iAC916C03C4A24D27
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M37156 Genomic DNA. Translation: AAA33377.1.
PIRiS00625. OPRHC.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M37156 Genomic DNA. Translation: AAA33377.1.
PIRiS00625. OPRHC.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ATJX-ray2.15A/B/C/D/E/F31-336[»]
1GW2X-ray2.15A31-338[»]
1GWOX-ray2.07A31-338[»]
1GWTX-ray1.70A31-338[»]
1GWUX-ray1.31A31-338[»]
1GX2X-ray2.20A/B31-338[»]
1H55X-ray1.61A31-338[»]
1H57X-ray1.60A31-338[»]
1H58X-ray1.70A31-338[»]
1H5AX-ray1.60A31-338[»]
1H5CX-ray1.62A31-338[»]
1H5DX-ray1.60A31-338[»]
1H5EX-ray1.60A31-338[»]
1H5FX-ray1.60A31-338[»]
1H5GX-ray1.57A31-338[»]
1H5HX-ray1.60A31-338[»]
1H5IX-ray1.60A31-338[»]
1H5JX-ray1.60A31-338[»]
1H5KX-ray1.60A31-338[»]
1H5LX-ray1.60A31-338[»]
1H5MX-ray1.57A31-338[»]
1HCHX-ray1.57A31-336[»]
1KZMX-ray2.00A31-338[»]
1W4WX-ray1.55A31-353[»]
1W4YX-ray1.60A31-353[»]
2ATJX-ray2.00A/B31-337[»]
2YLJX-ray1.69A31-336[»]
3ATJX-ray2.20A/B31-338[»]
4ATJX-ray2.50A/B31-338[»]
6ATJX-ray2.00A31-338[»]
7ATJX-ray1.47A31-338[»]
ProteinModelPortaliP00433.
SMRiP00433.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

PeroxiBasei90. AruPrx01-1.

PTM databases

UniCarbKBiP00433.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.11.1.7. 429.
SABIO-RKP00433.

Miscellaneous databases

EvolutionaryTraceiP00433.

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 nameiPER1A_ARMRU
AccessioniPrimary (citable) accession number: P00433
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1990
Last modified: November 30, 2016
This is version 125 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, Direct protein sequencing

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.