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P43311

- PPO_VITVI

UniProt

P43311 - PPO_VITVI

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Protein
Polyphenol oxidase, chloroplastic
Gene
N/A
Organism
Vitis vinifera (Grape)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of mono- and o-diphenols to o-diquinones.1 Publication

Catalytic activityi

2 catechol + O2 = 2 1,2-benzoquinone + 2 H2O.1 Publication

Cofactori

Binds 2 copper ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi190 – 1901Copper A
Metal bindingi211 – 2111Copper A
Metal bindingi220 – 2201Copper A
Metal bindingi342 – 3421Copper B
Metal bindingi346 – 3461Copper B
Metal bindingi375 – 3751Copper B

GO - Molecular functioni

  1. catechol oxidase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. pigment biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

BRENDAi1.10.3.1. 6671.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyphenol oxidase, chloroplastic (EC:1.10.3.1)
Short name:
PPO
Alternative name(s):
Catechol oxidase
OrganismiVitis vinifera (Grape)
Taxonomic identifieri29760 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsVitalesVitaceaeVitis

Subcellular locationi

GO - Cellular componenti

  1. chloroplast thylakoid lumen Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 103103Chloroplast Reviewed prediction
Add
BLAST
Chaini104 – 607504Polyphenol oxidase, chloroplastic
PRO_0000035920Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi114 ↔ 1291 Publication
Disulfide bondi128 ↔ 1911 Publication
Cross-linki194 ↔ 2112'-(S-cysteinyl)-histidine (Cys-His) By similarity

Keywords - PTMi

Disulfide bond, Thioether bond

Proteomic databases

PRIDEiP43311.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi111 – 1133
Beta strandi136 – 1383
Beta strandi144 – 1463
Beta strandi149 – 1513
Helixi154 – 1563
Helixi159 – 17315
Helixi183 – 19412
Beta strandi211 – 2133
Helixi216 – 23419
Helixi250 – 2523
Helixi257 – 2604
Beta strandi262 – 2643
Helixi273 – 2753
Helixi294 – 30916
Turni310 – 3123
Helixi316 – 3205
Helixi336 – 3394
Helixi342 – 3498
Beta strandi352 – 3554
Turni357 – 3604
Turni362 – 3643
Helixi365 – 3673
Helixi371 – 38515
Helixi399 – 4024
Beta strandi405 – 4095
Beta strandi415 – 4195
Helixi420 – 4234
Turni426 – 4305
Beta strandi431 – 4333

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P3XX-ray2.20A104-442[»]
ProteinModelPortaliP43311.
SMRiP43311. Positions 104-441.

Miscellaneous databases

EvolutionaryTraceiP43311.

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG254493.

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
InterProiIPR013788. Hemocyanin/hexamerin.
IPR016213. Polyphenol_oxidase.
IPR022740. Polyphenol_oxidase_C.
IPR022739. Polyphenol_oxidase_cen.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamiPF12142. PPO1_DWL. 1 hit.
PF12143. PPO1_KFDV. 1 hit.
PF00264. Tyrosinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000290. PPO_plant. 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.

P43311-1 [UniParc]FASTAAdd to Basket

« Hide

MASLPWSLTT STAIANTTNI SAFPPSPLFQ RASHVPVARN RSRRFAPSKV    50
SCNSANGDPN SDSTSDVRET SSGKLDRRNV LLGIGGLYGA AGGLGATKPL 100
AFGAPIQAPD ISKCGTATVP DGVTPTNCCP PVTTKIIDFQ LPSSGSPMRT 150
RPAAHLVSKE YLAKYKKAIE LQKALPDDDP RSFKQQANVH CTYCQGAYDQ 200
VGYTDLELQV HASWLFLPFH RYYLYFNERI LAKLIDDPTF ALPYWAWDNP 250
DGMYMPTIYA SSPSSLYDEK RNAKHLPPTV IDLDYDGTEP TIPDDELKTD 300
NLAIMYKQIV SGATTPKLFL GYPYRAGDAI DPGAGTLEHA PHNIVHKWTG 350
LADKPSEDMG NFYTAGRDPI FFGHHANVDR MWNIWKTIGG KNRKDFTDTD 400
WLDATFVFYD ENKQLVKVKV SDCVDTSKLR YQYQDIPIPW LPKNTKAKAK 450
TTTKSSKSGV AKAAELPKTT ISSIGDFPKA LNSVIRVEVP RPKKSRSKKE 500
KEDEEEVLLI KGIELDRENF VKFDVYINDE DYSVSRPKNS EFAGSFVNVP 550
HKHMKEMKTK TNLRFAINEL LEDLGAEDDE SVIVTIVPRA GGDDVTIGGI 600
EIEFVSD 607
Length:607
Mass (Da):67,347
Last modified:November 1, 1995 - v1
Checksum:iB9045598E69BC57B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z27411 mRNA. Translation: CAA81798.1.
UniGeneiVvi.108.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z27411 mRNA. Translation: CAA81798.1 .
UniGenei Vvi.108.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2P3X X-ray 2.20 A 104-442 [» ]
ProteinModelPortali P43311.
SMRi P43311. Positions 104-441.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P43311.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi NOG254493.

Enzyme and pathway databases

BRENDAi 1.10.3.1. 6671.

Miscellaneous databases

EvolutionaryTracei P43311.

Family and domain databases

Gene3Di 1.10.1280.10. 1 hit.
InterProi IPR013788. Hemocyanin/hexamerin.
IPR016213. Polyphenol_oxidase.
IPR022740. Polyphenol_oxidase_C.
IPR022739. Polyphenol_oxidase_cen.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view ]
Pfami PF12142. PPO1_DWL. 1 hit.
PF12143. PPO1_KFDV. 1 hit.
PF00264. Tyrosinase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000290. PPO_plant. 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. "Molecular cloning and characterisation of grape berry polyphenol oxidase."
    Dry I.B., Robinson S.P.
    Plant Mol. Biol. 26:495-502(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Sultana.
    Tissue: Fruit.
  2. "Cloning, sequencing, purification, and crystal structure of Grenache (Vitis vinifera) polyphenol oxidase."
    Virador V.M., Reyes Grajeda J.P., Blanco-Labra A., Mendiola-Olaya E., Smith G.M., Moreno A., Whitaker J.R.
    J. Agric. Food Chem. 58:1189-1201(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 104-442 IN COMPLEX WITH COPPER IONS, FUNCTION, CATALYTIC ACTIVITY, DISULFIDE BONDS.

Entry informationi

Entry nameiPPO_VITVI
AccessioniPrimary (citable) accession number: P43311
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 11, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant 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

External Data

Dasty 3

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