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C7FF04 (PPO3_AGABI) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 19. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 3

Short name=PPO3
Short name=Phenolase 3
EC=1.14.18.1
Alternative name(s):
Cresolase
Tyrosinase 3
Gene names
Name:PPO3
OrganismAgaricus bisporus (White button mushroom)
Taxonomic identifier5341 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesAgaricaceaeAgaricus

Protein attributes

Sequence length576 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Copper-containing oxidase that catalyzes both the o-hydroxylation of monophenols and the subsequent oxidation of the resulting o-diphenols into reactive o-quinones, which evolve spontaneously to produce intermediates, which associate in dark brown pigments. Involved in the initial step of melanin synthesis. Melanins constitute a mechanism of defense and resistance to stress such as UV radiations, free radicals, gamma rays, dehydratation and extreme temperatures, and contribute to the fungal cell-wall resistance against hydrolytic enzymes in avoiding cellular lysis. Fungal pigments are also involved in the formation and stability of spores By similarity.

Catalytic activity

2 L-dopa + O2 = 2 dopaquinone + 2 H2O.

L-tyrosine + O2 = dopaquinone + H2O.

Cofactor

Binds 2 copper ions per subunit. Ref.3

Subunit structure

Tetramer composed of two subunits of PPO3 (H subunits) and two subunits of the as yet uncharacterized product of ORF239342 (L subunits).

Post-translational modification

The C-ter is probably cleaved after Gly-392 since the mature active protein is smaller than the protein encoded by the gene.

Sequence similarities

Belongs to the tyrosinase family.

Ontologies

Keywords
   Biological processMelanin biosynthesis
   LigandCopper
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   PTMThioether bond
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processmelanin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

monophenol monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 392392Polyphenol oxidase 3
PRO_0000416864
Propeptide393 – 576184Removed in mature form Probable
PRO_0000416865

Sites

Metal binding611Copper 1; via tele nitrogen
Metal binding851Copper 1; via tele nitrogen
Metal binding941Copper 1; via tele nitrogen
Metal binding2591Copper 2; via tele nitrogen
Metal binding2631Copper 2; via tele nitrogen
Metal binding2961Copper 2; via tele nitrogen
Binding site2631Substrate
Site392 – 3932Cleavage Probable

Amino acid modifications

Cross-link83 ↔ 852'-(S-cysteinyl)-histidine (Cys-His)

Experimental info

Sequence conflict1061W → C in ADE67053. Ref.2

Secondary structure

................................................................. 576
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
C7FF04 [UniParc].

Last modified September 22, 2009. Version 1.
Checksum: A4ED6B3B762DCB26

FASTA57666,267
        10         20         30         40         50         60 
MSDKKSLMPL VGIPGEIKNR LNILDFVKND KFFTLYVRAL QVLQARDQSD YSSFFQLGGI 

        70         80         90        100        110        120 
HGLPYTEWAK AQPQLHLYKA NYCTHGTVLF PTWHRAYEST WEQTLWEAAG TVAQRFTTSD 

       130        140        150        160        170        180 
QAEWIQAAKD LRQPFWDWGY WPNDPDFIGL PDQVIRDKQV EITDYNGTKI EVENPILHYK 

       190        200        210        220        230        240 
FHPIEPTFEG DFAQWQTTMR YPDVQKQENI EGMIAGIKAA APGFREWTFN MLTKNYTWEL 

       250        260        270        280        290        300 
FSNHGAVVGA HANSLEMVHN TVHFLIGRDP TLDPLVPGHM GSVPHAAFDP IFWMHHCNVD 

       310        320        330        340        350        360 
RLLALWQTMN YDVYVSEGMN REATMGLIPG QVLTEDSPLE PFYTKNQDPW QSDDLEDWET 

       370        380        390        400        410        420 
LGFSYPDFDP VKGKSKEEKS VYINDWVHKH YGFVTTQTEN PALRLLSSFQ RAKSDHETQY 

       430        440        450        460        470        480 
ALYDWVIHAT FRYYELNNSF SIIFYFDEGE GCTLESIIGT VDAFRGTTSE NCANCARSQD 

       490        500        510        520        530        540 
LIAEGFVHLN YYIGCDIGQH ADHEDDAVPL YEPTRVKEYL KKRKIGCKVV SAEGELTSLV 

       550        560        570 
VEIKGAPYYL PVGEARPKLD HEKPIVILDD IIHRVN 

« Hide

References

[1]"Cloning, characterization and expression of two new polyphenol oxidase cDNAs from Agaricus bisporus."
Wu J., Chen H., Gao J., Liu X., Cheng W., Ma X.
Biotechnol. Lett. 32:1439-1447(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular cloning and characterization of two polyphenoloxidase genes from the mushrooms Agaricus bisporus."
Li N.Y., Cai W.M., Liu C.Y., Ran F.L.
Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: As2796.
[3]"Crystal structure of Agaricus bisporus mushroom tyrosinase: identity of the tetramer subunits and interaction with tropolone."
Ismaya W.T., Rozeboom H.J., Weijn A., Mes J.J., Fusetti F., Wichers H.J., Dijkstra B.W.
Biochemistry 50:5477-5486(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-392 IN COMPLEX WITH SUBSTRATE, COFACTOR, THIOESTER BOND.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
GQ354801 mRNA. Translation: ACU29457.1.
GU936494 Genomic DNA. Translation: ADE67053.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y9WX-ray2.30A/B2-392[»]
2Y9XX-ray2.78A/B/C/D2-392[»]
ProteinModelPortalC7FF04.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.1280.10. 1 hit.
InterProIPR002227. Tyrosinase.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamPF00264. Tyrosinase. 1 hit.
[Graphical view]
PRINTSPR00092. TYROSINASE.
SUPFAMSSF48056. SSF48056. 1 hit.
PROSITEPS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceC7FF04.

Entry information

Entry namePPO3_AGABI
AccessionPrimary (citable) accession number: C7FF04
Secondary accession number(s): D5LK97
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2012
Last sequence update: September 22, 2009
Last modified: October 16, 2013
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references