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Q06355 (PPOB_SOLTU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 73. 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:
Catechol oxidase B, chloroplastic

EC=1.10.3.1
Alternative name(s):
Polyphenol oxidase
Short name=PPO
OrganismSolanum tuberosum (Potato) [Reference proteome]
Taxonomic identifier4113 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum

Protein attributes

Sequence length588 AA.
Sequence statusFragment.
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
   Technical termComplete proteome
Reference proteome
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 peptide‹1 – 88›88Chloroplast Potential
Chain89 – 588500Catechol oxidase B, chloroplastic
PRO_0000035917

Sites

Metal binding1801Copper A By similarity
Metal binding1981Copper A By similarity
Metal binding2071Copper A By similarity
Metal binding3291Copper B By similarity
Metal binding3331Copper B By similarity
Metal binding3641Copper B By similarity

Amino acid modifications

Disulfide bond99 ↔ 115 By similarity
Disulfide bond114 ↔ 181 By similarity
Cross-link184 ↔ 1982'-(S-cysteinyl)-histidine (Cys-His) By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
Q06355 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: A7E25383273428CC

FASTA58866,241
        10         20         30         40         50         60 
SSSSTTTIPL CTNKSLSSSF TTNNSSFLSK PSQLFLHGRR NQSFKVSCNA NNNVGEHDKN 

        70         80         90        100        110        120 
LDTVDRRNVL LGLGGLYGAA NLAPLASASP IPPPDLKSCG VAHVTEGVDV TYSCCPPVPD 

       130        140        150        160        170        180 
DIDSVPYYKF PPMTKLRIRP PAHAADEEYV AKYQLATSRM RELDKDSFDP LGFKQQANIH 

       190        200        210        220        230        240 
CAYCNGAYKV GGKELQVHFS WLFFPFHRWY LYFYERILGS LINDPTFALP YWNWDHPKGM 

       250        260        270        280        290        300 
RIPPMFDREG SSLYDDKRNQ NHRNGTIIDL GHFGQEVDTP QLQIMTNNLT LMYRQMVTNA 

       310        320        330        340        350        360 
PCPSQFFGAA YPLGTEPSPG MGTIENIPHT PVHIWTGDSP RQKNGENMGN FYSAGLDPIF 

       370        380        390        400        410        420 
YCHHANVDRM WDEWKLIGGK RRDLSNKDWL NSEFFFYDEN RNPYRVKVRD CLDSKKMGFS 

       430        440        450        460        470        480 
YAPMPTPWRN FKPIRKTTAG KVNTASIAPV TKVFPLAKLD RAISFSITRP ASSRTTQEKN 

       490        500        510        520        530        540 
EQEEILTFNK VAYDDTKYVR FDVFLNVDKT VNADELDKAE FAGSYTSLPH VHGNNTNHVT 

       550        560        570        580 
SVTFKLAITE LLEDNGLEDE DTIAVTLVPK VGGEGVSIES VEIKLEDC 

« Hide

References

[1]"cDNA cloning and expression of potato polyphenol oxidase."
Hunt M.D., Eannetta N.T., Yu H., Newman S.M., Steffens J.C.
Plant Mol. Biol. 21:59-68(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Katahdin.
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M95197 mRNA. Translation: AAA02879.1.
PIRS30929.
UniGeneStu.266.

3D structure databases

ProteinModelPortalQ06355.
SMRQ06355. Positions 89-429.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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 namePPOB_SOLTU
AccessionPrimary (citable) accession number: Q06355
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 11, 2014
This is version 73 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