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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)LengthDescriptionGraphical viewFeature identifierActions
Sitei68 – 681Transition state stabilizer
Active sitei72 – 721Proton acceptor
Metal bindingi73 – 731Calcium 1
Metal bindingi76 – 761Calcium 1; via carbonyl oxygen
Metal bindingi78 – 781Calcium 1; via carbonyl oxygen
Metal bindingi80 – 801Calcium 1
Metal bindingi82 – 821Calcium 1
Metal bindingi94 – 941Calcium 1
Binding sitei169 – 1691Substrate; via carbonyl oxygen
Metal bindingi200 – 2001Iron (heme axial ligand)
Metal bindingi201 – 2011Calcium 2
Metal bindingi252 – 2521Calcium 2
Metal bindingi255 – 2551Calcium 2
Metal bindingi260 – 2601Calcium 2

GO - Molecular functioni

  1. heme binding Source: InterPro
  2. metal ion binding Source: UniProtKB-KW
  3. peroxidase activity Source: UniProtKB-KW

GO - Biological processi

  1. hydrogen peroxide catabolic process Source: UniProtKB-KW
  2. response to oxidative stress Source: InterPro
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

  1. Secreted Curated
  2. Vacuole Curated

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

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
  2. vacuole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 30301 PublicationAdd
BLAST
Chaini31 – 338308Peroxidase C1A1 PublicationPRO_0000023739Add
BLAST
Propeptidei339 – 35315PRO_0000023740Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei31 – 311Pyrrolidone carboxylic acidPROSITE-ProRule annotation1 Publication
Disulfide bondi41 ↔ 121PROSITE-ProRule annotation1 Publication
Glycosylationi43 – 431N-linked (GlcNAc...)1 Publication
Disulfide bondi74 ↔ 79PROSITE-ProRule annotation1 Publication
Glycosylationi87 – 871N-linked (GlcNAc...)1 Publication
Disulfide bondi127 ↔ 331
Glycosylationi188 – 1881N-linked (GlcNAc...)
Disulfide bondi207 ↔ 239
Glycosylationi216 – 2161N-linked (GlcNAc...)
Glycosylationi228 – 2281N-linked (GlcNAc...)
Glycosylationi244 – 2441N-linked (GlcNAc...)
Glycosylationi285 – 2851N-linked (GlcNAc...)
Glycosylationi298 – 2981N-linked (GlcNAc...)

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

PTM databases

UniCarbKBiP00433.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
353
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni34 – 407Combined sources
Helixi44 – 5815Combined sources
Helixi62 – 7413Combined sources
Turni75 – 773Combined sources
Beta strandi78 – 814Combined sources
Helixi82 – 843Combined sources
Beta strandi89 – 913Combined sources
Helixi94 – 963Combined sources
Turni98 – 1036Combined sources
Helixi107 – 12014Combined sources
Turni122 – 1243Combined sources
Helixi127 – 14115Combined sources
Helixi161 – 1677Combined sources
Helixi175 – 18410Combined sources
Helixi190 – 1978Combined sources
Helixi198 – 2014Combined sources
Beta strandi204 – 2063Combined sources
Helixi207 – 2104Combined sources
Helixi211 – 2155Combined sources
Helixi217 – 2193Combined sources
Beta strandi220 – 2223Combined sources
Helixi229 – 23810Combined sources
Beta strandi248 – 2514Combined sources
Beta strandi253 – 2553Combined sources
Helixi262 – 2687Combined sources
Helixi275 – 2828Combined sources
Turni284 – 2885Combined sources
Helixi289 – 29810Combined sources
Helixi300 – 31415Combined sources
Beta strandi324 – 3263Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 31-337.
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

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.

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
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. Positions 31-337.
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

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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Covalent structure of the glycoprotein horseradish peroxidase (EC 1.11.1.7)."
    Welinder K.G.
    FEBS Lett. 72:19-23(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 31-338.
  3. "Crystal structure of horseradish peroxidase C at 2.15-A resolution."
    Gajhede M., Schuller D.J., Henriksen A., Smith A.T., Poulos T.L.
    Nat. Struct. Biol. 4:1032-1038(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
  4. "Structural interactions between horseradish peroxidase C and the substrate benzhydroxamic acid determined by X-ray crystallography."
    Henriksen A., Schuller D.J., Meno K., Welinder K.G., Smith A.T., Gajhede M.
    Biochemistry 37:8054-8060(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  5. Meno K., White C.G., Smith A.T., Gajhede M.
    Submitted (DEC-1998) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

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: April 1, 2015
This is version 118 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

External Data

Dasty 3

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 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.