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C7FF04

- PPO3_AGABI

UniProt

C7FF04 - PPO3_AGABI

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Protein
Polyphenol oxidase 3
Gene
PPO3
Organism
Agaricus bisporus (White button mushroom)
Status
Reviewed - 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.

Catalytic activityi

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

Cofactori

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 – 2631Substrate
Metal bindingi296 – 2961Copper 2; via tele nitrogen
Sitei392 – 3932Cleavage Inferred

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 3
PRO_0000416864Add
BLAST
Propeptidei393 – 576184Removed in mature form Inferred
PRO_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).

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiC7FF04.

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.

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

MSDKKSLMPL VGIPGEIKNR LNILDFVKND KFFTLYVRAL QVLQARDQSD    50
YSSFFQLGGI HGLPYTEWAK AQPQLHLYKA NYCTHGTVLF PTWHRAYEST 100
WEQTLWEAAG TVAQRFTTSD QAEWIQAAKD LRQPFWDWGY WPNDPDFIGL 150
PDQVIRDKQV EITDYNGTKI EVENPILHYK FHPIEPTFEG DFAQWQTTMR 200
YPDVQKQENI EGMIAGIKAA APGFREWTFN MLTKNYTWEL FSNHGAVVGA 250
HANSLEMVHN TVHFLIGRDP TLDPLVPGHM GSVPHAAFDP IFWMHHCNVD 300
RLLALWQTMN YDVYVSEGMN REATMGLIPG QVLTEDSPLE PFYTKNQDPW 350
QSDDLEDWET LGFSYPDFDP VKGKSKEEKS VYINDWVHKH YGFVTTQTEN 400
PALRLLSSFQ RAKSDHETQY ALYDWVIHAT FRYYELNNSF SIIFYFDEGE 450
GCTLESIIGT VDAFRGTTSE NCANCARSQD LIAEGFVHLN YYIGCDIGQH 500
ADHEDDAVPL YEPTRVKEYL KKRKIGCKVV SAEGELTSLV VEIKGAPYYL 550
PVGEARPKLD HEKPIVILDD IIHRVN 576
Length:576
Mass (Da):66,267
Last modified:September 22, 2009 - v1
Checksum:iA4ED6B3B762DCB26
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061W → C in ADE67053. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
GQ354801 mRNA. Translation: ACU29457.1.
GU936494 Genomic DNA. Translation: ADE67053.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
GQ354801 mRNA. Translation: ACU29457.1 .
GU936494 Genomic DNA. Translation: ADE67053.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2Y9W X-ray 2.30 A/B 2-392 [» ]
2Y9X X-ray 2.78 A/B/C/D 2-392 [» ]
ProteinModelPortali C7FF04.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei C7FF04.

Family and domain databases

Gene3Di 1.10.1280.10. 1 hit.
InterProi IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view ]
Pfami PF00264. Tyrosinase. 1 hit.
[Graphical view ]
PRINTSi PR00092. TYROSINASE.
SUPFAMi SSF48056. SSF48056. 1 hit.
PROSITEi PS00498. TYROSINASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 20 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

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