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C7FF05

- PPO4_AGABI

UniProt

C7FF05 - PPO4_AGABI

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Protein

Polyphenol oxidase 4

Gene

PPO4

Organism
Agaricus bisporus (White button mushroom)
Status
Reviewed - 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 bindingi82 – 821Copper 1; via tele nitrogenBy similarity
Metal bindingi91 – 911Copper 1; via tele nitrogenBy similarity
Metal bindingi251 – 2511Copper 2; via tele nitrogenBy similarity
Metal bindingi255 – 2551Copper 2; via tele nitrogenBy similarity
Binding sitei255 – 2551SubstrateBy similarity
Metal bindingi283 – 2831Copper 2; via tele nitrogenBy similarity
Sitei379 – 3802CleavageCurated

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 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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 379379Polyphenol oxidase 4PRO_0000416866Add
BLAST
Propeptidei380 – 611232Removed in mature formCuratedPRO_0000416867Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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

Keywords - PTMi

Thioether bond

Interactioni

Subunit structurei

Heterotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliC7FF05.
ModBaseiSearch...
MobiDBiSearch...

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.
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.

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.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortali C7FF05.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

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 PS00497. TYROSINASE_1. 1 hit.
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.

Entry informationi

Entry nameiPPO4_AGABI
AccessioniPrimary (citable) accession number: C7FF05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2012
Last sequence update: September 22, 2009
Last modified: November 26, 2014
This is version 21 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