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Reviewed, UniProtKB/Swiss-Prot Q08307 (PPOE_SOLLC)

Last modified November 4, 2008. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Polyphenol oxidase E, chloroplastic
      Short name=PPO
    EC=1.10.3.1
Alternative name(s):
    Catechol oxidase
OrganismSolanum lycopersicum (Tomato) (Lycopersicon esculentum)
Taxonomic identifier4081 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon

Protein attributes

Sequence length587 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 + O(2) = 2 1,2-benzoquinone + 2 H(2)O.

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
   DomainTransit peptide
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMThioether bond

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncatechol oxidase activity

Inferred from electronic annotation. Source: EC

copper 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 – 8787Chloroplast
Chain88 – 587500Polyphenol oxidase E, chloroplastic
PRO_0000035914

Sites

Metal binding1791Copper A By similarity
Metal binding1971Copper A By similarity
Metal binding2061Copper A By similarity
Metal binding3281Copper B By similarity
Metal binding3321Copper B By similarity
Metal binding3631Copper B By similarity

Amino acid modifications

Disulfide bond98 ↔ 114 By similarity
Disulfide bond113 ↔ 180 By similarity
Cross-link183 ↔ 1972'-(S-cysteinyl)-histidine (Cys-His) By similarity

Experimental info

Sequence conflict311 – 3155PLGSE → LWVLN in AAB22610. Ref.2
Sequence conflict4101C → V in AAB22610. Ref.2
Sequence conflict5411L → V in AAB22610. Ref.2
Sequence conflict5671V → I in AAB22610. Ref.2
Sequence conflict5741E → G in AAB22610. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q08307-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: A796AA1DD6454E3D

FASTA58766,237
        10         20         30         40         50         60 
MSSSSSITTT LPLCTNKSLS SSFTTTNSSL LSKPSQLFLH GRRNQSFKVS CNANNVDKNP 

        70         80         90        100        110        120 
DAVDRRNVLL GLGGLYGAAN LAPLATAAPI PPPDLKSCGT AHVKEGVDVI YSCCPPVPDD 

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

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

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

       310        320        330        340        350        360 
CPSQFFGAAY PLGSEPSPGQ GTIENIPHTP VHIWTGDKPR QKNGEDMGNF YSAGLDPIFY 

       370        380        390        400        410        420 
CHHANVDRMW NEWKLIGGKR RDLTDKDWLN SEFFFYDENR NPYRVKVRDC LDSKKMGFDY 

       430        440        450        460        470        480 
APMPTPWRNF KPIRKSSSGK VNTASIAPVS KVFPLAKLDR AISFSITRPA SSRTTQEKNE 

       490        500        510        520        530        540 
QEEILTFNKI SYDDRNYVRF DVFLNVDKTV NADELDKAEF AGSYTSLPHV HGSNTNHVTS 

       550        560        570        580 
LTFKLAITEL LEDIGLEDED TIAVTLVPKA GGEEVSIESV EIKLEDC 

« 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.
[2]"The tomato 66.3-kD polyphenoloxidase gene: molecular identification and developmental expression."
Shahar T., Hennig N., Gutfinger T., Hareven D., Lifschitz E.
Plant Cell 4:135-147(1992) [PubMed: 1633491] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Tiny tim.

Cross-references

Sequence databases

Z12837 Genomic DNA. Translation: CAA78299.1.
S40548 Genomic DNA. Translation: AAB22610.1.
PIRS33543.

3D structure databases

ModBaseSearch...

Family and domain databases

InterProIPR008922. Di-copper_centre.
IPR016213. Polyphenol_Oxase_pln.
IPR002227. Tyrosinase.
[Graphical view]
Gene3DG3DSA:1.10.1280.10. Di-copper_centre. 1 hit.
PfamPF00264. Tyrosinase. 1 hit.
[Graphical view]
PIRSFPIRSF000290. PPO_plant. 1 hit.
PRINTSPR00092. TYROSINASE.
PROSITEPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePPOE_SOLLC
AccessionPrimary (citable) accession number: Q08307
Secondary accession number(s): Q41175
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 4, 2008
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents