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O42713 (PPO2_AGABI) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 61. 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 2

Short name=PPO2
Short name=Phenolase 2
EC=1.14.18.1
Alternative name(s):
Cresolase 2
Tyrosinase 2
Gene names
Name:PPO2
OrganismAgaricus bisporus (White button mushroom)
Taxonomic identifier5341 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesAgaricaceaeAgaricus

Protein attributes

Sequence length556 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.

Developmental stage

Expressed during the fruiting body stage. Ref.3

Post-translational modification

The C-ter is probably cleaved after Gly-378 since the mature active protein is smaller than the protein encoded by the gene By similarity.

Sequence similarities

Belongs to the tyrosinase family.

Sequence caution

The sequence CAA61562.1 differs from that shown. Reason: Frameshift at position 445.

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 – 378378Polyphenol oxidase 2
PRO_0000186731
Propeptide379 – 556178Removed in mature form Probable
PRO_0000416863

Sites

Metal binding571Copper 1; via tele nitrogen By similarity
Metal binding811Copper 1; via tele nitrogen By similarity
Metal binding901Copper 1; via tele nitrogen By similarity
Metal binding2501Copper 2; via tele nitrogen By similarity
Metal binding2541Copper 2; via tele nitrogen By similarity
Metal binding2821Copper 2; via tele nitrogen By similarity
Binding site2541Substrate By similarity
Site378 – 3792Cleavage Probable

Amino acid modifications

Cross-link79 ↔ 812'-(S-cysteinyl)-histidine (Cys-His) By similarity

Sequences

Sequence LengthMass (Da)Tools
O42713 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: DE10827A209895DA

FASTA55663,927
        10         20         30         40         50         60 
MSLIATVGPT GGVKNRLNIV DFVKNEKFFT LYVRSLELLQ AKEQHDYSSF FQLAGIHGLP 

        70         80         90        100        110        120 
FTEWAKERPS MNLYKAGYCT HGQVLFPTWH RTYLSVLEQI LQGAAIEVAK KFTSNQTDWV 

       130        140        150        160        170        180 
QAAQDLRQPY WDWGFELMPP DEVIKNEEVN ITNYDGKKIS VKNPILRYHF HPIDPSFKPY 

       190        200        210        220        230        240 
GDFATWRTTV RNPDRNRRED IPGLIKKMRL EEGQIREKTY NMLKFNDAWE RFSNHGISDD 

       250        260        270        280        290        300 
QHANSLESVH DDIHVMVGYG KIEGHMDHPF FAAFDPIFWL HHTNVDRLLS LWKAINPDVW 

       310        320        330        340        350        360 
VTSGRNRDGT MGIAPNAQIN SETPLEPFYQ SGDKVWTSAS LADTARLGYS YPDFDKLVGG 

       370        380        390        400        410        420 
TKELIRDAID DLIDERYGSK PSSGARNTAF DLLADFKGIT KEHKEDLKMY DWTIHVAFKK 

       430        440        450        460        470        480 
FELKESFSLL FYFASDGGDY DQENCFVGSI NAFRGTAPET CANCQDNENL IQEGFIHLNH 

       490        500        510        520        530        540 
YLARDLESFE PQDVHKFLKE KGLSYKLYSR GDKPLTSLSV KIEGRPLHLP PGEHRPKYDH 

       550 
TQARVVFDDV AVHVIN 

« 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.
[2]"Characterization of a fruiting body-expressed gene encoding a putative polyphenol oxidase of Agaricus bisporus."
Ebbelar C.E.M., Wichers H.J., Van Den Bosch T., Oyevaar J.I., Recourt K.
Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 122-556.
Strain: Horst U1.
[3]"Expression of phenol oxidase and heat-shock genes during the development of Agaricus bisporus fruiting bodies, healthy and infected by Lecanicillium fungicola."
Largeteau M.L., Latapy C., Minvielle N., Regnault-Roger C., Savoie J.M.
Appl. Microbiol. Biotechnol. 85:1499-1507(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ223816 mRNA. Translation: CAA11562.1.
X89382 mRNA. Translation: CAA61562.1. Frameshift.

3D structure databases

ProteinModelPortalO42713.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBO42713.
ChEMBLCHEMBL3318.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKO42713.

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 namePPO2_AGABI
AccessionPrimary (citable) accession number: O42713
Secondary accession number(s): Q12543
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: December 11, 2013
This is version 61 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