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Protein

Polyphenol oxidase 4

Gene

PPO4

Organism
Agaricus bisporus (White button mushroom)
Status
Reviewed-Annotation score: Annotation score: 3 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+By similarityNote: Binds 2 copper ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi57Copper ABy similarity1
Metal bindingi82Copper ABy similarity1
Metal bindingi91Copper ABy similarity1
Metal bindingi251Copper BBy similarity1
Metal bindingi255Copper BBy similarity1
Binding sitei255SubstrateBy similarity1
Metal bindingi283Copper BBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionMonooxygenase, Oxidoreductase
Biological processMelanin biosynthesis
LigandCopper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Polyphenol oxidase 4 (EC:1.14.18.1)
Short name:
PPO4
Short name:
Phenolase 4
Alternative name(s):
Cresolase
Tyrosinase 4
Gene namesi
Name:PPO4
OrganismiAgaricus bisporus (White button mushroom)
Taxonomic identifieri5341 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesAgaricaceaeAgaricus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004168661 – 379Polyphenol oxidase 4Add BLAST379
PropeptideiPRO_0000416867380 – 611Removed in mature formCuratedAdd BLAST232

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki80 ↔ 822'-(S-cysteinyl)-histidine (Cys-His)By similarity

Post-translational modificationi

The C-ter is probably cleaved after Gly-379 since the mature active protein is smaller than the protein encoded by the gene.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei379 – 380CleavageCurated2

Keywords - PTMi

Thioether bond

Interactioni

Subunit structurei

Heterotetramer.By similarity

Structurei

Secondary structure

1611
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 12Combined sources3
Helixi19 – 22Combined sources4
Helixi26 – 41Combined sources16
Helixi50 – 57Combined sources8
Beta strandi58 – 60Combined sources3
Helixi87 – 110Combined sources24
Turni115 – 118Combined sources4
Helixi119 – 125Combined sources7
Turni134 – 136Combined sources3
Turni142 – 146Combined sources5
Beta strandi148 – 153Combined sources6
Beta strandi159 – 163Combined sources5
Beta strandi165 – 167Combined sources3
Helixi176 – 178Combined sources3
Beta strandi179 – 181Combined sources3
Turni182 – 186Combined sources5
Beta strandi192 – 194Combined sources3
Helixi202 – 225Combined sources24
Helixi231 – 234Combined sources4
Helixi247 – 259Combined sources13
Beta strandi260 – 264Combined sources5
Turni270 – 272Combined sources3
Helixi273 – 275Combined sources3
Helixi279 – 296Combined sources18
Beta strandi312 – 314Combined sources3
Beta strandi330 – 332Combined sources3
Helixi341 – 343Combined sources3
Helixi345 – 348Combined sources4
Helixi353 – 355Combined sources3
Turni357 – 360Combined sources4
Helixi363 – 377Combined sources15
Helixi389 – 397Combined sources9
Beta strandi408 – 420Combined sources13
Beta strandi423 – 426Combined sources4
Beta strandi428 – 434Combined sources7
Beta strandi439 – 441Combined sources3
Beta strandi447 – 452Combined sources6
Beta strandi472 – 478Combined sources7
Helixi480 – 486Combined sources7
Helixi492 – 501Combined sources10
Beta strandi504 – 514Combined sources11
Beta strandi521 – 531Combined sources11
Beta strandi542 – 544Combined sources3
Beta strandi547 – 549Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5M6BX-ray3.25A/B/C/D1-565[»]
ProteinModelPortaliC7FF05.
SMRiC7FF05.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.Curated

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
InterProiView protein in InterPro
IPR016216. Monophenol_mOase_fun.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
PfamiView protein in Pfam
PF00264. Tyrosinase. 1 hit.
PIRSFiPIRSF000340. MPO_fungal. 1 hit.
PRINTSiPR00092. TYROSINASE.
SUPFAMiSSF48056. SSF48056. 1 hit.
PROSITEiView protein in PROSITE
PS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.

Sequencei

Sequence statusi: Complete.

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

C7FF05-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLLATVGPT GGVKNRLDIV DFVRDEKFFT LYVRALQAIQ DKDQADYSSF
60 70 80 90 100
FQLSGIHGLP FTPWAKPKDT PTVPYESGYC THSQVLFPTW HRVYVSIYEQ
110 120 130 140 150
VLQEAAKGIA KKFTVHKKEW VQAAEDLRQP YWDTGFALVP PDEIIKLEQV
160 170 180 190 200
KITNYDGTKI TVRNPILRYS FHPIDPSFSG YPNFDTWRTT VRNPDADKKE
210 220 230 240 250
NIPALIAKLD LEADSTREKT YNMLKFNANW EAFSNHGEFD DTHANSLEAV
260 270 280 290 300
HDDIHGFVGR GAIRGHMTHA LFAAFDPIFW LHHSNVDRHL SLWQALYPGV
310 320 330 340 350
WVTQGPEREG SMGFAPGTEL NKDSALEPFY ETEDKPWTSV PLTDTALLNY
360 370 380 390 400
SYPDFDKVKG GTPDLVRDYI NDHIDRRYGI KKSEGGKNPA LDLLSDFKGV
410 420 430 440 450
THDHNEDLKM FDWTIQASWK KFELDDSFAI IFYFAADGST NVTKENYIGS
460 470 480 490 500
INIFRGTTPT NCANCRTQDN LVQEGFVHLD RFIARDLDTF DPQAVHRYLK
510 520 530 540 550
EKKLSYKVVA DDHSVTLKSL RIRVQGRPLH LPPGVSFPRL DKNIPIVNFD
560 570 580 590 600
DVLDLVTGVV NIGLTAVGAT AGVAIGVVGA TAGTAIGVAG AATDAVTNIA
610
KGGLGALGRI F
Length:611
Mass (Da):68,318
Last modified:September 22, 2009 - v1
Checksum:iD9667D24204E614B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GQ354802 mRNA. Translation: ACU29458.1.
GU936493 Genomic DNA. Translation: ADE67052.1.

Similar proteinsi

Entry informationi

Entry nameiPPO4_AGABI
AccessioniPrimary (citable) accession number: C7FF05
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 18, 2012
Last sequence update: September 22, 2009
Last modified: August 30, 2017
This is version 26 of the entry and version 1 of the sequence. See 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