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P43309

- PPO_MALDO

UniProt

P43309 - PPO_MALDO

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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

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 A By similarity
Metal bindingi196 – 1961Copper A By similarity
Metal bindingi205 – 2051Copper A By similarity
Metal bindingi327 – 3271Copper B By similarity
Metal bindingi331 – 3311Copper B By similarity
Metal bindingi361 – 3611Copper B By 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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 8989Chloroplast Reviewed prediction
Add
BLAST
Chaini90 – 593504Polyphenol oxidase, chloroplastic
PRO_0000035916Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi100 ↔ 115 By similarity
Disulfide bondi114 ↔ 176 By 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.

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.

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: June 11, 2014
This is version 76 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

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