[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=cv. VFNT Cherry; DOI=10.1007/BF00023601; PubMed=8098228 [NCBI, ExPASy, EBI, Israel, Japan] Newman S.M., Eannetta N.T., Yu H., Prince J.P., de Vicente M.C., Tanksley S.D., Steffens J.C.; "Organisation of the tomato polyphenol oxidase gene family."; Plant Mol. Biol. 21:1035-1051(1993).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=cv. Tiny tim; DOI=10.1105/tpc.4.2.135; PubMed=1633491 [NCBI, ExPASy, EBI, Israel, Japan] Shahar T., Hennig N., Gutfinger T., Hareven D., Lifschitz E.; "The tomato 66.3-kD polyphenoloxidase gene: molecular identification and developmental expression."; Plant Cell 4:135-147(1992).

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.
SIMILARITY: Belongs to the tyrosinase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Z12837; CAA78299.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S40548; AAB22610.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S33543; S33543.

3D structure databases

ModBase

Q08307.

Ontologies

GO:0004097;	Molecular function: catechol oxidase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR008922; Di-copper_centre.
IPR016213; Polyphenol_Oxase_pln.
IPR002227; Tyrosinase.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.1280.10; Di-copper_centre; 1.

Pfam

PF00264; Tyrosinase; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000290; PPO_plant; 1.

PRINTS

PR00092; TYROSINASE.

PROSITE

PS00497; TYROSINASE_1; 1.
PS00498; TYROSINASE_2; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Chloroplast; Copper; Metal-binding; Oxidoreductase; Plastid; Thioether bond; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 87`	`87`	`Chloroplast.`
`CHAIN`	`88 587`	`500`	`Polyphenol oxidase E, chloroplastic.`	`PRO_0000035914`
`METAL`	`179 179`		`Copper A (By similarity).`
`METAL`	`197 197`		`Copper A (By similarity).`
`METAL`	`206 206`		`Copper A (By similarity).`
`METAL`	`328 328`		`Copper B (By similarity).`
`METAL`	`332 332`		`Copper B (By similarity).`
`METAL`	`363 363`		`Copper B (By similarity).`
`DISULFID`	`98 114`		`By similarity.`
`DISULFID`	`113 180`		`By similarity.`
`CROSSLNK`	`183 197`		`2'-(S-cysteinyl)-histidine (Cys-His) (By similarity).`
`CONFLICT`	`311 315`		`PLGSE -> LWVLN (in Ref. 2; AAB22610).`
`CONFLICT`	`410 410`		`C -> V (in Ref. 2; AAB22610).`
`CONFLICT`	`541 541`		`L -> V (in Ref. 2; AAB22610).`
`CONFLICT`	`567 567`		`V -> I (in Ref. 2; AAB22610).`
`CONFLICT`	`574 574`		`E -> G (in Ref. 2; AAB22610).`

Sequence information

Length: 587 AA [This is the length of the unprocessed precursor]

Molecular weight: 66237 Da [This is the MW of the unprocessed precursor]

CRC64: A796AA1DD6454E3D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSSSSSITTT LPLCTNKSLS SSFTTTNSSL LSKPSQLFLH GRRNQSFKVS CNANNVDKNP 

        70         80         90        100        110        120 
DAVDRRNVLL GLGGLYGAAN LAPLATAAPI PPPDLKSCGT AHVKEGVDVI YSCCPPVPDD 

       130        140        150        160        170        180 
IDSVPYYKFP SMTKLRIRPP AHAADEEYVA KYQLATSRMR ELDKDPFDPL GFKQQANIHC 

       190        200        210        220        230        240 
AYCNGAYKVG GKELQVHFSW LFFPFHRWYL YFYERILGSL INDPTFALPY WNWDHPKGMR 

       250        260        270        280        290        300 
IPPMFDREGS SLYDEKRNQN HRNGTIIDLG HFGKEVDTPQ LQIMTNNLTL MYRQMVTNAP 

       310        320        330        340        350        360 
CPSQFFGAAY PLGSEPSPGQ GTIENIPHTP VHIWTGDKPR QKNGEDMGNF YSAGLDPIFY 

       370        380        390        400        410        420 
CHHANVDRMW NEWKLIGGKR RDLTDKDWLN SEFFFYDENR NPYRVKVRDC LDSKKMGFDY 

       430        440        450        460        470        480 
APMPTPWRNF KPIRKSSSGK VNTASIAPVS KVFPLAKLDR AISFSITRPA SSRTTQEKNE 

       490        500        510        520        530        540 
QEEILTFNKI SYDDRNYVRF DVFLNVDKTV NADELDKAEF AGSYTSLPHV HGSNTNHVTS 

       550        560        570        580 
LTFKLAITEL LEDIGLEDED TIAVTLVPKA GGEEVSIESV EIKLEDC

Q08307 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools