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P43310 (PPO_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polyphenol oxidase, chloroplastic

Short name=PPO
EC=1.10.3.1
Alternative name(s):
Catechol oxidase
OrganismSpinacia oleracea (Spinach)
Taxonomic identifier3562 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Protein attributes

Sequence length639 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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

Plastidchloroplast thylakoid lumen.

Sequence similarities

Belongs to the tyrosinase family.

Ontologies

Keywords
   Cellular componentChloroplast
Plastid
Thylakoid
   DomainTransit peptide
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMDisulfide bond
Thioether bond
Gene Ontology (GO)
   Biological_processpigment biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentchloroplast thylakoid lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncatechol oxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 101101Chloroplast Potential
Chain102 – 639538Polyphenol oxidase, chloroplastic
PRO_0000035918

Sites

Metal binding1931Copper A By similarity
Metal binding2141Copper A By similarity
Metal binding2231Copper A By similarity
Metal binding3541Copper B By similarity
Metal binding3581Copper B By similarity
Metal binding3881Copper B By similarity

Amino acid modifications

Disulfide bond111 ↔ 127 By similarity
Disulfide bond126 ↔ 194 By similarity
Cross-link197 ↔ 2142'-(S-cysteinyl)-histidine (Cys-His) By similarity

Sequences

Sequence LengthMass (Da)Tools
P43310 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 56917BBF12F5162A

FASTA63973,237
        10         20         30         40         50         60 
MATLSSPTII TTTSILLNNP FLPKTPQLSA HHHRGVRSVN GKVSCQTKNN NGNDENNQFQ 

        70         80         90        100        110        120 
LIQNPNTNTP YLLDRRNILL GLGGMYAALG SEGANYYNTL AAPILPDVEK CTLSDALWDG 

       130        140        150        160        170        180 
SVGDHCCPPP FDLNITKDFE FKNYHNHVKK VRRPAHKAYE DQEWLNDYKR AIAIMKSLPM 

       190        200        210        220        230        240 
SDPRSHMQQA RVHCAYCDGS YPVLGHNDTR LEVHASWLFP SFHRWYLYFY ERILGKLINK 

       250        260        270        280        290        300 
PDFALPYWNW DHRDGMRIPE IFKEMDSPLF DPNRNTNHLD KMMNLSFVSD EEGSDVNEDD 

       310        320        330        340        350        360 
QYEENILLMR KAMVYPSVSD DPNKAELFLG SPYRAGDKME GDVSGAGILE RMPHNSVHVW 

       370        380        390        400        410        420 
TRSNTIKGNQ DMGAFWSAGR DPLFYCHHSN VDRMWSLWTD VLHGGNFPKT PEYDDYRNAY 

       430        440        450        460        470        480 
FYFYDENANP VRVYVRDSFD TERLGYKYED QELPWMSITQ QQQQQQRQQQ RQPLLGGRLK 

       490        500        510        520        530        540 
TRTFSLVKKV LTELKVMLPL PLKYSVIKTK VDRPKKSRTK EDKLEHEEVL VINFKLGKSK 

       550        560        570        580        590        600 
DFIKFDVYIN DGTDYKPEDK TKINLEYAGS FTSLTHGGGG GGGDMSHMAE EDMGKNTVLK 

       610        620        630 
LALNQLLEDL DATDDDSIQV TIVPKSGTDS IVITGIDIE 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U19270 mRNA. Translation: AAC49041.1.
Z66559 mRNA. Translation: CAA91448.1.

3D structure databases

ProteinModelPortalP43310.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.1280.10. 1 hit.
InterProIPR016213. Polyphenol_oxidase.
IPR022740. Polyphenol_oxidase_C.
IPR022739. Polyphenol_oxidase_cen.
IPR002227. Tyrosinase.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamPF12142. PPO1_DWL. 1 hit.
PF12143. PPO1_KFDV. 1 hit.
PF00264. Tyrosinase. 1 hit.
[Graphical view]
PIRSFPIRSF000290. PPO_plant. 1 hit.
PRINTSPR00092. TYROSINASE.
SUPFAMSSF48056. SSF48056. 1 hit.
PROSITEPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePPO_SPIOL
AccessionPrimary (citable) accession number: P43310
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 19, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families