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Protein

Polyphenol oxidase, chloroplastic

Gene
N/A
Organism
Malus domestica (Apple) (Pyrus malus)
Status
Reviewed-Annotation score: 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

Cu2+By similarityNote: 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
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 – 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

        10         20         30         40         50
MTSLSPPVVT TPTVPNPATK PLSPFSQNNS QVSLLTKPKR SFARKVSCKA
60 70 80 90 100
TNNDQNDQAQ SKLDRRNVLL GLGGLYGVAG MGTDPFAFAK PIAPPDVSKC
110 120 130 140 150
GPADLPQGAV PTNCCPPPST KIIDFKLPAP AKLRIRPPAH AVDQAYRDKY
160 170 180 190 200
YKAMELMKAL PDDDPRSFKQ QAAVHCAYCD GAYDQVGFPE LELQIHNSWL
210 220 230 240 250
FFPFHRYYLY FFEKILGKLI NDPTFALPFW NWDSPAGMPL PAIYADPKSP
260 270 280 290 300
LYDKLRSANH QPPTLVDLDY NGTEDNVSKE TTINANLKIM YRQMVSNSKN
310 320 330 340 350
AKLFFGNPYR AGDEPDPGGG SIEGTPHAPV HLWTGDNTQP NFEDMGNFYS
360 370 380 390 400
AGRDPIFFAH HSNVDRMWSI WKTLGGKRTD LTDSDWLDSG FLFYNENAEL
410 420 430 440 450
VRVKVRDCLE TKNLGYVYQD VDIPWLSSKP TPRRAKVALS KVAKKLGVAH
460 470 480 490 500
AAVASSSKVV AGTEFPISLG SKISTVVKRP KQKKRSKKAK EDEEEILVIE
510 520 530 540 550
GIEFDRDVAV KFDVYVNDVD DLPSGPDKTE FAGSFVSVPH SHKHKKKMNT
560 570 580 590
ILRLGLTDLL EEIEAEDDDS VVVTLVPKFG AVKIGGIKIE FAS
Length:593
Mass (Da):65,721
Last modified:November 1, 1995 - v1
Checksum:i545296ADB9DD13B9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29450 mRNA. Translation: AAA69902.1.
PIRiS52984.
RefSeqiXP_008383785.1. XM_008385563.1.

Genome annotation databases

GeneIDi103446446.
KEGGimdm:103446446.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29450 mRNA. Translation: AAA69902.1.
PIRiS52984.
RefSeqiXP_008383785.1. XM_008385563.1.

3D structure databases

ProteinModelPortaliP43309.
SMRiP43309. Positions 91-426.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi103446446.
KEGGimdm:103446446.

Enzyme and pathway databases

SABIO-RKP43309.

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]
ProtoNetiSearch...

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: February 4, 2015
This is version 81 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.