C7FF04 (PPO3_AGABI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Polyphenol oxidase 3
Short name=PPO3
Short name=Phenolase 3
EC=1.14.18.1

Alternative name(s):
Cresolase
Tyrosinase 3

Gene names

Name:

PPO3

Organism

Agaricus bisporus (White button mushroom)

Taxonomic identifier

5341 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Agaricomycetes › Agaricomycetidae › Agaricales › Agaricaceae › Agaricus

Protein attributes

Sequence length	576 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	2 L-dopa + O2 = 2 dopaquinone + 2 H2O. L-tyrosine + O2 = dopaquinone + H2O.
Cofactor	Binds 2 copper ions per subunit. Ref.3
Subunit structure	Tetramer composed of two subunits of PPO3 (H subunits) and two subunits of the as yet uncharacterized product of ORF239342 (L subunits).
Post-translational modification	The C-ter is probably cleaved after Gly-392 since the mature active protein is smaller than the protein encoded by the gene.
Sequence similarities	Belongs to the tyrosinase family.

Ontologies

Keywords
Biological process	Melanin biosynthesis
Ligand	Copper Metal-binding
Molecular function	Monooxygenase Oxidoreductase
PTM	Thioether bond
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	melanin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW monophenol monooxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 392

392

Polyphenol oxidase 3

PRO_0000416864

Propeptide

393 – 576

184

Removed in mature form Probable

PRO_0000416865

Sites

Metal binding

61

1

Copper 1; via tele nitrogen

Metal binding

85

1

Copper 1; via tele nitrogen

Metal binding

94

1

Copper 1; via tele nitrogen

Metal binding

259

1

Copper 2; via tele nitrogen

Metal binding

263

1

Copper 2; via tele nitrogen

Metal binding

296

1

Copper 2; via tele nitrogen

Binding site

263

1

Substrate

Site

392 – 393

2

Cleavage Probable

Amino acid modifications

Cross-link

83 ↔ 85

2'-(S-cysteinyl)-histidine (Cys-His)

Experimental info

Sequence conflict

106

1

W → C in ADE67053. Ref.2

Secondary structure

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576

Helix Strand Turn

Details...

Beta strand

6 – 8

3

Helix

23 – 26

4

Helix

30 – 45

16

Helix

54 – 59

6

Beta strand

62 – 64

3

Beta strand

69 – 72

4

Helix

90 – 113

24

Helix

121 – 130

10

Helix

152 – 155

4

Beta strand

158 – 163

6

Beta strand

169 – 173

5

Turn

175 – 177

3

Helix

191 – 194

4

Beta strand

200 – 202

3

Beta strand

206 – 208

3

Helix

210 – 233

24

Helix

238 – 242

5

Turn

245 – 249

5

Helix

255 – 267

13

Helix

279 – 281

3

Turn

283 – 285

3

Helix

286 – 288

3

Helix

291 – 309

19

Turn

310 – 312

3

Beta strand

318 – 320

3

Beta strand

325 – 327

3

Beta strand

331 – 333

3

Beta strand

337 – 343

7

Beta strand

349 – 351

3

Helix

352 – 355

4

Helix

358 – 361

4

Beta strand

362 – 364

3

Helix

366 – 371

6

Helix

376 – 391

16

Sequences

	Sequence		Length	Mass (Da)
	C7FF04 [UniParc]. Last modified September 22, 2009. Version 1. Checksum: A4ED6B3B762DCB26	FASTA	576	66,267
	10 20 30 40 50 60 MSDKKSLMPL VGIPGEIKNR LNILDFVKND KFFTLYVRAL QVLQARDQSD YSSFFQLGGI 70 80 90 100 110 120 HGLPYTEWAK AQPQLHLYKA NYCTHGTVLF PTWHRAYEST WEQTLWEAAG TVAQRFTTSD 130 140 150 160 170 180 QAEWIQAAKD LRQPFWDWGY WPNDPDFIGL PDQVIRDKQV EITDYNGTKI EVENPILHYK 190 200 210 220 230 240 FHPIEPTFEG DFAQWQTTMR YPDVQKQENI EGMIAGIKAA APGFREWTFN MLTKNYTWEL 250 260 270 280 290 300 FSNHGAVVGA HANSLEMVHN TVHFLIGRDP TLDPLVPGHM GSVPHAAFDP IFWMHHCNVD 310 320 330 340 350 360 RLLALWQTMN YDVYVSEGMN REATMGLIPG QVLTEDSPLE PFYTKNQDPW QSDDLEDWET 370 380 390 400 410 420 LGFSYPDFDP VKGKSKEEKS VYINDWVHKH YGFVTTQTEN PALRLLSSFQ RAKSDHETQY 430 440 450 460 470 480 ALYDWVIHAT FRYYELNNSF SIIFYFDEGE GCTLESIIGT VDAFRGTTSE NCANCARSQD 490 500 510 520 530 540 LIAEGFVHLN YYIGCDIGQH ADHEDDAVPL YEPTRVKEYL KKRKIGCKVV SAEGELTSLV 550 560 570 VEIKGAPYYL PVGEARPKLD HEKPIVILDD IIHRVN

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

GQ354801 mRNA. Translation: ACU29457.1.
GU936494 Genomic DNA. Translation: ADE67053.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

C7FF04.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

1.10.1280.10. 1 hit.

InterPro

IPR002227. Tyrosinase.
IPR008922. Unchr_di-copper_centre.
[Graphical view]

Pfam

PF00264. Tyrosinase. 1 hit.
[Graphical view]

PRINTS

PR00092. TYROSINASE.

SUPFAM

SSF48056. Di-copper_centre. 1 hit.

PROSITE

PS00498. TYROSINASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

C7FF04.

Entry information

Entry name

PPO3_AGABI

Accession

Primary (citable) accession number: C7FF04
Secondary accession number(s): D5LK97

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 18, 2012
Last sequence update:	September 22, 2009
Last modified:	March 6, 2013
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program