Reviewed, UniProtKB/Swiss-Prot Q9MB14 (PPO2_IPOBA)

Names and origin

Protein names

Recommended name:
    Polyphenol oxidase II, chloroplastic
      Short name=PPO-II
    EC=1.10.3.1
Alternative name(s):
    Catechol oxidase II

Gene names

Name:	co-2
Synonyms:	ppo-I

Organism

Ipomoea batatas (Sweet potato) (Batate)

Taxonomic identifier

4120 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Convolvulaceae › Ipomoeeae › Ipomoea

Protein attributes

Sequence length	588 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 By similarity.
Catalytic activity	2 catechol + O2 = 2 1,2-benzoquinone + 2 H2O.
Cofactor	Binds 2 copper ions per subunit By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Plastid › chloroplast thylakoid lumen By similarity.
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	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast thylakoid lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	catechol oxidase activity Inferred from electronic annotation. Source: EC copper 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 – 50	50	Chloroplast Potential
	Transit peptide	51 – 88	38	Thylakoid By similarity
	Chain	89 – 588	500	Polyphenol oxidase II, chloroplastic		PRO_0000035909
Sites
	Metal binding	178	1	Copper A By similarity
	Metal binding	199	1	Copper A By similarity
	Metal binding	208	1	Copper A By similarity
	Metal binding	330	1	Copper B By similarity
	Metal binding	334	1	Copper B By similarity
	Metal binding	366	1	Copper B By similarity
Amino acid modifications
	Disulfide bond	99 ↔ 116		By similarity
	Disulfide bond	115 ↔ 179		By similarity
	Cross-link	182 ↔ 199		2'-(S-cysteinyl)-histidine (Cys-His) By similarity
Experimental info
	Sequence conflict	130	1	K → R in CAC29040. Ref.2
	Sequence conflict	277	1	T → N in CAC29040. Ref.2
	Sequence conflict	493	1	Q → E in BAA92317. Ref.1
	Sequence conflict	563	1	A → P in CAC83610. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9MB14-1 [UniParc]. Last modified March 29, 2005. Version 2. Checksum: F0DF1A03FDC33AC2	FASTA	588	65,651
	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

References

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

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB038994 mRNA. Translation: BAA92317.1. AJ245880 mRNA. Translation: CAC29040.1. AJ309176 Genomic DNA. Translation: CAC83610.1.
3D structure databases
HSSP	HSSP built from PDB template 1BT3 based on UniProtKB Q9ZP19.
SMR	Q9MB14. Positions 90-433.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.10.3.1. 21210.
Family and domain databases
InterPro	IPR008922. Di-copper_centre. IPR016213. Polyphenol_Oxase_pln. IPR002227. Tyrosinase. [Graphical view]
Gene3D	G3DSA:1.10.1280.10. Di-copper_centre. 1 hit.
Pfam	PF00264. Tyrosinase. 1 hit. [Graphical view]
PIRSF	PIRSF000290. PPO_plant. 1 hit.
PRINTS	PR00092. TYROSINASE.
PROSITE	PS00497. TYROSINASE_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PPO2_IPOBA

Accession

Primary (citable) accession number: Q9MB14
Secondary accession number(s): Q84V52, Q9ARD3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	March 29, 2005
Last modified:	June 16, 2009
This is version 34 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)