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P00433

- PER1A_ARMRU

UniProt

P00433 - PER1A_ARMRU

Protein

Peroxidase C1A

Gene

PRXC1A

Organism
Armoracia rusticana (Horseradish) (Armoracia laphatifolia)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (01 Apr 1990)
      Previous versions | rss
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    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

    Binds 2 calcium ions per subunit.
    Binds 1 heme B (iron-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

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Keywords - Biological processi

    Hydrogen peroxide

    Keywords - Ligandi

    Calcium, Heme, Iron, Metal-binding

    Enzyme and pathway databases

    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

    1. extracellular region Source: UniProtKB-SubCell
    2. vacuole Source: UniProtKB-SubCell

    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 acid1 PublicationPROSITE-ProRule annotation
    Disulfide bondi41 ↔ 1211 PublicationPROSITE-ProRule annotation
    Glycosylationi43 – 431N-linked (GlcNAc...)1 Publication
    Disulfide bondi74 ↔ 791 PublicationPROSITE-ProRule annotation
    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 – 407
    Helixi44 – 5815
    Helixi62 – 7413
    Turni75 – 773
    Beta strandi78 – 814
    Helixi82 – 843
    Beta strandi89 – 913
    Helixi94 – 963
    Turni98 – 1036
    Helixi107 – 12014
    Turni122 – 1243
    Helixi127 – 14115
    Helixi161 – 1677
    Helixi175 – 18410
    Helixi190 – 1978
    Helixi198 – 2014
    Beta strandi204 – 2063
    Helixi207 – 2104
    Helixi211 – 2155
    Helixi217 – 2193
    Beta strandi220 – 2223
    Helixi229 – 23810
    Beta strandi248 – 2514
    Beta strandi253 – 2553
    Helixi262 – 2687
    Helixi275 – 2828
    Turni284 – 2885
    Helixi289 – 29810
    Helixi300 – 31415
    Beta strandi324 – 3263

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MHFSSSSTLF TCITLIPLVC LILHASLSDA QLTPTFYDNS CPNVSNIVRD    50
    TIVNELRSDP RIAASILRLH FHDCFVNGCD ASILLDNTTS FRTEKDAFGN 100
    ANSARGFPVI DRMKAAVESA CPRTVSCADL LTIAAQQSVT LAGGPSWRVP 150
    LGRRDSLQAF LDLANANLPA PFFTLPQLKD SFRNVGLNRS SDLVALSGGH 200
    TFGKNQCRFI MDRLYNFSNT GLPDPTLNTT YLQTLRGLCP LNGNLSALVD 250
    FDLRTPTIFD NKYYVNLEEQ KGLIQSDQEL FSSPNATDTI PLVRSFANST 300
    QTFFNAFVEA MDRMGNITPL TGTQGQIRLN CRVVNSNSLL HDMVEVVDFV 350
    SSM 353
    Length:353
    Mass (Da):38,825
    Last modified:April 1, 1990 - v2
    Checksum:iAC916C03C4A24D27
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M37156 Genomic DNA. Translation: AAA33377.1.
    PIRiS00625. OPRHC.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M37156 Genomic DNA. Translation: AAA33377.1 .
    PIRi S00625. OPRHC.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ATJ X-ray 2.15 A/B/C/D/E/F 31-336 [» ]
    1GW2 X-ray 2.15 A 31-338 [» ]
    1GWO X-ray 2.07 A 31-338 [» ]
    1GWT X-ray 1.70 A 31-338 [» ]
    1GWU X-ray 1.31 A 31-338 [» ]
    1GX2 X-ray 2.20 A/B 31-338 [» ]
    1H55 X-ray 1.61 A 31-338 [» ]
    1H57 X-ray 1.60 A 31-338 [» ]
    1H58 X-ray 1.70 A 31-338 [» ]
    1H5A X-ray 1.60 A 31-338 [» ]
    1H5C X-ray 1.62 A 31-338 [» ]
    1H5D X-ray 1.60 A 31-338 [» ]
    1H5E X-ray 1.60 A 31-338 [» ]
    1H5F X-ray 1.60 A 31-338 [» ]
    1H5G X-ray 1.57 A 31-338 [» ]
    1H5H X-ray 1.60 A 31-338 [» ]
    1H5I X-ray 1.60 A 31-338 [» ]
    1H5J X-ray 1.60 A 31-338 [» ]
    1H5K X-ray 1.60 A 31-338 [» ]
    1H5L X-ray 1.60 A 31-338 [» ]
    1H5M X-ray 1.57 A 31-338 [» ]
    1HCH X-ray 1.57 A 31-336 [» ]
    1KZM X-ray 2.00 A 31-338 [» ]
    1W4W X-ray 1.55 A 31-353 [» ]
    1W4Y X-ray 1.60 A 31-353 [» ]
    2ATJ X-ray 2.00 A/B 31-337 [» ]
    2YLJ X-ray 1.69 A 31-336 [» ]
    3ATJ X-ray 2.20 A/B 31-338 [» ]
    4ATJ X-ray 2.50 A/B 31-338 [» ]
    6ATJ X-ray 2.00 A 31-338 [» ]
    7ATJ X-ray 1.47 A 31-338 [» ]
    ProteinModelPortali P00433.
    SMRi P00433. Positions 31-337.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    PeroxiBasei 90. AruPrx01-1.

    PTM databases

    UniCarbKBi P00433.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P00433.

    Miscellaneous databases

    EvolutionaryTracei P00433.

    Family and domain databases

    InterProi IPR010255. Haem_peroxidase.
    IPR002016. Haem_peroxidase_pln/fun/bac.
    IPR000823. Peroxidase_pln.
    IPR019794. Peroxidases_AS.
    IPR019793. Peroxidases_heam-ligand_BS.
    [Graphical view ]
    Pfami PF00141. peroxidase. 1 hit.
    [Graphical view ]
    PRINTSi PR00458. PEROXIDASE.
    PR00461. PLPEROXIDASE.
    SUPFAMi SSF48113. SSF48113. 1 hit.
    PROSITEi PS00435. PEROXIDASE_1. 1 hit.
    PS00436. PEROXIDASE_2. 1 hit.
    PS50873. PEROXIDASE_4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 113 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