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Protein

Catechol oxidase B, chloroplastic

Gene
N/A
Organism
Solanum tuberosum (Potato)
Status
Reviewed-Annotation score: 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 bindingi180 – 1801Copper ABy similarity
Metal bindingi198 – 1981Copper ABy similarity
Metal bindingi207 – 2071Copper ABy similarity
Metal bindingi329 – 3291Copper BBy similarity
Metal bindingi333 – 3331Copper BBy similarity
Metal bindingi364 – 3641Copper BBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Catechol oxidase B, chloroplastic (EC:1.10.3.1)
Alternative name(s):
Polyphenol oxidase
Short name:
PPO
OrganismiSolanum tuberosum (Potato)
Taxonomic identifieri4113 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
ProteomesiUP000011115 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei‹1 – 88›88ChloroplastSequence AnalysisAdd
BLAST
Chaini89 – 588500Catechol oxidase B, chloroplasticPRO_0000035917Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi99 ↔ 115By similarity
Disulfide bondi114 ↔ 181By similarity
Cross-linki184 ↔ 1982'-(S-cysteinyl)-histidine (Cys-His)By similarity

Keywords - PTMi

Disulfide bond, Thioether bond

Structurei

3D structure databases

ProteinModelPortaliQ06355.
SMRiQ06355. Positions 89-429.
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: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q06355-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SSSSTTTIPL CTNKSLSSSF TTNNSSFLSK PSQLFLHGRR NQSFKVSCNA
60 70 80 90 100
NNNVGEHDKN LDTVDRRNVL LGLGGLYGAA NLAPLASASP IPPPDLKSCG
110 120 130 140 150
VAHVTEGVDV TYSCCPPVPD DIDSVPYYKF PPMTKLRIRP PAHAADEEYV
160 170 180 190 200
AKYQLATSRM RELDKDSFDP LGFKQQANIH CAYCNGAYKV GGKELQVHFS
210 220 230 240 250
WLFFPFHRWY LYFYERILGS LINDPTFALP YWNWDHPKGM RIPPMFDREG
260 270 280 290 300
SSLYDDKRNQ NHRNGTIIDL GHFGQEVDTP QLQIMTNNLT LMYRQMVTNA
310 320 330 340 350
PCPSQFFGAA YPLGTEPSPG MGTIENIPHT PVHIWTGDSP RQKNGENMGN
360 370 380 390 400
FYSAGLDPIF YCHHANVDRM WDEWKLIGGK RRDLSNKDWL NSEFFFYDEN
410 420 430 440 450
RNPYRVKVRD CLDSKKMGFS YAPMPTPWRN FKPIRKTTAG KVNTASIAPV
460 470 480 490 500
TKVFPLAKLD RAISFSITRP ASSRTTQEKN EQEEILTFNK VAYDDTKYVR
510 520 530 540 550
FDVFLNVDKT VNADELDKAE FAGSYTSLPH VHGNNTNHVT SVTFKLAITE
560 570 580
LLEDNGLEDE DTIAVTLVPK VGGEGVSIES VEIKLEDC
Length:588
Mass (Da):66,241
Last modified:November 1, 1995 - v1
Checksum:iA7E25383273428CC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95197 mRNA. Translation: AAA02879.1.
PIRiS30929.
UniGeneiStu.266.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95197 mRNA. Translation: AAA02879.1.
PIRiS30929.
UniGeneiStu.266.

3D structure databases

ProteinModelPortaliQ06355.
SMRiQ06355. Positions 89-429.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]
ProtoNetiSearch...

Publicationsi

  1. "cDNA cloning and expression of potato polyphenol oxidase."
    Hunt M.D., Eannetta N.T., Yu H., Newman S.M., Steffens J.C.
    Plant Mol. Biol. 21:59-68(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Katahdin.
    Tissue: Leaf.

Entry informationi

Entry nameiPPOB_SOLTU
AccessioniPrimary (citable) accession number: Q06355
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 24, 2015
This is version 78 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.