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Q9ZP19

- PPO1_IPOBA

UniProt

Q9ZP19 - PPO1_IPOBA

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Protein

Polyphenol oxidase I, chloroplastic

Gene

co-1

Organism
Ipomoea batatas (Sweet potato) (Convolvulus batatas)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of mono- and o-diphenols to o-diquinones.

Catalytic activityi

2 catechol + O2 = 2 1,2-benzoquinone + 2 H2O.

Cofactori

Cu2+Note: Binds 2 copper ions per subunit.

Enzyme regulationi

Inhibited by phenylthiourea.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi88 – 881Copper A1 Publication
Metal bindingi109 – 1091Copper A1 Publication
Metal bindingi118 – 1181Copper A1 Publication
Metal bindingi240 – 2401Copper B1 Publication
Metal bindingi244 – 2441Copper B1 Publication
Metal bindingi274 – 2741Copper B1 Publication

GO - Molecular functioni

  1. catechol oxidase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Polyphenol oxidase I, chloroplastic (EC:1.10.3.1)
Short name:
PPO-I
Alternative name(s):
Catechol oxidase I
Gene namesi
Name:co-1
OrganismiIpomoea batatas (Sweet potato) (Convolvulus batatas)
Taxonomic identifieri4120 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesConvolvulaceaeIpomoeeaeIpomoea

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-KW
  2. thylakoid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 496496Polyphenol oxidase I, chloroplasticPRO_0000186741Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi11 ↔ 281 Publication
Disulfide bondi27 ↔ 891 Publication
Cross-linki92 ↔ 1092'-(S-cysteinyl)-histidine (Cys-His)

Keywords - PTMi

Disulfide bond, Thioether bond

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
496
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 103Combined sources
Beta strandi33 – 375Combined sources
Beta strandi47 – 493Combined sources
Helixi52 – 543Combined sources
Helixi57 – 7115Combined sources
Helixi81 – 9212Combined sources
Beta strandi96 – 983Combined sources
Beta strandi101 – 1055Combined sources
Beta strandi109 – 1113Combined sources
Helixi114 – 13320Combined sources
Helixi148 – 1503Combined sources
Helixi155 – 1584Combined sources
Beta strandi167 – 1693Combined sources
Helixi171 – 1733Combined sources
Helixi192 – 20716Combined sources
Turni208 – 2103Combined sources
Helixi214 – 2185Combined sources
Helixi234 – 2374Combined sources
Helixi240 – 2478Combined sources
Turni256 – 2594Combined sources
Turni261 – 2633Combined sources
Helixi264 – 2663Combined sources
Helixi269 – 28719Combined sources
Helixi299 – 3024Combined sources
Beta strandi305 – 3095Combined sources
Beta strandi315 – 3195Combined sources
Helixi320 – 3223Combined sources
Helixi326 – 3294Combined sources
Beta strandi331 – 3333Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BT1X-ray2.70A/B1-345[»]
1BT2X-ray2.70A/B1-345[»]
1BT3X-ray2.50A1-345[»]
1BUGX-ray2.70A/B1-345[»]
ProteinModelPortaliQ9ZP19.
SMRiQ9ZP19. Positions 1-341.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ZP19.

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.Curated

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
InterProiIPR022740. Polyphenol_oxidase_C.
IPR022739. Polyphenol_oxidase_cen.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamiPF12142. PPO1_DWL. 1 hit.
PF12143. PPO1_KFDV. 1 hit.
PF00264. Tyrosinase. 1 hit.
[Graphical view]
PRINTSiPR00092. TYROSINASE.
SUPFAMiSSF48056. SSF48056. 1 hit.
PROSITEiPS00497. TYROSINASE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ZP19-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
APIQAPEISK CVVPPADLPP GAVVDNCCPP VASNIVDYKL PAVTTMKVRP
60 70 80 90 100
AAHTMDKDAI AKFAKAVELM KALPADDPRN FYQQALVHCA YCNGGYDQVN
110 120 130 140 150
FPDQEIQVHN SWLFFPFHRW YLYFYERILG KLIGDPSFGL PFWNWDNPGG
160 170 180 190 200
MVLPDFLNDS TSSLYDSNRN QSHLPPVVVD LGYNGADTDV TDQQRITDNL
210 220 230 240 250
ALMYKQMVTN AGTAELFLGK AYRAGDAPSP GAGSIETSPH IPIHRWVGDP
260 270 280 290 300
RNTNNEDMGN FYSAGRDIAF YCHHSNVDRM WTIWQQLAGK PRKRDYTDSD
310 320 330 340 350
WLNATFLFYD ENGQAVKVRI GDSLDNQKMG YKYAKTPLPW LDSKPVPTKK
360 370 380 390 400
KGGYASKSKA PFVASVFPVT LDKVVQVKVA RPKKSRSAEE KEAEEEILLI
410 420 430 440 450
VGIEVEIDKY AKFDVYLNDS DDPSGGKDKA EYAGSFAHLP HKHKGMKKIR
460 470 480 490
TTLSLGLNEP LEDLGAEDDD TILVTLAPKV GGGVVSVDNV KVVYGS
Length:496
Mass (Da):55,011
Last modified:May 1, 1999 - v1
Checksum:i806717DBF5B09705
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 423LPA → IPV in CAC83609. 1 PublicationCurated
Sequence conflicti65 – 651K → R in CAC83609. 1 PublicationCurated
Sequence conflicti68 – 681E → D in CAC83609. 1 PublicationCurated
Sequence conflicti71 – 711K → R in CAC83609. 1 PublicationCurated
Sequence conflicti75 – 751A → G in CAC83609. 1 PublicationCurated
Sequence conflicti282 – 2821T → A in CAC83609. 1 PublicationCurated
Sequence conflicti401 – 4033VGI → EGV in CAC83609. 1 PublicationCurated
Sequence conflicti436 – 4361F → S in CAC83609. 1 PublicationCurated
Sequence conflicti475 – 4751T → A in CAC83609. 1 PublicationCurated
Sequence conflicti490 – 4901V → I in CAC83609. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ006097 mRNA. Translation: CAA06855.1.
AJ309175 Genomic DNA. Translation: CAC83609.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ006097 mRNA. Translation: CAA06855.1 .
AJ309175 Genomic DNA. Translation: CAC83609.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali Q9ZP19.
SMRi Q9ZP19. Positions 1-341.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q9ZP19.

Family and domain databases

Gene3Di 1.10.1280.10. 1 hit.
InterProi IPR022740. Polyphenol_oxidase_C.
IPR022739. Polyphenol_oxidase_cen.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view ]
Pfami PF12142. PPO1_DWL. 1 hit.
PF12143. PPO1_KFDV. 1 hit.
PF00264. Tyrosinase. 1 hit.
[Graphical view ]
PRINTSi PR00092. TYROSINASE.
SUPFAMi SSF48056. SSF48056. 1 hit.
PROSITEi PS00497. TYROSINASE_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-345 IN COMPLEX WITH COPPER AND N-PHENYLTHIOUREA, DISULFIDE BONDS.

Entry informationi

Entry nameiPPO1_IPOBA
AccessioniPrimary (citable) accession number: Q9ZP19
Secondary accession number(s): Q84V53
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: May 1, 1999
Last modified: November 26, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3