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Q08296 (PPOF_SOLLC) Reviewed, UniProtKB/Swiss-Prot

Last modified July 27, 2011. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Polyphenol oxidase F, chloroplastic
Short name=PPO
EC=1.10.3.1
Alternative name(s):
Catechol oxidase
OrganismSolanum lycopersicum (Tomato) (Lycopersicon esculentum)
Taxonomic identifier4081 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum › Lycopersicon

Protein attributes

Sequence length585 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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

Plastid › chloroplast 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)
   Cellular componentchloroplast thylakoid lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncatechol oxidase activity

Inferred from electronic annotation. Source: 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 – 8686Chloroplast By similarity
Chain87 – 585499Polyphenol oxidase F, chloroplastic
PRO_0000035915

Sites

Metal binding1791Copper A By similarity
Metal binding1971Copper A By similarity
Metal binding2061Copper A By similarity
Metal binding3261Copper B By similarity
Metal binding3301Copper B By similarity
Metal binding3611Copper B By similarity

Amino acid modifications

Disulfide bond97 ↔ 114 By similarity
Disulfide bond113 ↔ 180 By similarity
Cross-link183 ↔ 1972'-(S-cysteinyl)-histidine (Cys-His) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q08296 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 6C8C7C1D2F00DD5D

FASTA58566,183
        10         20         30         40         50         60 
MSSSTPNTLP LLSTNKSLSS PFTNNHSTFL SKPSQPFLHG RRCQSFKVSC NVGEHDKNLD 

        70         80         90        100        110        120 
AVDRRNVLLG LGGFYGAANL APLASAAPIP PPDLKSCGVA HIDDKGTEVS YSCCPPVPDD 

       130        140        150        160        170        180 
IDSVPYYKFP PMTKLRIRPP AHAADEEYVA KYQLATSRMR ELDKDPFDPL GFKQQANIHC 

       190        200        210        220        230        240 
AYCNGAYKIG GKELQVHFSW LFFPFHRWYL YFYERILGSL INDPTFALPY WNWDHPKGMR 

       250        260        270        280        290        300 
IPPMFDREGS SLYDEKRNQN HRNGTIIDLG HFGKDVRTPQ LQIMTNNLTL MYRQMVTNAP 

       310        320        330        340        350        360 
CPSQFFGAPL GSDPEPGMGT IENIPHTPVH IWTGDSPRQG HGEDMGNFYS AGLDPLFYCH 

       370        380        390        400        410        420 
HANVDRMWNE WKLIGGKRRD LSNKDWLNSE FFFYDENRNP YRVKVRDCLD SKKMGFDYPP 

       430        440        450        460        470        480 
MPTPWRNFKP IRRSSSGKVN TASIAPVSKV FPLAKLDRAI SFSLTRPASS RTTQEKNEQQ 

       490        500        510        520        530        540 
EILTFNKMAY DDTKYVRFDV FLNVDKTVNA EELDKAEFAG SYTSLPHVHG NNDNHVKDVT 

       550        560        570        580 
FTLAITELLE DIGLEDEDTI AVTLVPKVGG EGVSIESVEI KLEDC

« Hide

References

[1]"Organisation of the tomato polyphenol oxidase gene family."
Newman S.M., Eannetta N.T., Yu H., Prince J.P., de Vicente M.C., Tanksley S.D., Steffens J.C.
Plant Mol. Biol. 21:1035-1051(1993) [PubMed: 8098228] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. VFNT Cherry.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z12838 Genomic DNA. Translation: CAA78300.1.
PIRS33544.

3D structure databases

ProteinModelPortalQ08296.
SMRQ08296. Positions 87-426.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR016213. Polyphenol_oxidase.
IPR022740. Polyphenol_oxidase_C.
IPR022739. Polyphenol_oxidase_cen.
IPR002227. Tyrosinase.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
Gene3DG3DSA:1.10.1280.10. Di-copper_centre. 1 hit.
PfamPF12142. PPO1_DWL. 1 hit.
PF12143. PPO1_KFDV. 1 hit.
PF00264. Tyrosinase. 1 hit.
[Graphical view]
PIRSFPIRSF000290. PPO_plant. 1 hit.
PRINTSPR00092. TYROSINASE.
SUPFAMSSF48056. Di-copper_centre. 1 hit.
PROSITEPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePPOF_SOLLC
AccessionPrimary (citable) accession number: Q08296
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 27, 2011
This is version 66 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

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