Reviewed, UniProtKB/Swiss-Prot Q9ZP19 (PPO1_IPOBA)

Names and origin

Protein names

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

Gene names

Name:

co-1

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	496 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Enzyme regulation	Inhibited by phenylthiourea.
Subunit structure	Monomer.
Subcellular location	Plastid › chloroplast thylakoid lumen By similarity.
Sequence similarities	Belongs to the tyrosinase family.

Ontologies

Keywords
Cellular component	Chloroplast Plastid Thylakoid
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond Thioether bond
Technical term	3D-structure
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

Chain

1 – 496

496

Polyphenol oxidase I, chloroplastic

PRO_0000186741

Sites

Metal binding

88

1

Copper A

Metal binding

109

1

Copper A

Metal binding

118

1

Copper A

Metal binding

240

1

Copper B

Metal binding

244

1

Copper B

Metal binding

274

1

Copper B

Amino acid modifications

Disulfide bond

11 ↔ 28

Disulfide bond

27 ↔ 89

Cross-link

92 ↔ 109

2'-(S-cysteinyl)-histidine (Cys-His)

Experimental info

Sequence conflict

40 – 42

3

LPA → IPV in CAC83609. Ref.2

Sequence conflict

65

1

K → R in CAC83609. Ref.2

Sequence conflict

68

1

E → D in CAC83609. Ref.2

Sequence conflict

71

1

K → R in CAC83609. Ref.2

Sequence conflict

75

1

A → G in CAC83609. Ref.2

Sequence conflict

282

1

T → A in CAC83609. Ref.2

Sequence conflict

401 – 403

3

VGI → EGV in CAC83609. Ref.2

Sequence conflict

436

1

F → S in CAC83609. Ref.2

Sequence conflict

475

1

T → A in CAC83609. Ref.2

Sequence conflict

490

1

V → I in CAC83609. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

496

Helix Strand Turn

Details...

Helix

8 – 10

3

Beta strand

33 – 37

5

Beta strand

47 – 49

3

Helix

52 – 54

3

Helix

57 – 71

15

Helix

81 – 92

12

Beta strand

109 – 111

3

Helix

114 – 132

19

Helix

148 – 150

3

Helix

155 – 158

4

Helix

192 – 207

16

Helix

209 – 211

3

Helix

214 – 218

5

Helix

234 – 237

4

Helix

240 – 247

8

Turn

256 – 259

4

Turn

261 – 263

3

Helix

264 – 266

3

Helix

268 – 285

18

Helix

299 – 302

4

Beta strand

305 – 309

5

Beta strand

315 – 319

5

Helix

320 – 323

4

Helix

327 – 329

3

Beta strand

331 – 333

3

Sequences

	Sequence		Length	Mass (Da)
	Q9ZP19-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 806717DBF5B09705	FASTA	496	55,011
	10 20 30 40 50 60 APIQAPEISK CVVPPADLPP GAVVDNCCPP VASNIVDYKL PAVTTMKVRP AAHTMDKDAI 70 80 90 100 110 120 AKFAKAVELM KALPADDPRN FYQQALVHCA YCNGGYDQVN FPDQEIQVHN SWLFFPFHRW 130 140 150 160 170 180 YLYFYERILG KLIGDPSFGL PFWNWDNPGG MVLPDFLNDS TSSLYDSNRN QSHLPPVVVD 190 200 210 220 230 240 LGYNGADTDV TDQQRITDNL ALMYKQMVTN AGTAELFLGK AYRAGDAPSP GAGSIETSPH 250 260 270 280 290 300 IPIHRWVGDP RNTNNEDMGN FYSAGRDIAF YCHHSNVDRM WTIWQQLAGK PRKRDYTDSD 310 320 330 340 350 360 WLNATFLFYD ENGQAVKVRI GDSLDNQKMG YKYAKTPLPW LDSKPVPTKK KGGYASKSKA 370 380 390 400 410 420 PFVASVFPVT LDKVVQVKVA RPKKSRSAEE KEAEEEILLI VGIEVEIDKY AKFDVYLNDS 430 440 450 460 470 480 DDPSGGKDKA EYAGSFAHLP HKHKGMKKIR TTLSLGLNEP LEDLGAEDDD TILVTLAPKV 490 GGGVVSVDNV KVVYGS

References

[1]	"Cloning and characterization of cDNA coding for Ipomoea batatas catechol oxidase." Gerdemann C., Eicken C., Meyer H., Spener F., Krebs B. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Root.
[2]	"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]. Strain: cv. Bushbuck.
[3]	"Crystal structure of a plant catechol oxidase containing a dicopper center." Klabunde T., Eicken C., Sacchettini J.C., Krebs B. Nat. Struct. Biol. 5:1084-1090(1998) [PubMed: 9846879] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-345.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AJ006097 mRNA. Translation: CAA06855.1.
AJ309175 Genomic DNA. Translation: CAC83609.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BT1	X-ray	2.70	A/B	1-345	[»]
1BT2	X-ray	2.70	A/B	1-345	[»]
1BT3	X-ray	2.50	A	1-345	[»]
1BUG	X-ray	2.70	A/B	1-345	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.10.3.1. 21210.

Family and domain databases

InterPro

IPR008922. Di-copper_centre.
IPR002227. Tyrosinase.
[Graphical view]

Gene3D

G3DSA:1.10.1280.10. Di-copper_centre. 1 hit.

Pfam

PF00264. Tyrosinase. 1 hit.
[Graphical view]

PRINTS

PR00092. TYROSINASE.

PROSITE

PS00497. TYROSINASE_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PPO1_IPOBA

Accession

Primary (citable) accession number: Q9ZP19
Secondary accession number(s): Q84V53

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	May 1, 1999
Last modified:	June 16, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)