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P43309 (PPO_MALDO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polyphenol oxidase, chloroplastic

Short name=PPO
EC=1.10.3.1
Alternative name(s):
Catechol oxidase
OrganismMalus domestica (Apple) (Pyrus malus)
Taxonomic identifier3750 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeMaloideaeMaleaeMalus

Protein attributes

Sequence length593 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 2 copper ions per subunit By similarity.

Subcellular location

Plastidchloroplast thylakoid lumen.

Sequence similarities

Belongs to the tyrosinase family.

Ontologies

Keywords
   Cellular componentChloroplast
Plastid
Thylakoid
   DomainTransit peptide
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMDisulfide bond
Thioether bond
Gene Ontology (GO)
   Biological_processpigment biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentchloroplast thylakoid lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncatechol oxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 8989Chloroplast Potential
Chain90 – 593504Polyphenol oxidase, chloroplastic
PRO_0000035916

Sites

Metal binding1751Copper A By similarity
Metal binding1961Copper A By similarity
Metal binding2051Copper A By similarity
Metal binding3271Copper B By similarity
Metal binding3311Copper B By similarity
Metal binding3611Copper B By similarity

Amino acid modifications

Disulfide bond100 ↔ 115 By similarity
Disulfide bond114 ↔ 176 By similarity
Cross-link179 ↔ 1962'-(S-cysteinyl)-histidine (Cys-His) By similarity

Sequences

Sequence LengthMass (Da)Tools
P43309 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 545296ADB9DD13B9

FASTA59365,721
        10         20         30         40         50         60 
MTSLSPPVVT TPTVPNPATK PLSPFSQNNS QVSLLTKPKR SFARKVSCKA TNNDQNDQAQ 

        70         80         90        100        110        120 
SKLDRRNVLL GLGGLYGVAG MGTDPFAFAK PIAPPDVSKC GPADLPQGAV PTNCCPPPST 

       130        140        150        160        170        180 
KIIDFKLPAP AKLRIRPPAH AVDQAYRDKY YKAMELMKAL PDDDPRSFKQ QAAVHCAYCD 

       190        200        210        220        230        240 
GAYDQVGFPE LELQIHNSWL FFPFHRYYLY FFEKILGKLI NDPTFALPFW NWDSPAGMPL 

       250        260        270        280        290        300 
PAIYADPKSP LYDKLRSANH QPPTLVDLDY NGTEDNVSKE TTINANLKIM YRQMVSNSKN 

       310        320        330        340        350        360 
AKLFFGNPYR AGDEPDPGGG SIEGTPHAPV HLWTGDNTQP NFEDMGNFYS AGRDPIFFAH 

       370        380        390        400        410        420 
HSNVDRMWSI WKTLGGKRTD LTDSDWLDSG FLFYNENAEL VRVKVRDCLE TKNLGYVYQD 

       430        440        450        460        470        480 
VDIPWLSSKP TPRRAKVALS KVAKKLGVAH AAVASSSKVV AGTEFPISLG SKISTVVKRP 

       490        500        510        520        530        540 
KQKKRSKKAK EDEEEILVIE GIEFDRDVAV KFDVYVNDVD DLPSGPDKTE FAGSFVSVPH 

       550        560        570        580        590 
SHKHKKKMNT ILRLGLTDLL EEIEAEDDDS VVVTLVPKFG AVKIGGIKIE FAS 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L29450 mRNA. Translation: AAA69902.1.
PIRS52984.

3D structure databases

ProteinModelPortalP43309.
SMRP43309. Positions 91-426.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP43309.

Family and domain databases

Gene3D1.10.1280.10. 1 hit.
InterProIPR016213. Polyphenol_oxidase.
IPR022740. Polyphenol_oxidase_C.
IPR022739. Polyphenol_oxidase_cen.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamPF12142. PPO1_DWL. 1 hit.
PF12143. PPO1_KFDV. 1 hit.
PF00264. Tyrosinase. 1 hit.
[Graphical view]
PIRSFPIRSF000290. PPO_plant. 1 hit.
PRINTSPR00092. TYROSINASE.
SUPFAMSSF48056. SSF48056. 1 hit.
PROSITEPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePPO_MALDO
AccessionPrimary (citable) accession number: P43309
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families