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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

Cu2+Note: 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 Source: UniProtKB-KW
  2. thylakoid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 103103ChloroplastSequence AnalysisAdd
BLAST
Chaini104 – 607504Polyphenol oxidase, chloroplasticPRO_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

1
607
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi111 – 1133Combined sources
Beta strandi136 – 1383Combined sources
Beta strandi144 – 1463Combined sources
Beta strandi149 – 1513Combined sources
Helixi154 – 1563Combined sources
Helixi159 – 17315Combined sources
Helixi183 – 19412Combined sources
Beta strandi211 – 2133Combined sources
Helixi216 – 23419Combined sources
Helixi250 – 2523Combined sources
Helixi257 – 2604Combined sources
Beta strandi262 – 2643Combined sources
Helixi273 – 2753Combined sources
Helixi294 – 30916Combined sources
Turni310 – 3123Combined sources
Helixi316 – 3205Combined sources
Helixi336 – 3394Combined sources
Helixi342 – 3498Combined sources
Beta strandi352 – 3554Combined sources
Turni357 – 3604Combined sources
Turni362 – 3643Combined sources
Helixi365 – 3673Combined sources
Helixi371 – 38515Combined sources
Helixi399 – 4024Combined sources
Beta strandi405 – 4095Combined sources
Beta strandi415 – 4195Combined sources
Helixi420 – 4234Combined sources
Turni426 – 4305Combined sources
Beta strandi431 – 4333Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P3XX-ray2.20A104-442[»]
ProteinModelPortaliP43311.
SMRiP43311. Positions 104-441.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43311.

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.Curated

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

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

EIEFVSD
Length:607
Mass (Da):67,347
Last modified:November 1, 1995 - v1
Checksum:iB9045598E69BC57B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z27411 mRNA. Translation: CAA81798.1.
UniGeneiVvi.108.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z27411 mRNA. Translation: CAA81798.1 .
UniGenei Vvi.108.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 83 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