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Q9ZP19 (PPO1_IPOBA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
OrganismIpomoea batatas (Sweet potato) (Convolvulus batatas)
Taxonomic identifier4120 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Convolvulaceae › Ipomoeeae › Ipomoea

Protein attributes

Sequence length496 AA.
Sequence statusComplete.
Protein existenceEvidence 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 componentChloroplast
Plastid
Thylakoid
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMDisulfide bond
Thioether bond
   Technical term3D-structure
Gene Ontology (GO)
   Cellular_componentchloroplast thylakoid lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncatechol oxidase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 496496Polyphenol oxidase I, chloroplastic
PRO_0000186741

Sites

Metal binding881Copper A
Metal binding1091Copper A
Metal binding1181Copper A
Metal binding2401Copper B
Metal binding2441Copper B
Metal binding2741Copper B

Amino acid modifications

Disulfide bond11 ↔ 28 Ref.3
Disulfide bond27 ↔ 89 Ref.3
Cross-link92 ↔ 1092'-(S-cysteinyl)-histidine (Cys-His)

Experimental info

Sequence conflict40 – 423LPA → IPV in CAC83609. Ref.2
Sequence conflict651K → R in CAC83609. Ref.2
Sequence conflict681E → D in CAC83609. Ref.2
Sequence conflict711K → R in CAC83609. Ref.2
Sequence conflict751A → G in CAC83609. Ref.2
Sequence conflict2821T → A in CAC83609. Ref.2
Sequence conflict401 – 4033VGI → EGV in CAC83609. Ref.2
Sequence conflict4361F → S in CAC83609. Ref.2
Sequence conflict4751T → A in CAC83609. Ref.2
Sequence conflict4901V → I in CAC83609. Ref.2

Secondary structure

1 ........................................................ 496
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9ZP19 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 806717DBF5B09705

FASTA49655,011
        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

« Hide

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ006097 mRNA. Translation: CAA06855.1.
AJ309175 Genomic DNA. Translation: CAC83609.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BT1X-ray2.70A/B1-345[»]
1BT2X-ray2.70A/B1-345[»]
1BT3X-ray2.50A1-345[»]
1BUGX-ray2.70A/B1-345[»]
ProteinModelPortalQ9ZP19.
SMRQ9ZP19. Positions 1-341.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.1280.10. 1 hit.
InterProIPR022740. Polyphenol_oxidase_C.
IPR022739. Polyphenol_oxidase_cen.
IPR002227. Tyrosinase.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamPF12142. PPO1_DWL. 1 hit.
PF12143. PPO1_KFDV. 1 hit.
PF00264. Tyrosinase. 1 hit.
[Graphical view]
PRINTSPR00092. TYROSINASE.
SUPFAMSSF48056. Di-copper_centre. 1 hit.
PROSITEPS00497. TYROSINASE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9ZP19.

Entry information

Entry namePPO1_IPOBA
AccessionPrimary (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: March 6, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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