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Q9MB14

- PPO2_IPOBA

UniProt

Q9MB14 - PPO2_IPOBA

Protein

Polyphenol oxidase II, chloroplastic

Gene

co-2

Organism
Ipomoea batatas (Sweet potato) (Convolvulus batatas)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 2 (29 Mar 2005)
      Previous versions | rss
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    Functioni

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

    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 bindingi178 – 1781Copper ABy similarity
    Metal bindingi199 – 1991Copper ABy similarity
    Metal bindingi208 – 2081Copper ABy similarity
    Metal bindingi330 – 3301Copper BBy similarity
    Metal bindingi334 – 3341Copper BBy similarity
    Metal bindingi366 – 3661Copper 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 II, chloroplastic (EC:1.10.3.1)
    Short name:
    PPO-II
    Alternative name(s):
    Catechol oxidase II
    Gene namesi
    Name:co-2
    Synonyms:ppo-I
    OrganismiIpomoea batatas (Sweet potato) (Convolvulus batatas)
    Taxonomic identifieri4120 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesConvolvulaceaeIpomoeeaeIpomoea

    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 – 5050ChloroplastSequence AnalysisAdd
    BLAST
    Transit peptidei51 – 8838ThylakoidBy similarityAdd
    BLAST
    Chaini89 – 588500Polyphenol oxidase II, chloroplasticPRO_0000035909Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi99 ↔ 116By similarity
    Disulfide bondi115 ↔ 179By similarity
    Cross-linki182 ↔ 1992'-(S-cysteinyl)-histidine (Cys-His)By similarity

    Keywords - PTMi

    Disulfide bond, Thioether bond

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ9MB14.
    SMRiQ9MB14. Positions 90-433.
    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.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9MB14-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASFTTSPCT SAAPKTPKSL SSSATISSPL PKPSQIHIAT AKRTHHFKVS    50
    CNAPNGDSQP KLDRRDVLLG LGGLAGAASL INNPLAFAEP IHAPEISKCV 100
    VPPKDLPPDA IVDNCCPPLA TNVIPYKVPK TSPSAMKIRP AIHRMDKEYI 150
    AKFEKAIRLM KELPADDPRN FYQQALVHCA YCNGGYVQTD YPDKEIQVHN 200
    SWLFFPFHRW YLYFYERILG KLIGDPTFGL PFWNWDTPAG MLIPQYFRNQ 250
    NSPLYDENRN QSHLPLVMDL GYAGTDTDVT DQERISNNLA LMYKSMVTNA 300
    GTAELFLGKP YKAGDDPVNK GGGSIENIPH TPVHRWVGDV KPRTQNGEDM 350
    GNFYSAGRDI LFYCHHSNVD RMWTIWQQLG GKGRRRDFTD SDWLDATFIF 400
    YDENKQAVRV RVGDALDNQK LGYKYEFTNL PWLNSKPLPT KKKTGLAARS 450
    KAPFVTDVFP LTLDKVVQVK VPRPKKSRSK EEKEAEEEIL EIQGIEVAID 500
    QYAKFDVYLN DEDEPEAGKE KAEYAGSFAH LPHKHTGSKK IRTSLSLGLN 550
    EPLEDLGAED DDAVLVTLAP KVGGGVVTVE NIKIVYGS 588
    Length:588
    Mass (Da):65,651
    Last modified:March 29, 2005 - v2
    Checksum:iF0DF1A03FDC33AC2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti130 – 1301K → R in CAC29040. 1 PublicationCurated
    Sequence conflicti277 – 2771T → N in CAC29040. 1 PublicationCurated
    Sequence conflicti493 – 4931Q → E in BAA92317. 1 PublicationCurated
    Sequence conflicti563 – 5631A → P in CAC83610. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB038994 mRNA. Translation: BAA92317.1.
    AJ245880 mRNA. Translation: CAC29040.1.
    AJ309176 Genomic DNA. Translation: CAC83610.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB038994 mRNA. Translation: BAA92317.1 .
    AJ245880 mRNA. Translation: CAC29040.1 .
    AJ309176 Genomic DNA. Translation: CAC83610.1 .

    3D structure databases

    ProteinModelPortali Q9MB14.
    SMRi Q9MB14. Positions 90-433.
    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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Ipomoea batatas polyphenol oxidase I mRNA."
      Hashimoto H., Nozue M., Tanaka I.
      Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Sequence and structural implications of two isozymes of Ipomoea batatas catechol oxidase differing in catalase activity."
      Gerdemann C., Eicken C., Magrini A., Meier H.E., Spener F., Krebs B.
      Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 89-588.
      Strain: cv. Bushbuck.
      Tissue: Root.
    3. "Sequencing and cloning of genomic DNA encoding two isozymes of Ipomoea batatas catechol oxidase."
      Greving J., Gerdemann C., Spener F., Krebs B.
      Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 89-588.
      Strain: cv. Bushbuck.

    Entry informationi

    Entry nameiPPO2_IPOBA
    AccessioniPrimary (citable) accession number: Q9MB14
    Secondary accession number(s): Q84V52, Q9ARD3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: March 29, 2005
    Last modified: October 1, 2014
    This is version 52 of the entry and version 2 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