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Q06215 (PPO_VICFA) 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:
Polyphenol oxidase A1, chloroplastic

Short name=PPO
EC=1.10.3.1
Alternative name(s):
Catechol oxidase
OrganismVicia faba (Broad bean) (Faba vulgaris)
Taxonomic identifier3906 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaeVicia

Protein attributes

Sequence length606 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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 termDirect protein sequencing
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 – 9292Chloroplast Ref.2
Chain93 – 606514Polyphenol oxidase A1, chloroplastic
PRO_0000035919

Sites

Metal binding1811Copper A By similarity
Metal binding2021Copper A By similarity
Metal binding2111Copper A By similarity
Metal binding3331Copper B By similarity
Metal binding3371Copper B By similarity
Metal binding3671Copper B By similarity

Amino acid modifications

Disulfide bond103 ↔ 121 By similarity
Disulfide bond120 ↔ 182 By similarity
Cross-link185 ↔ 2022'-(S-cysteinyl)-histidine (Cys-His) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q06215 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: FC539F9F041B503C

FASTA60668,541
        10         20         30         40         50         60 
MTSISALSFI STINVSSNSK ISHSSVYPFL QKQHQSSKLR KPKRQVTCSS NNNQNNPKEE 

        70         80         90        100        110        120 
QELSNIVGHR RNVLIGLGGI YGTLATNPSA LASPISPPDL SKCVPPSDLP SGTTPPNINC 

       130        140        150        160        170        180 
CPPYSTKITD FKFPSNQPLR VRQAAHLVDN EFLEKYKKAT ELMKALPSND PRNFTQQANI 

       190        200        210        220        230        240 
HCAYCDGAYS QIGFPDLKLQ VHGSWLFFPF HRWYLYFYER ILGSLINDPT FALPFWNYDA 

       250        260        270        280        290        300 
PDGMQLPTIY ADKASPLYDE LRNASHQPPT LIDLNFCDIG SDIDRNELIK TNLSIMYRQV 

       310        320        330        340        350        360 
YSNGKTSRLF LGNPYRAGDA EPQGAGSIEN VPHAPVHTWT GDNTQTNIED MGIFYSAARD 

       370        380        390        400        410        420 
PIFYSHHSNV DRLWYIWKTL GGKKHDFTDK DWLESGFLFY DENKNLVRVN VKDSLDIDKL 

       430        440        450        460        470        480 
GYAYQDVPIP WEKAKPVPRR TKVQKLVEVE VNDGNLRKSP TIFLVRQQSP RKYVTFPLVL 

       490        500        510        520        530        540 
NNKVSAIVKR PKKLRSKKEK EEEEEVLVIE GIEFYMNIAI KFDVYINDED DKVGAGNTEF 

       550        560        570        580        590        600 
AGSFVNIPHS AHGHKNKKII TSLRLGITDL LEDLHVEGDD NIVVTLVPKC GSGQVKINNV 


EIVFED 

« Hide

References

[1]"Cloning and characterization of cDNAs coding for Vicia faba polyphenol oxidase."
Cary J.W., Lax A.R., Flurkey W.H.
Plant Mol. Biol. 20:245-253(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Leaf.
[2]"Polypeptide composition and amino-terminal sequence of broad bean polyphenol oxidase."
Flurkey W.H.
Plant Physiol. 91:481-483(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 93-119.
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z11702 mRNA. Translation: CAA77764.1.
PIRS24758.

3D structure databases

ProteinModelPortalQ06215.
SMRQ06215. Positions 93-431.
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 namePPO_VICFA
AccessionPrimary (citable) accession number: Q06215
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