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P43310

- PPO_SPIOL

UniProt

P43310 - PPO_SPIOL

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Protein

Polyphenol oxidase, chloroplastic

Gene
N/A
Organism
Spinacia oleracea (Spinach)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

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

Cofactori

Cu2+By similarityNote: Binds 2 copper ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi193 – 1931Copper ABy similarity
Metal bindingi214 – 2141Copper ABy similarity
Metal bindingi223 – 2231Copper ABy similarity
Metal bindingi354 – 3541Copper BBy similarity
Metal bindingi358 – 3581Copper BBy similarity
Metal bindingi388 – 3881Copper BBy similarity

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

Names & Taxonomyi

Protein namesi
Recommended name:
Polyphenol oxidase, chloroplastic (EC:1.10.3.1)
Short name:
PPO
Alternative name(s):
Catechol oxidase
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

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 – 101101ChloroplastSequence AnalysisAdd
BLAST
Chaini102 – 639538Polyphenol oxidase, chloroplasticPRO_0000035918Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi111 ↔ 127By similarity
Disulfide bondi126 ↔ 194By similarity
Cross-linki197 ↔ 2142'-(S-cysteinyl)-histidine (Cys-His)By similarity

Keywords - PTMi

Disulfide bond, Thioether bond

Structurei

3D structure databases

ProteinModelPortaliP43310.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.Curated

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
InterProiIPR016213. 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.

P43310-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATLSSPTII TTTSILLNNP FLPKTPQLSA HHHRGVRSVN GKVSCQTKNN
60 70 80 90 100
NGNDENNQFQ LIQNPNTNTP YLLDRRNILL GLGGMYAALG SEGANYYNTL
110 120 130 140 150
AAPILPDVEK CTLSDALWDG SVGDHCCPPP FDLNITKDFE FKNYHNHVKK
160 170 180 190 200
VRRPAHKAYE DQEWLNDYKR AIAIMKSLPM SDPRSHMQQA RVHCAYCDGS
210 220 230 240 250
YPVLGHNDTR LEVHASWLFP SFHRWYLYFY ERILGKLINK PDFALPYWNW
260 270 280 290 300
DHRDGMRIPE IFKEMDSPLF DPNRNTNHLD KMMNLSFVSD EEGSDVNEDD
310 320 330 340 350
QYEENILLMR KAMVYPSVSD DPNKAELFLG SPYRAGDKME GDVSGAGILE
360 370 380 390 400
RMPHNSVHVW TRSNTIKGNQ DMGAFWSAGR DPLFYCHHSN VDRMWSLWTD
410 420 430 440 450
VLHGGNFPKT PEYDDYRNAY FYFYDENANP VRVYVRDSFD TERLGYKYED
460 470 480 490 500
QELPWMSITQ QQQQQQRQQQ RQPLLGGRLK TRTFSLVKKV LTELKVMLPL
510 520 530 540 550
PLKYSVIKTK VDRPKKSRTK EDKLEHEEVL VINFKLGKSK DFIKFDVYIN
560 570 580 590 600
DGTDYKPEDK TKINLEYAGS FTSLTHGGGG GGGDMSHMAE EDMGKNTVLK
610 620 630
LALNQLLEDL DATDDDSIQV TIVPKSGTDS IVITGIDIE
Length:639
Mass (Da):73,237
Last modified:November 1, 1995 - v1
Checksum:i56917BBF12F5162A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19270 mRNA. Translation: AAC49041.1.
Z66559 mRNA. Translation: CAA91448.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19270 mRNA. Translation: AAC49041.1 .
Z66559 mRNA. Translation: CAA91448.1 .

3D structure databases

ProteinModelPortali P43310.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 1.10.1280.10. 1 hit.
InterProi 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. "Spinach thylakoid polyphenol oxidase: cloning, characterization, and relation to a putative protein kinase."
    Hind G., Marshak D.R., Coughlan S.J.
    Biochemistry 34:8157-8164(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Hybrid 424.
    Tissue: Leaf.

Entry informationi

Entry nameiPPO_SPIOL
AccessioniPrimary (citable) accession number: P43310
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 26, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3