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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)DescriptionActionsGraphical viewLength
Metal bindingi61Copper 1; via tele nitrogen1 Publication1
Metal bindingi85Copper 1; via tele nitrogen1 Publication1
Metal bindingi94Copper 1; via tele nitrogen1 Publication1
Metal bindingi259Copper 2; via tele nitrogen1 Publication1
Metal bindingi263Copper 2; via tele nitrogen1 Publication1
Binding sitei263Substrate1 Publication1
Metal bindingi296Copper 2; via tele nitrogen1 Publication1

GO - Molecular functioni

GO - Biological processi

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)DescriptionActionsGraphical viewLength
ChainiPRO_00004168641 – 392Polyphenol oxidase 3Add BLAST392
PropeptideiPRO_0000416865393 – 576Removed in mature formCuratedAdd BLAST184

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki83 ↔ 852'-(S-cysteinyl)-histidine (Cys-His)1 Publication

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei392 – 393CleavageCurated2

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

1576
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 8Combined sources3
Helixi23 – 26Combined sources4
Helixi30 – 45Combined sources16
Helixi54 – 59Combined sources6
Beta strandi62 – 64Combined sources3
Beta strandi69 – 72Combined sources4
Helixi90 – 113Combined sources24
Helixi121 – 130Combined sources10
Helixi152 – 155Combined sources4
Beta strandi158 – 163Combined sources6
Beta strandi169 – 173Combined sources5
Turni175 – 177Combined sources3
Helixi191 – 194Combined sources4
Beta strandi200 – 202Combined sources3
Beta strandi206 – 208Combined sources3
Helixi210 – 233Combined sources24
Helixi238 – 242Combined sources5
Turni245 – 249Combined sources5
Helixi255 – 267Combined sources13
Helixi279 – 281Combined sources3
Turni283 – 285Combined sources3
Helixi286 – 288Combined sources3
Helixi291 – 309Combined sources19
Turni310 – 312Combined sources3
Beta strandi318 – 320Combined sources3
Beta strandi325 – 327Combined sources3
Beta strandi331 – 333Combined sources3
Beta strandi337 – 343Combined sources7
Beta strandi349 – 351Combined sources3
Helixi352 – 355Combined sources4
Helixi358 – 361Combined sources4
Beta strandi362 – 364Combined sources3
Helixi366 – 371Combined sources6
Helixi376 – 391Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Y9WX-ray2.30A/B2-392[»]
2Y9XX-ray2.78A/B/C/D2-392[»]
ProteinModelPortaliC7FF04.
SMRiC7FF04.
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)DescriptionActionsGraphical viewLength
Sequence conflicti106W → C in ADE67053 (Ref. 2) Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Y9WX-ray2.30A/B2-392[»]
2Y9XX-ray2.78A/B/C/D2-392[»]
ProteinModelPortaliC7FF04.
SMRiC7FF04.
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...

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 2, 2016
This is version 25 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

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 one 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.