[1]	NUCLEOTIDE SEQUENCE [MRNA]. Hashimoto H., Nozue M., Tanaka I.; "Ipomoea batatas polyphenol oxidase I mRNA."; Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 89-588. STRAIN=cv. Bushbuck; TISSUE=Root; Gerdemann C., Eicken C., Magrini A., Meier H.E., Spener F., Krebs B.; "Sequence and structural implications of two isozymes of Ipomoea batatas catechol oxidase differing in catalase activity."; Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 89-588. STRAIN=cv. Bushbuck; Greving J., Gerdemann C., Spener F., Krebs B.; "Sequencing and cloning of genomic DNA encoding two isozymes of Ipomoea batatas catechol oxidase."; Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Catalyzes the oxidation of mono- and o-diphenols to o-diquinones (By similarity).
CATALYTIC ACTIVITY: 2 catechol + O₂ = 2 1,2-benzoquinone + 2 H₂O.
COFACTOR: Binds 2 copper ions per subunit (By similarity).
SUBUNIT: Monomer (By similarity).
SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen (By similarity).
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

AB038994; BAA92317.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ245880; CAC29040.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ309176; CAC83610.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q9ZP19; 1BT3. [HSSP ENTRY / PDB]

SMR

Q9MB14; 90-433.

ModBase

Q9MB14.

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.

Other

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 50`	`50`	`Chloroplast (Potential).`
`TRANSIT`	`51 88`	`38`	`Thylakoid (By similarity).`
`CHAIN`	`89 588`	`500`	`Polyphenol oxidase II, chloroplastic.`	`PRO_0000035909`
`METAL`	`178 178`		`Copper A (By similarity).`
`METAL`	`199 199`		`Copper A (By similarity).`
`METAL`	`208 208`		`Copper A (By similarity).`
`METAL`	`330 330`		`Copper B (By similarity).`
`METAL`	`334 334`		`Copper B (By similarity).`
`METAL`	`366 366`		`Copper B (By similarity).`
`DISULFID`	`99 116`		`By similarity.`
`DISULFID`	`115 179`		`By similarity.`
`CROSSLNK`	`182 199`		`2'-(S-cysteinyl)-histidine (Cys-His) (By similarity).`
`CONFLICT`	`130 130`		`K -> R (in Ref. 2; CAC29040).`
`CONFLICT`	`277 277`		`T -> N (in Ref. 2; CAC29040).`
`CONFLICT`	`493 493`		`Q -> E (in Ref. 1; BAA92317).`
`CONFLICT`	`563 563`		`A -> P (in Ref. 3; CAC83610).`

Sequence information

Length: 588 AA [This is the length of the unprocessed precursor]

Molecular weight: 65651 Da [This is the MW of the unprocessed precursor]

CRC64: F0DF1A03FDC33AC2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASFTTSPCT SAAPKTPKSL SSSATISSPL PKPSQIHIAT AKRTHHFKVS CNAPNGDSQP 

        70         80         90        100        110        120 
KLDRRDVLLG LGGLAGAASL INNPLAFAEP IHAPEISKCV VPPKDLPPDA IVDNCCPPLA 

       130        140        150        160        170        180 
TNVIPYKVPK TSPSAMKIRP AIHRMDKEYI AKFEKAIRLM KELPADDPRN FYQQALVHCA 

       190        200        210        220        230        240 
YCNGGYVQTD YPDKEIQVHN SWLFFPFHRW YLYFYERILG KLIGDPTFGL PFWNWDTPAG 

       250        260        270        280        290        300 
MLIPQYFRNQ NSPLYDENRN QSHLPLVMDL GYAGTDTDVT DQERISNNLA LMYKSMVTNA 

       310        320        330        340        350        360 
GTAELFLGKP YKAGDDPVNK GGGSIENIPH TPVHRWVGDV KPRTQNGEDM GNFYSAGRDI 

       370        380        390        400        410        420 
LFYCHHSNVD RMWTIWQQLG GKGRRRDFTD SDWLDATFIF YDENKQAVRV RVGDALDNQK 

       430        440        450        460        470        480 
LGYKYEFTNL PWLNSKPLPT KKKTGLAARS KAPFVTDVFP LTLDKVVQVK VPRPKKSRSK 

       490        500        510        520        530        540 
EEKEAEEEIL EIQGIEVAID QYAKFDVYLN DEDEPEAGKE KAEYAGSFAH LPHKHTGSKK 

       550        560        570        580 
IRTSLSLGLN EPLEDLGAED DDAVLVTLAP KVGGGVVTVE NIKIVYGS

Q9MB14 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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