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C7FF05 (PPO4_AGABI) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 18. 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 4

Short name=PPO4
Short name=Phenolase 4
EC=1.14.18.1
Alternative name(s):
Cresolase
Tyrosinase 4
Gene names
Name:PPO4
OrganismAgaricus bisporus (White button mushroom)
Taxonomic identifier5341 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesAgaricaceaeAgaricus

Protein attributes

Sequence length611 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

Subunit structure

Heterotetramer By similarity.

Post-translational modification

The C-ter is probably cleaved after Gly-379 since the mature active protein is smaller than the protein encoded by the gene By similarity.

Sequence similarities

Belongs to the tyrosinase family.

Ontologies

Keywords
   Biological processMelanin biosynthesis
   LigandCopper
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   PTMThioether bond
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 – 379379Polyphenol oxidase 4
PRO_0000416866
Propeptide380 – 611232Removed in mature form Probable
PRO_0000416867

Sites

Metal binding571Copper 1; via tele nitrogen By similarity
Metal binding821Copper 1; via tele nitrogen By similarity
Metal binding911Copper 1; via tele nitrogen By similarity
Metal binding2511Copper 2; via tele nitrogen By similarity
Metal binding2551Copper 2; via tele nitrogen By similarity
Metal binding2831Copper 2; via tele nitrogen By similarity
Binding site2551Substrate By similarity
Site379 – 3802Cleavage Probable

Amino acid modifications

Cross-link80 ↔ 822'-(S-cysteinyl)-histidine (Cys-His) By similarity

Sequences

Sequence LengthMass (Da)Tools
C7FF05 [UniParc].

Last modified September 22, 2009. Version 1.
Checksum: D9667D24204E614B

FASTA61168,318
        10         20         30         40         50         60 
MSLLATVGPT GGVKNRLDIV DFVRDEKFFT LYVRALQAIQ DKDQADYSSF FQLSGIHGLP 

        70         80         90        100        110        120 
FTPWAKPKDT PTVPYESGYC THSQVLFPTW HRVYVSIYEQ VLQEAAKGIA KKFTVHKKEW 

       130        140        150        160        170        180 
VQAAEDLRQP YWDTGFALVP PDEIIKLEQV KITNYDGTKI TVRNPILRYS FHPIDPSFSG 

       190        200        210        220        230        240 
YPNFDTWRTT VRNPDADKKE NIPALIAKLD LEADSTREKT YNMLKFNANW EAFSNHGEFD 

       250        260        270        280        290        300 
DTHANSLEAV HDDIHGFVGR GAIRGHMTHA LFAAFDPIFW LHHSNVDRHL SLWQALYPGV 

       310        320        330        340        350        360 
WVTQGPEREG SMGFAPGTEL NKDSALEPFY ETEDKPWTSV PLTDTALLNY SYPDFDKVKG 

       370        380        390        400        410        420 
GTPDLVRDYI NDHIDRRYGI KKSEGGKNPA LDLLSDFKGV THDHNEDLKM FDWTIQASWK 

       430        440        450        460        470        480 
KFELDDSFAI IFYFAADGST NVTKENYIGS INIFRGTTPT NCANCRTQDN LVQEGFVHLD 

       490        500        510        520        530        540 
RFIARDLDTF DPQAVHRYLK EKKLSYKVVA DDHSVTLKSL RIRVQGRPLH LPPGVSFPRL 

       550        560        570        580        590        600 
DKNIPIVNFD DVLDLVTGVV NIGLTAVGAT AGVAIGVVGA TAGTAIGVAG AATDAVTNIA 

       610 
KGGLGALGRI F 

« 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
GQ354802 mRNA. Translation: ACU29458.1.
GU936493 Genomic DNA. Translation: ADE67052.1.

3D structure databases

ProteinModelPortalC7FF05.
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.
PROSITEPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePPO4_AGABI
AccessionPrimary (citable) accession number: C7FF05
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2012
Last sequence update: September 22, 2009
Last modified: October 16, 2013
This is version 18 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