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Q06215

- PPO_VICFA

UniProt

Q06215 - PPO_VICFA

Protein

Polyphenol oxidase A1, chloroplastic

Gene
N/A
Organism
Vicia faba (Broad bean) (Faba vulgaris)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Catalyzes the oxidation of mono- and o-diphenols to o-diquinones.

    Catalytic activityi

    2 catechol + O2 = 2 1,2-benzoquinone + 2 H2O.

    Cofactori

    Binds 2 copper ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi181 – 1811Copper ABy similarity
    Metal bindingi202 – 2021Copper ABy similarity
    Metal bindingi211 – 2111Copper ABy similarity
    Metal bindingi333 – 3331Copper BBy similarity
    Metal bindingi337 – 3371Copper BBy similarity
    Metal bindingi367 – 3671Copper BBy similarity

    GO - Molecular functioni

    1. catechol oxidase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. pigment biosynthetic process Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Copper, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polyphenol oxidase A1, chloroplastic (EC:1.10.3.1)
    Short name:
    PPO
    Alternative name(s):
    Catechol oxidase
    OrganismiVicia faba (Broad bean) (Faba vulgaris)
    Taxonomic identifieri3906 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaeVicia

    Subcellular locationi

    GO - Cellular componenti

    1. chloroplast thylakoid lumen Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Plastid, Thylakoid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 9292ChloroplastAdd
    BLAST
    Chaini93 – 606514Polyphenol oxidase A1, chloroplasticPRO_0000035919Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi103 ↔ 121By similarity
    Disulfide bondi120 ↔ 182By similarity
    Cross-linki185 ↔ 2022'-(S-cysteinyl)-histidine (Cys-His)By similarity

    Keywords - PTMi

    Disulfide bond, Thioether bond

    Structurei

    3D structure databases

    ProteinModelPortaliQ06215.
    SMRiQ06215. Positions 93-431.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tyrosinase family.Curated

    Keywords - Domaini

    Transit peptide

    Family and domain databases

    Gene3Di1.10.1280.10. 1 hit.
    InterProiIPR016213. Polyphenol_oxidase.
    IPR022740. Polyphenol_oxidase_C.
    IPR022739. Polyphenol_oxidase_cen.
    IPR002227. Tyrosinase_Cu-bd.
    IPR008922. Unchr_di-copper_centre.
    [Graphical view]
    PfamiPF12142. PPO1_DWL. 1 hit.
    PF12143. PPO1_KFDV. 1 hit.
    PF00264. Tyrosinase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000290. PPO_plant. 1 hit.
    PRINTSiPR00092. TYROSINASE.
    SUPFAMiSSF48056. SSF48056. 1 hit.
    PROSITEiPS00497. TYROSINASE_1. 1 hit.
    PS00498. TYROSINASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q06215-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTSISALSFI STINVSSNSK ISHSSVYPFL QKQHQSSKLR KPKRQVTCSS    50
    NNNQNNPKEE QELSNIVGHR RNVLIGLGGI YGTLATNPSA LASPISPPDL 100
    SKCVPPSDLP SGTTPPNINC CPPYSTKITD FKFPSNQPLR VRQAAHLVDN 150
    EFLEKYKKAT ELMKALPSND PRNFTQQANI HCAYCDGAYS QIGFPDLKLQ 200
    VHGSWLFFPF HRWYLYFYER ILGSLINDPT FALPFWNYDA PDGMQLPTIY 250
    ADKASPLYDE LRNASHQPPT LIDLNFCDIG SDIDRNELIK TNLSIMYRQV 300
    YSNGKTSRLF LGNPYRAGDA EPQGAGSIEN VPHAPVHTWT GDNTQTNIED 350
    MGIFYSAARD PIFYSHHSNV DRLWYIWKTL GGKKHDFTDK DWLESGFLFY 400
    DENKNLVRVN VKDSLDIDKL GYAYQDVPIP WEKAKPVPRR TKVQKLVEVE 450
    VNDGNLRKSP TIFLVRQQSP RKYVTFPLVL NNKVSAIVKR PKKLRSKKEK 500
    EEEEEVLVIE GIEFYMNIAI KFDVYINDED DKVGAGNTEF AGSFVNIPHS 550
    AHGHKNKKII TSLRLGITDL LEDLHVEGDD NIVVTLVPKC GSGQVKINNV 600
    EIVFED 606
    Length:606
    Mass (Da):68,541
    Last modified:November 1, 1995 - v1
    Checksum:iFC539F9F041B503C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z11702 mRNA. Translation: CAA77764.1.
    PIRiS24758.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z11702 mRNA. Translation: CAA77764.1 .
    PIRi S24758.

    3D structure databases

    ProteinModelPortali Q06215.
    SMRi Q06215. Positions 93-431.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 1.10.1280.10. 1 hit.
    InterProi IPR016213. Polyphenol_oxidase.
    IPR022740. Polyphenol_oxidase_C.
    IPR022739. Polyphenol_oxidase_cen.
    IPR002227. Tyrosinase_Cu-bd.
    IPR008922. Unchr_di-copper_centre.
    [Graphical view ]
    Pfami PF12142. PPO1_DWL. 1 hit.
    PF12143. PPO1_KFDV. 1 hit.
    PF00264. Tyrosinase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000290. PPO_plant. 1 hit.
    PRINTSi PR00092. TYROSINASE.
    SUPFAMi SSF48056. SSF48056. 1 hit.
    PROSITEi PS00497. TYROSINASE_1. 1 hit.
    PS00498. TYROSINASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of cDNAs coding for Vicia faba polyphenol oxidase."
      Cary J.W., Lax A.R., Flurkey W.H.
      Plant Mol. Biol. 20:245-253(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Leaf.
    2. "Polypeptide composition and amino-terminal sequence of broad bean polyphenol oxidase."
      Flurkey W.H.
      Plant Physiol. 91:481-483(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY PROTEIN SEQUENCE OF 93-119.
      Tissue: Leaf.

    Entry informationi

    Entry nameiPPO_VICFA
    AccessioniPrimary (citable) accession number: Q06215
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 75 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3