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O42713

- PPO2_AGABI

UniProt

O42713 - PPO2_AGABI

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Protein

Polyphenol oxidase 2

Gene

PPO2

Organism
Agaricus bisporus (White button mushroom)
Status
Reviewed - Annotation score: 4 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

Binds 2 copper ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi57 – 571Copper 1; via tele nitrogenBy similarity
Metal bindingi81 – 811Copper 1; via tele nitrogenBy similarity
Metal bindingi90 – 901Copper 1; via tele nitrogenBy similarity
Metal bindingi250 – 2501Copper 2; via tele nitrogenBy similarity
Metal bindingi254 – 2541Copper 2; via tele nitrogenBy similarity
Binding sitei254 – 2541SubstrateBy similarity
Metal bindingi282 – 2821Copper 2; via tele nitrogenBy similarity
Sitei378 – 3792CleavageCurated

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

Enzyme and pathway databases

SABIO-RKO42713.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyphenol oxidase 2 (EC:1.14.18.1)
Short name:
PPO2
Short name:
Phenolase 2
Alternative name(s):
Cresolase 2
Tyrosinase 2
Gene namesi
Name:PPO2
OrganismiAgaricus bisporus (White button mushroom)
Taxonomic identifieri5341 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesAgaricaceaeAgaricus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 378378Polyphenol oxidase 2PRO_0000186731Add
BLAST
Propeptidei379 – 556178Removed in mature formCuratedPRO_0000416863Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki79 ↔ 812'-(S-cysteinyl)-histidine (Cys-His)By similarity

Post-translational modificationi

The C-ter is probably cleaved after Gly-378 since the mature active protein is smaller than the protein encoded by the gene.By similarity

Keywords - PTMi

Thioether bond

Expressioni

Developmental stagei

Expressed during the fruiting body stage.1 Publication

Interactioni

Subunit structurei

Heterotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO42713.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.Curated

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
InterProiIPR016216. Monophenol_mOase_fun.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamiPF00264. Tyrosinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000340. MPO_fungal. 1 hit.
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.

O42713-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSLIATVGPT GGVKNRLNIV DFVKNEKFFT LYVRSLELLQ AKEQHDYSSF
60 70 80 90 100
FQLAGIHGLP FTEWAKERPS MNLYKAGYCT HGQVLFPTWH RTYLSVLEQI
110 120 130 140 150
LQGAAIEVAK KFTSNQTDWV QAAQDLRQPY WDWGFELMPP DEVIKNEEVN
160 170 180 190 200
ITNYDGKKIS VKNPILRYHF HPIDPSFKPY GDFATWRTTV RNPDRNRRED
210 220 230 240 250
IPGLIKKMRL EEGQIREKTY NMLKFNDAWE RFSNHGISDD QHANSLESVH
260 270 280 290 300
DDIHVMVGYG KIEGHMDHPF FAAFDPIFWL HHTNVDRLLS LWKAINPDVW
310 320 330 340 350
VTSGRNRDGT MGIAPNAQIN SETPLEPFYQ SGDKVWTSAS LADTARLGYS
360 370 380 390 400
YPDFDKLVGG TKELIRDAID DLIDERYGSK PSSGARNTAF DLLADFKGIT
410 420 430 440 450
KEHKEDLKMY DWTIHVAFKK FELKESFSLL FYFASDGGDY DQENCFVGSI
460 470 480 490 500
NAFRGTAPET CANCQDNENL IQEGFIHLNH YLARDLESFE PQDVHKFLKE
510 520 530 540 550
KGLSYKLYSR GDKPLTSLSV KIEGRPLHLP PGEHRPKYDH TQARVVFDDV

AVHVIN
Length:556
Mass (Da):63,927
Last modified:June 1, 1998 - v1
Checksum:iDE10827A209895DA
GO

Sequence cautioni

The sequence CAA61562.1 differs from that shown. Reason: Frameshift at position 445.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ223816 mRNA. Translation: CAA11562.1.
X89382 mRNA. Translation: CAA61562.1. Frameshift.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ223816 mRNA. Translation: CAA11562.1 .
X89382 mRNA. Translation: CAA61562.1 . Frameshift.

3D structure databases

ProteinModelPortali O42713.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi O42713.
ChEMBLi CHEMBL3318.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK O42713.

Family and domain databases

Gene3Di 1.10.1280.10. 1 hit.
InterProi IPR016216. Monophenol_mOase_fun.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view ]
Pfami PF00264. Tyrosinase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000340. MPO_fungal. 1 hit.
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, expression and characterisation of two tyrosinase cDNAs from Agaricus bisporus."
    Wichers H., Recourt K., Hendriks M., Ebbelaar C.E.M., Biancone G., Hoeberichts F., Mooibroek H., Soler-Rivas C.
    Appl. Microbiol. Biotechnol. 61:336-341(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Horst U1.
  2. "Characterization of a fruiting body-expressed gene encoding a putative polyphenol oxidase of Agaricus bisporus."
    Ebbelar C.E.M., Wichers H.J., Van Den Bosch T., Oyevaar J.I., Recourt K.
    Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 122-556.
    Strain: Horst U1.
  3. "Expression of phenol oxidase and heat-shock genes during the development of Agaricus bisporus fruiting bodies, healthy and infected by Lecanicillium fungicola."
    Largeteau M.L., Latapy C., Minvielle N., Regnault-Roger C., Savoie J.M.
    Appl. Microbiol. Biotechnol. 85:1499-1507(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiPPO2_AGABI
AccessioniPrimary (citable) accession number: O42713
Secondary accession number(s): Q12543
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: October 1, 2014
This is version 63 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