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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

Binds 2 copper ions per subunit.

Enzyme regulationi

Inhibited by phenylthiourea.

Sites

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

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 thylakoid lumen Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 496496Polyphenol oxidase I, chloroplastic
PRO_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.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiQ9ZP19.

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.

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

APIQAPEISK CVVPPADLPP GAVVDNCCPP VASNIVDYKL PAVTTMKVRP    50
AAHTMDKDAI AKFAKAVELM KALPADDPRN FYQQALVHCA YCNGGYDQVN 100
FPDQEIQVHN SWLFFPFHRW YLYFYERILG KLIGDPSFGL PFWNWDNPGG 150
MVLPDFLNDS TSSLYDSNRN QSHLPPVVVD LGYNGADTDV TDQQRITDNL 200
ALMYKQMVTN AGTAELFLGK AYRAGDAPSP GAGSIETSPH IPIHRWVGDP 250
RNTNNEDMGN FYSAGRDIAF YCHHSNVDRM WTIWQQLAGK PRKRDYTDSD 300
WLNATFLFYD ENGQAVKVRI GDSLDNQKMG YKYAKTPLPW LDSKPVPTKK 350
KGGYASKSKA PFVASVFPVT LDKVVQVKVA RPKKSRSAEE KEAEEEILLI 400
VGIEVEIDKY AKFDVYLNDS DDPSGGKDKA EYAGSFAHLP HKHKGMKKIR 450
TTLSLGLNEP LEDLGAEDDD TILVTLAPKV GGGVVSVDNV KVVYGS 496
Length:496
Mass (Da):55,011
Last modified:May 1, 1999 - v1
Checksum:i806717DBF5B09705
GO

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ006097 mRNA. Translation: CAA06855.1.
AJ309175 Genomic DNA. Translation: CAC83609.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ006097 mRNA. Translation: CAA06855.1 .
AJ309175 Genomic DNA. Translation: CAC83609.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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: June 11, 2014
This is version 62 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

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