Q06355 (PPOB_SOLTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Catechol oxidase B, chloroplastic EC=1.10.3.1 Alternative name(s): Polyphenol oxidase Short name=PPO
Organism	Solanum tuberosum (Potato) [Reference proteome]
Taxonomic identifier	4113 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum

Protein attributes

Sequence length	588 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Plastid › chloroplast thylakoid lumen.
Sequence similarities	Belongs to the tyrosinase family.

Ontologies

Keywords
Cellular component	Chloroplast Plastid Thylakoid
Domain	Transit peptide
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond Thioether bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	pigment biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	chloroplast thylakoid lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	catechol oxidase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	‹1 – 88	›88	Chloroplast Potential
	Chain	89 – 588	500	Catechol oxidase B, chloroplastic		PRO_0000035917
Sites
	Metal binding	180	1	Copper A By similarity
	Metal binding	198	1	Copper A By similarity
	Metal binding	207	1	Copper A By similarity
	Metal binding	329	1	Copper B By similarity
	Metal binding	333	1	Copper B By similarity
	Metal binding	364	1	Copper B By similarity
Amino acid modifications
	Disulfide bond	99 ↔ 115		By similarity
	Disulfide bond	114 ↔ 181		By similarity
	Cross-link	184 ↔ 198		2'-(S-cysteinyl)-histidine (Cys-His) By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Q06355 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: A7E25383273428CC	FASTA	588	66,241
	10 20 30 40 50 60 SSSSTTTIPL CTNKSLSSSF TTNNSSFLSK PSQLFLHGRR NQSFKVSCNA NNNVGEHDKN 70 80 90 100 110 120 LDTVDRRNVL LGLGGLYGAA NLAPLASASP IPPPDLKSCG VAHVTEGVDV TYSCCPPVPD 130 140 150 160 170 180 DIDSVPYYKF PPMTKLRIRP PAHAADEEYV AKYQLATSRM RELDKDSFDP LGFKQQANIH 190 200 210 220 230 240 CAYCNGAYKV GGKELQVHFS WLFFPFHRWY LYFYERILGS LINDPTFALP YWNWDHPKGM 250 260 270 280 290 300 RIPPMFDREG SSLYDDKRNQ NHRNGTIIDL GHFGQEVDTP QLQIMTNNLT LMYRQMVTNA 310 320 330 340 350 360 PCPSQFFGAA YPLGTEPSPG MGTIENIPHT PVHIWTGDSP RQKNGENMGN FYSAGLDPIF 370 380 390 400 410 420 YCHHANVDRM WDEWKLIGGK RRDLSNKDWL NSEFFFYDEN RNPYRVKVRD CLDSKKMGFS 430 440 450 460 470 480 YAPMPTPWRN FKPIRKTTAG KVNTASIAPV TKVFPLAKLD RAISFSITRP ASSRTTQEKN 490 500 510 520 530 540 EQEEILTFNK VAYDDTKYVR FDVFLNVDKT VNADELDKAE FAGSYTSLPH VHGNNTNHVT 550 560 570 580 SVTFKLAITE LLEDNGLEDE DTIAVTLVPK VGGEGVSIES VEIKLEDC

References

[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M95197 mRNA. Translation: AAA02879.1.
PIR	S30929.
3D structure databases
ProteinModelPortal	Q06355.
SMR	Q06355. Positions 89-429.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	1.10.1280.10. 1 hit.
InterPro	IPR016213. Polyphenol_oxidase. IPR022740. Polyphenol_oxidase_C. IPR022739. Polyphenol_oxidase_cen. IPR002227. Tyrosinase. IPR008922. Unchr_di-copper_centre. [Graphical view]
Pfam	PF12142. PPO1_DWL. 1 hit. PF12143. PPO1_KFDV. 1 hit. PF00264. Tyrosinase. 1 hit. [Graphical view]
PIRSF	PIRSF000290. PPO_plant. 1 hit.
PRINTS	PR00092. TYROSINASE.
SUPFAM	SSF48056. Di-copper_centre. 1 hit.
PROSITE	PS00497. TYROSINASE_1. 1 hit. PS00498. TYROSINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PPOB_SOLTU

Accession

Primary (citable) accession number: Q06355

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program