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Protein

Polyphenol oxidase 1

Gene

PPO1

Organism
Agaricus bisporus (White button mushroom)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

Cu2+By similarityNote: Binds 2 copper ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi57 – 571Copper 1; via tele nitrogenBy similarity
Metal bindingi85 – 851Copper 1; via tele nitrogenBy similarity
Metal bindingi94 – 941Copper 1; via tele nitrogenBy similarity
Metal bindingi257 – 2571Copper 2; via tele nitrogenBy similarity
Metal bindingi261 – 2611Copper 2; via tele nitrogenBy similarity
Binding sitei261 – 2611SubstrateBy similarity
Metal bindingi286 – 2861Copper 2; via tele nitrogenBy similarity
Sitei382 – 3832CleavageCurated

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. monophenol monooxygenase activity Source: UniProtKB-EC

GO - Biological processi

  1. melanin biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Melanin biosynthesis

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

SABIO-RKQ00024.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyphenol oxidase 1 (EC:1.14.18.1)
Short name:
PPO1
Short name:
Phenolase 1
Alternative name(s):
Cresolase 1
Tyrosinase 1
Gene namesi
Name:PPO1
OrganismiAgaricus bisporus (White button mushroom)
Taxonomic identifieri5341 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesAgaricaceaeAgaricus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 568568Polyphenol oxidase 1PRO_0000186740Add
BLAST
Propeptidei383 – 565183Removed in mature formCuratedPRO_0000416862Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki83 ↔ 852'-(S-cysteinyl)-histidine (Cys-His)By similarity

Post-translational modificationi

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

Keywords - PTMi

Thioether bond

Interactioni

Subunit structurei

Heterotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ00024.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.Curated

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
InterProiIPR016216. Monophenol_mOase_fun.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamiPF00264. Tyrosinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000340. MPO_fungal. 1 hit.
PRINTSiPR00092. TYROSINASE.
SUPFAMiSSF48056. SSF48056. 1 hit.
PROSITEiPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q00024-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHLLVSPLG GGVQPRLEIN NFVKNDRQFS LYVQALDRMY ATPQNETASY
60 70 80 90 100
FQVAGVHGYP LIPFDDAVGP TEFSPFDQWT GYCTHGSTLF PTWHRPYVLI
110 120 130 140 150
LEQILSGHAQ QIADTYTVNK SEWKKAATEF RHPYWDWASN SVPPPEVISL
160 170 180 190 200
PKVTITTPNG QKTSVANPLM RYTFNSVNDG GFYGPYNQWD TTLRQPDSTG
210 220 230 240 250
VNAKDNVNRL KSVLKNAQAS LTRATYDMFN RVTTWPHFSS HTPASGGSTS
260 270 280 290 300
NSIEAIHDNI HVLVGGNGHM SDPSVAPFDP IFFLHHANVD RLIALWSAIR
310 320 330 340 350
YDVWTSPGDA QFGTYTLRYK QSVDESTDLA PWWKTQNEYW KSNELRSTES
360 370 380 390 400
LGYTYPEFVG LDMYNKDAVN KTISRKVAQL YGPQRGGQRS LVEDLSNSHA
410 420 430 440 450
RRSQRPAKRS RLGQLLKGLF SDWSAQIKFN RHEVGQSFSV CLFLGNVPED
460 470 480 490 500
PREWLVSPNL VGARHAFVRS VKTDHVAEEI GFIPINQWIA EHTGLPSFAV
510 520 530 540 550
DLVKPLLAQG LQWRVLLADG TPAELDSLEV TILEVPSELT DDEPNPRSRP
560
PRYHKDITHG KRGGCREA
Length:568
Mass (Da):63,898
Last modified:October 31, 1996 - v1
Checksum:iF5CBADB73533685A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85113 mRNA. Translation: CAA59432.1.
PIRiS53017.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85113 mRNA. Translation: CAA59432.1.
PIRiS53017.

3D structure databases

ProteinModelPortaliQ00024.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKQ00024.

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
InterProiIPR016216. Monophenol_mOase_fun.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamiPF00264. Tyrosinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000340. MPO_fungal. 1 hit.
PRINTSiPR00092. TYROSINASE.
SUPFAMiSSF48056. SSF48056. 1 hit.
PROSITEiPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Horst U1.

Entry informationi

Entry nameiPPO1_AGABI
AccessioniPrimary (citable) accession number: Q00024
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2000
Last sequence update: October 31, 1996
Last modified: November 25, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.