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Q06355

- PPOB_SOLTU

UniProt

Q06355 - PPOB_SOLTU

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Protein
Catechol oxidase B, chloroplastic
Gene
N/A
Organism
Solanum tuberosum (Potato)
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

Binds 2 copper ions per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi180 – 1801Copper A By similarity
Metal bindingi198 – 1981Copper A By similarity
Metal bindingi207 – 2071Copper A By similarity
Metal bindingi329 – 3291Copper B By similarity
Metal bindingi333 – 3331Copper B By similarity
Metal bindingi364 – 3641Copper B By 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:
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: Unplaced

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 peptidei‹1 – 88›88Chloroplast Reviewed prediction
Add
BLAST
Chaini89 – 588500Catechol oxidase B, chloroplastic
PRO_0000035917Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi99 ↔ 115 By similarity
Disulfide bondi114 ↔ 181 By 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.

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.

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

SSSSTTTIPL CTNKSLSSSF TTNNSSFLSK PSQLFLHGRR NQSFKVSCNA    50
NNNVGEHDKN LDTVDRRNVL LGLGGLYGAA NLAPLASASP IPPPDLKSCG 100
VAHVTEGVDV TYSCCPPVPD DIDSVPYYKF PPMTKLRIRP PAHAADEEYV 150
AKYQLATSRM RELDKDSFDP LGFKQQANIH CAYCNGAYKV GGKELQVHFS 200
WLFFPFHRWY LYFYERILGS LINDPTFALP YWNWDHPKGM RIPPMFDREG 250
SSLYDDKRNQ NHRNGTIIDL GHFGQEVDTP QLQIMTNNLT LMYRQMVTNA 300
PCPSQFFGAA YPLGTEPSPG MGTIENIPHT PVHIWTGDSP RQKNGENMGN 350
FYSAGLDPIF YCHHANVDRM WDEWKLIGGK RRDLSNKDWL NSEFFFYDEN 400
RNPYRVKVRD CLDSKKMGFS YAPMPTPWRN FKPIRKTTAG KVNTASIAPV 450
TKVFPLAKLD RAISFSITRP ASSRTTQEKN EQEEILTFNK VAYDDTKYVR 500
FDVFLNVDKT VNADELDKAE FAGSYTSLPH VHGNNTNHVT SVTFKLAITE 550
LLEDNGLEDE DTIAVTLVPK VGGEGVSIES VEIKLEDC 588
Length:588
Mass (Da):66,241
Last modified:November 1, 1995 - v1
Checksum:iA7E25383273428CC
GO

Non-terminal residue

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M95197 mRNA. Translation: AAA02879.1.
PIRiS30929.
UniGeneiStu.266.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M95197 mRNA. Translation: AAA02879.1 .
PIRi S30929.
UniGenei Stu.266.

3D structure databases

ProteinModelPortali Q06355.
SMRi Q06355. Positions 89-429.
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. "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 11, 2014
This is version 73 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

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