P43310 (PPO_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Polyphenol oxidase, chloroplastic Short name=PPO EC=1.10.3.1 Alternative name(s): Catechol oxidase
Organism	Spinacia oleracea (Spinach)
Taxonomic identifier	3562 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Spinacia

Protein attributes

Sequence length	639 AA.
Sequence status	Complete.
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
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 – 101	101	Chloroplast Potential
	Chain	102 – 639	538	Polyphenol oxidase, chloroplastic		PRO_0000035918
Sites
	Metal binding	193	1	Copper A By similarity
	Metal binding	214	1	Copper A By similarity
	Metal binding	223	1	Copper A By similarity
	Metal binding	354	1	Copper B By similarity
	Metal binding	358	1	Copper B By similarity
	Metal binding	388	1	Copper B By similarity
Amino acid modifications
	Disulfide bond	111 ↔ 127		By similarity
	Disulfide bond	126 ↔ 194		By similarity
	Cross-link	197 ↔ 214		2'-(S-cysteinyl)-histidine (Cys-His) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P43310 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 56917BBF12F5162A	FASTA	639	73,237
	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

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
ProteinModelPortal	P43310.
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_SPIOL

Accession

Primary (citable) accession number: P43310

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	April 3, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program