Q06215 (PPO_VICFA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Polyphenol oxidase A1, chloroplastic Short name=PPO EC=1.10.3.1 Alternative name(s): Catechol oxidase
Organism	Vicia faba (Broad bean) (Faba vulgaris)
Taxonomic identifier	3906 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Fabeae › Vicia

Protein attributes

Sequence length	606 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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	Direct protein sequencing
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 – 92	92	Chloroplast Ref.2
	Chain	93 – 606	514	Polyphenol oxidase A1, chloroplastic		PRO_0000035919
Sites
	Metal binding	181	1	Copper A By similarity
	Metal binding	202	1	Copper A By similarity
	Metal binding	211	1	Copper A By similarity
	Metal binding	333	1	Copper B By similarity
	Metal binding	337	1	Copper B By similarity
	Metal binding	367	1	Copper B By similarity
Amino acid modifications
	Disulfide bond	103 ↔ 121		By similarity
	Disulfide bond	120 ↔ 182		By similarity
	Cross-link	185 ↔ 202		2'-(S-cysteinyl)-histidine (Cys-His) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q06215 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: FC539F9F041B503C	FASTA	606	68,541
	10 20 30 40 50 60 MTSISALSFI STINVSSNSK ISHSSVYPFL QKQHQSSKLR KPKRQVTCSS NNNQNNPKEE 70 80 90 100 110 120 QELSNIVGHR RNVLIGLGGI YGTLATNPSA LASPISPPDL SKCVPPSDLP SGTTPPNINC 130 140 150 160 170 180 CPPYSTKITD FKFPSNQPLR VRQAAHLVDN EFLEKYKKAT ELMKALPSND PRNFTQQANI 190 200 210 220 230 240 HCAYCDGAYS QIGFPDLKLQ VHGSWLFFPF HRWYLYFYER ILGSLINDPT FALPFWNYDA 250 260 270 280 290 300 PDGMQLPTIY ADKASPLYDE LRNASHQPPT LIDLNFCDIG SDIDRNELIK TNLSIMYRQV 310 320 330 340 350 360 YSNGKTSRLF LGNPYRAGDA EPQGAGSIEN VPHAPVHTWT GDNTQTNIED MGIFYSAARD 370 380 390 400 410 420 PIFYSHHSNV DRLWYIWKTL GGKKHDFTDK DWLESGFLFY DENKNLVRVN VKDSLDIDKL 430 440 450 460 470 480 GYAYQDVPIP WEKAKPVPRR TKVQKLVEVE VNDGNLRKSP TIFLVRQQSP RKYVTFPLVL 490 500 510 520 530 540 NNKVSAIVKR PKKLRSKKEK EEEEEVLVIE GIEFYMNIAI KFDVYINDED DKVGAGNTEF 550 560 570 580 590 600 AGSFVNIPHS AHGHKNKKII TSLRLGITDL LEDLHVEGDD NIVVTLVPKC GSGQVKINNV EIVFED

References

[1]	"Cloning and characterization of cDNAs coding for Vicia faba polyphenol oxidase." Cary J.W., Lax A.R., Flurkey W.H. Plant Mol. Biol. 20:245-253(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Leaf.
[2]	"Polypeptide composition and amino-terminal sequence of broad bean polyphenol oxidase." Flurkey W.H. Plant Physiol. 91:481-483(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PRELIMINARY PROTEIN SEQUENCE OF 93-119. Tissue: Leaf.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z11702 mRNA. Translation: CAA77764.1.
PIR	S24758.
3D structure databases
ProteinModelPortal	Q06215.
SMR	Q06215. Positions 93-431.
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

PPO_VICFA

Accession

Primary (citable) accession number: Q06215

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	April 3, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program