Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Polyphenol oxidase 3

Gene

PPO3

Organism
Agaricus bisporus (White button mushroom)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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+1 PublicationNote: Binds 2 copper ions per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi61 – 611Copper 1; via tele nitrogen
Metal bindingi85 – 851Copper 1; via tele nitrogen
Metal bindingi94 – 941Copper 1; via tele nitrogen
Metal bindingi259 – 2591Copper 2; via tele nitrogen
Metal bindingi263 – 2631Copper 2; via tele nitrogen
Binding sitei263 – 2631Substrate1 Publication
Metal bindingi296 – 2961Copper 2; via tele nitrogen
Sitei392 – 3932CleavageCurated

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

Names & Taxonomyi

Protein namesi
Recommended name:
Polyphenol oxidase 3 (EC:1.14.18.1)
Short name:
PPO3
Short name:
Phenolase 3
Alternative name(s):
Cresolase
Tyrosinase 3
Gene namesi
Name:PPO3
OrganismiAgaricus bisporus (White button mushroom)
Taxonomic identifieri5341 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesAgaricaceaeAgaricus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 392392Polyphenol oxidase 3PRO_0000416864Add
BLAST
Propeptidei393 – 576184Removed in mature formCuratedPRO_0000416865Add
BLAST

Amino acid modifications

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

Post-translational modificationi

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

Keywords - PTMi

Thioether bond

Interactioni

Subunit structurei

Tetramer composed of two subunits of PPO3 (H subunits) and two subunits of the as yet uncharacterized product of ORF239342 (L subunits).1 Publication

Structurei

Secondary structure

1
576
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83Combined sources
Helixi23 – 264Combined sources
Helixi30 – 4516Combined sources
Helixi54 – 596Combined sources
Beta strandi62 – 643Combined sources
Beta strandi69 – 724Combined sources
Helixi90 – 11324Combined sources
Helixi121 – 13010Combined sources
Helixi152 – 1554Combined sources
Beta strandi158 – 1636Combined sources
Beta strandi169 – 1735Combined sources
Turni175 – 1773Combined sources
Helixi191 – 1944Combined sources
Beta strandi200 – 2023Combined sources
Beta strandi206 – 2083Combined sources
Helixi210 – 23324Combined sources
Helixi238 – 2425Combined sources
Turni245 – 2495Combined sources
Helixi255 – 26713Combined sources
Helixi279 – 2813Combined sources
Turni283 – 2853Combined sources
Helixi286 – 2883Combined sources
Helixi291 – 30919Combined sources
Turni310 – 3123Combined sources
Beta strandi318 – 3203Combined sources
Beta strandi325 – 3273Combined sources
Beta strandi331 – 3333Combined sources
Beta strandi337 – 3437Combined sources
Beta strandi349 – 3513Combined sources
Helixi352 – 3554Combined sources
Helixi358 – 3614Combined sources
Beta strandi362 – 3643Combined sources
Helixi366 – 3716Combined sources
Helixi376 – 39116Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y9WX-ray2.30A/B2-392[»]
2Y9XX-ray2.78A/B/C/D2-392[»]
ProteinModelPortaliC7FF04.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiC7FF04.

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.Curated

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
InterProiIPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamiPF00264. Tyrosinase. 1 hit.
[Graphical view]
PRINTSiPR00092. TYROSINASE.
SUPFAMiSSF48056. SSF48056. 1 hit.
PROSITEiPS00498. TYROSINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

C7FF04-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDKKSLMPL VGIPGEIKNR LNILDFVKND KFFTLYVRAL QVLQARDQSD
60 70 80 90 100
YSSFFQLGGI HGLPYTEWAK AQPQLHLYKA NYCTHGTVLF PTWHRAYEST
110 120 130 140 150
WEQTLWEAAG TVAQRFTTSD QAEWIQAAKD LRQPFWDWGY WPNDPDFIGL
160 170 180 190 200
PDQVIRDKQV EITDYNGTKI EVENPILHYK FHPIEPTFEG DFAQWQTTMR
210 220 230 240 250
YPDVQKQENI EGMIAGIKAA APGFREWTFN MLTKNYTWEL FSNHGAVVGA
260 270 280 290 300
HANSLEMVHN TVHFLIGRDP TLDPLVPGHM GSVPHAAFDP IFWMHHCNVD
310 320 330 340 350
RLLALWQTMN YDVYVSEGMN REATMGLIPG QVLTEDSPLE PFYTKNQDPW
360 370 380 390 400
QSDDLEDWET LGFSYPDFDP VKGKSKEEKS VYINDWVHKH YGFVTTQTEN
410 420 430 440 450
PALRLLSSFQ RAKSDHETQY ALYDWVIHAT FRYYELNNSF SIIFYFDEGE
460 470 480 490 500
GCTLESIIGT VDAFRGTTSE NCANCARSQD LIAEGFVHLN YYIGCDIGQH
510 520 530 540 550
ADHEDDAVPL YEPTRVKEYL KKRKIGCKVV SAEGELTSLV VEIKGAPYYL
560 570
PVGEARPKLD HEKPIVILDD IIHRVN
Length:576
Mass (Da):66,267
Last modified:September 22, 2009 - v1
Checksum:iA4ED6B3B762DCB26
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061W → C in ADE67053 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GQ354801 mRNA. Translation: ACU29457.1.
GU936494 Genomic DNA. Translation: ADE67053.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GQ354801 mRNA. Translation: ACU29457.1.
GU936494 Genomic DNA. Translation: ADE67053.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y9WX-ray2.30A/B2-392[»]
2Y9XX-ray2.78A/B/C/D2-392[»]
ProteinModelPortaliC7FF04.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiC7FF04.

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
InterProiIPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamiPF00264. Tyrosinase. 1 hit.
[Graphical view]
PRINTSiPR00092. TYROSINASE.
SUPFAMiSSF48056. SSF48056. 1 hit.
PROSITEiPS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiPPO3_AGABI
AccessioniPrimary (citable) accession number: C7FF04
Secondary accession number(s): D5LK97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2012
Last sequence update: September 22, 2009
Last modified: November 26, 2014
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.