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Q00024 (PPO1_AGABI) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 66. 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 1

Short name=PPO1
Short name=Phenolase 1
EC=1.14.18.1
Alternative name(s):
Cresolase 1
Tyrosinase 1
Gene names
Name:PPO1
OrganismAgaricus bisporus (White button mushroom)
Taxonomic identifier5341 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesAgaricaceaeAgaricus

Protein attributes

Sequence length568 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-382 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 – 568568Polyphenol oxidase 1
PRO_0000186740
Propeptide383 – 565183Removed in mature form Probable
PRO_0000416862

Sites

Metal binding571Copper 1; via tele nitrogen By similarity
Metal binding851Copper 1; via tele nitrogen By similarity
Metal binding941Copper 1; via tele nitrogen By similarity
Metal binding2571Copper 2; via tele nitrogen By similarity
Metal binding2611Copper 2; via tele nitrogen By similarity
Metal binding2861Copper 2; via tele nitrogen By similarity
Binding site2611Substrate By similarity
Site382 – 3832Cleavage Probable

Amino acid modifications

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

Sequences

Sequence LengthMass (Da)Tools
Q00024 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: F5CBADB73533685A

FASTA56863,898
        10         20         30         40         50         60 
MSHLLVSPLG GGVQPRLEIN NFVKNDRQFS LYVQALDRMY ATPQNETASY FQVAGVHGYP 

        70         80         90        100        110        120 
LIPFDDAVGP TEFSPFDQWT GYCTHGSTLF PTWHRPYVLI LEQILSGHAQ QIADTYTVNK 

       130        140        150        160        170        180 
SEWKKAATEF RHPYWDWASN SVPPPEVISL PKVTITTPNG QKTSVANPLM RYTFNSVNDG 

       190        200        210        220        230        240 
GFYGPYNQWD TTLRQPDSTG VNAKDNVNRL KSVLKNAQAS LTRATYDMFN RVTTWPHFSS 

       250        260        270        280        290        300 
HTPASGGSTS NSIEAIHDNI HVLVGGNGHM SDPSVAPFDP IFFLHHANVD RLIALWSAIR 

       310        320        330        340        350        360 
YDVWTSPGDA QFGTYTLRYK QSVDESTDLA PWWKTQNEYW KSNELRSTES LGYTYPEFVG 

       370        380        390        400        410        420 
LDMYNKDAVN KTISRKVAQL YGPQRGGQRS LVEDLSNSHA RRSQRPAKRS RLGQLLKGLF 

       430        440        450        460        470        480 
SDWSAQIKFN RHEVGQSFSV CLFLGNVPED PREWLVSPNL VGARHAFVRS VKTDHVAEEI 

       490        500        510        520        530        540 
GFIPINQWIA EHTGLPSFAV DLVKPLLAQG LQWRVLLADG TPAELDSLEV TILEVPSELT 

       550        560 
DDEPNPRSRP PRYHKDITHG KRGGCREA 

« Hide

References

[1]"Cloning, expression and characterisation of two tyrosinase cDNAs from Agaricus bisporus."
Wichers H., Recourt K., Hendriks M., Ebbelaar C.E.M., Biancone G., Hoeberichts F., Mooibroek H., Soler-Rivas C.
Appl. Microbiol. Biotechnol. 61:336-341(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Horst U1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X85113 mRNA. Translation: CAA59432.1.
PIRS53017.

3D structure databases

ProteinModelPortalQ00024.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKQ00024.

Family and domain databases

Gene3D1.10.1280.10. 1 hit.
InterProIPR016216. Monophenol_mOase_fun.
IPR002227. Tyrosinase.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamPF00264. Tyrosinase. 1 hit.
[Graphical view]
PIRSFPIRSF000340. MPO_fungal. 1 hit.
PRINTSPR00092. TYROSINASE.
SUPFAMSSF48056. SSF48056. 1 hit.
PROSITEPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePPO1_AGABI
AccessionPrimary (citable) accession number: Q00024
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: October 16, 2013
This is version 66 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