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P43309

- PPO_MALDO

UniProt

P43309 - PPO_MALDO

Protein

Polyphenol oxidase, chloroplastic

Gene
N/A
Organism
Malus domestica (Apple) (Pyrus malus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 77 (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 bindingi175 – 1751Copper ABy similarity
    Metal bindingi196 – 1961Copper ABy similarity
    Metal bindingi205 – 2051Copper ABy similarity
    Metal bindingi327 – 3271Copper BBy similarity
    Metal bindingi331 – 3311Copper BBy similarity
    Metal bindingi361 – 3611Copper 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

    Enzyme and pathway databases

    SABIO-RKP43309.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polyphenol oxidase, chloroplastic (EC:1.10.3.1)
    Short name:
    PPO
    Alternative name(s):
    Catechol oxidase
    OrganismiMalus domestica (Apple) (Pyrus malus)
    Taxonomic identifieri3750 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeMaloideaeMaleaeMalus

    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 – 8989ChloroplastSequence AnalysisAdd
    BLAST
    Chaini90 – 593504Polyphenol oxidase, chloroplasticPRO_0000035916Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi100 ↔ 115By similarity
    Disulfide bondi114 ↔ 176By similarity
    Cross-linki179 ↔ 1962'-(S-cysteinyl)-histidine (Cys-His)By similarity

    Keywords - PTMi

    Disulfide bond, Thioether bond

    Structurei

    3D structure databases

    ProteinModelPortaliP43309.
    SMRiP43309. Positions 91-426.
    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.

    P43309-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTSLSPPVVT TPTVPNPATK PLSPFSQNNS QVSLLTKPKR SFARKVSCKA    50
    TNNDQNDQAQ SKLDRRNVLL GLGGLYGVAG MGTDPFAFAK PIAPPDVSKC 100
    GPADLPQGAV PTNCCPPPST KIIDFKLPAP AKLRIRPPAH AVDQAYRDKY 150
    YKAMELMKAL PDDDPRSFKQ QAAVHCAYCD GAYDQVGFPE LELQIHNSWL 200
    FFPFHRYYLY FFEKILGKLI NDPTFALPFW NWDSPAGMPL PAIYADPKSP 250
    LYDKLRSANH QPPTLVDLDY NGTEDNVSKE TTINANLKIM YRQMVSNSKN 300
    AKLFFGNPYR AGDEPDPGGG SIEGTPHAPV HLWTGDNTQP NFEDMGNFYS 350
    AGRDPIFFAH HSNVDRMWSI WKTLGGKRTD LTDSDWLDSG FLFYNENAEL 400
    VRVKVRDCLE TKNLGYVYQD VDIPWLSSKP TPRRAKVALS KVAKKLGVAH 450
    AAVASSSKVV AGTEFPISLG SKISTVVKRP KQKKRSKKAK EDEEEILVIE 500
    GIEFDRDVAV KFDVYVNDVD DLPSGPDKTE FAGSFVSVPH SHKHKKKMNT 550
    ILRLGLTDLL EEIEAEDDDS VVVTLVPKFG AVKIGGIKIE FAS 593
    Length:593
    Mass (Da):65,721
    Last modified:November 1, 1995 - v1
    Checksum:i545296ADB9DD13B9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29450 mRNA. Translation: AAA69902.1.
    PIRiS52984.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29450 mRNA. Translation: AAA69902.1 .
    PIRi S52984.

    3D structure databases

    ProteinModelPortali P43309.
    SMRi P43309. Positions 91-426.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P43309.

    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. "An apple polyphenol oxidase cDNA is up-regulated in wounded tissues."
      Boss P.K., Gardner R.C., Janssen B.-J., Ross G.S.
      Plant Mol. Biol. 27:429-433(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Skin.

    Entry informationi

    Entry nameiPPO_MALDO
    AccessioniPrimary (citable) accession number: P43309
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 77 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3