Reviewed, UniProtKB/Swiss-Prot P43311 (PPO_VITVI)

Names and origin

Protein names	Recommended name:     Polyphenol oxidase, chloroplastic       Short name=PPO     EC=1.10.3.1 Alternative name(s):     Catechol oxidase
Organism	Vitis vinifera (Grape)
Taxonomic identifier	29760 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Vitales › Vitaceae › Vitis

Protein attributes

Sequence length	607 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	Catalyzes the oxidation of mono- and o-diphenols to o-diquinones.
Catalytic activity	2 catechol + O2 = 2 1,2-benzoquinone + 2 H2O.
Cofactor	Binds 2 copper ions per subunit By similarity.
Subcellular location	Plastid › chloroplast thylakoid lumen.
Sequence similarities	Belongs to the tyrosinase family.

Ontologies

Keywords
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond Thioether bond
Technical term	3D-structure
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast thylakoid lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	catechol oxidase activity Inferred from electronic annotation. Source: EC copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 103

103

Chloroplast Potential

Chain

104 – 607

504

Polyphenol oxidase, chloroplastic

PRO_0000035920

Sites

Metal binding

190

1

Copper A By similarity

Metal binding

211

1

Copper A By similarity

Metal binding

220

1

Copper A By similarity

Metal binding

342

1

Copper B By similarity

Metal binding

346

1

Copper B By similarity

Metal binding

375

1

Copper B By similarity

Amino acid modifications

Disulfide bond

114 ↔ 129

By similarity

Disulfide bond

128 ↔ 191

By similarity

Cross-link

194 ↔ 211

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

Secondary structure

1

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607

Helix Strand Turn

Details...

Helix

111 – 113

3

Beta strand

136 – 138

3

Beta strand

144 – 146

3

Beta strand

149 – 151

3

Helix

154 – 156

3

Helix

159 – 173

15

Helix

183 – 194

12

Beta strand

211 – 213

3

Helix

216 – 234

19

Helix

250 – 252

3

Helix

257 – 260

4

Beta strand

262 – 264

3

Helix

273 – 275

3

Helix

294 – 309

16

Turn

310 – 312

3

Helix

316 – 320

5

Helix

336 – 339

4

Helix

342 – 349

8

Beta strand

352 – 355

4

Turn

357 – 360

4

Turn

362 – 364

3

Helix

365 – 367

3

Helix

371 – 385

15

Helix

399 – 402

4

Beta strand

405 – 409

5

Beta strand

415 – 419

5

Helix

420 – 423

4

Turn

426 – 430

5

Beta strand

431 – 433

3

Sequences

	Sequence		Length	Mass (Da)
	P43311-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: B9045598E69BC57B	FASTA	607	67,347
	10 20 30 40 50 60 MASLPWSLTT STAIANTTNI SAFPPSPLFQ RASHVPVARN RSRRFAPSKV SCNSANGDPN 70 80 90 100 110 120 SDSTSDVRET SSGKLDRRNV LLGIGGLYGA AGGLGATKPL AFGAPIQAPD ISKCGTATVP 130 140 150 160 170 180 DGVTPTNCCP PVTTKIIDFQ LPSSGSPMRT RPAAHLVSKE YLAKYKKAIE LQKALPDDDP 190 200 210 220 230 240 RSFKQQANVH CTYCQGAYDQ VGYTDLELQV HASWLFLPFH RYYLYFNERI LAKLIDDPTF 250 260 270 280 290 300 ALPYWAWDNP DGMYMPTIYA SSPSSLYDEK RNAKHLPPTV IDLDYDGTEP TIPDDELKTD 310 320 330 340 350 360 NLAIMYKQIV SGATTPKLFL GYPYRAGDAI DPGAGTLEHA PHNIVHKWTG LADKPSEDMG 370 380 390 400 410 420 NFYTAGRDPI FFGHHANVDR MWNIWKTIGG KNRKDFTDTD WLDATFVFYD ENKQLVKVKV 430 440 450 460 470 480 SDCVDTSKLR YQYQDIPIPW LPKNTKAKAK TTTKSSKSGV AKAAELPKTT ISSIGDFPKA 490 500 510 520 530 540 LNSVIRVEVP RPKKSRSKKE KEDEEEVLLI KGIELDRENF VKFDVYINDE DYSVSRPKNS 550 560 570 580 590 600 EFAGSFVNVP HKHMKEMKTK TNLRFAINEL LEDLGAEDDE SVIVTIVPRA GGDDVTIGGI EIEFVSD

References

[1]	"Molecular cloning and characterisation of grape berry polyphenol oxidase." Dry I.B., Robinson S.P. Plant Mol. Biol. 26:495-502(1994) [PubMed: 7948897] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Sultana. Tissue: Fruit.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Z27411 mRNA. Translation: CAA81798.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2P3X	X-ray	2.20	A	104-442	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.10.3.1. 81671.

Family and domain databases

InterPro

IPR008922. Di-copper_centre.
IPR016213. Polyphenol_Oxase_pln.
IPR002227. Tyrosinase.
[Graphical view]

Gene3D

G3DSA:1.10.1280.10. Di-copper_centre. 1 hit.

Pfam

PF00264. Tyrosinase. 1 hit.
[Graphical view]

PIRSF

PIRSF000290. PPO_plant. 1 hit.

PRINTS

PR00092. TYROSINASE.

PROSITE

PS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PPO_VITVI

Accession

Primary (citable) accession number: P43311

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)