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Protein

Polyphenol oxidase II, chloroplastic

Gene

co-2

Organism
Ipomoea batatas (Sweet potato) (Convolvulus batatas)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

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

Cofactori

Cu2+By similarityNote: Binds 2 copper ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi178Copper ABy similarity1
Metal bindingi199Copper ABy similarity1
Metal bindingi208Copper ABy similarity1
Metal bindingi330Copper BBy similarity1
Metal bindingi334Copper BBy similarity1
Metal bindingi366Copper BBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Polyphenol oxidase II, chloroplastic (EC:1.10.3.1)
Short name:
PPO-II
Alternative name(s):
Catechol oxidase II
Gene namesi
Name:co-2
Synonyms:ppo-I
OrganismiIpomoea batatas (Sweet potato) (Convolvulus batatas)
Taxonomic identifieri4120 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesConvolvulaceaeIpomoeeaeIpomoea

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 50ChloroplastSequence analysisAdd BLAST50
Transit peptidei51 – 88ThylakoidBy similarityAdd BLAST38
ChainiPRO_000003590989 – 588Polyphenol oxidase II, chloroplasticAdd BLAST500

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi99 ↔ 116By similarity
Disulfide bondi115 ↔ 179By similarity
Cross-linki182 ↔ 1992'-(S-cysteinyl)-histidine (Cys-His)By similarity

Keywords - PTMi

Disulfide bond, Thioether bond

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9MB14.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.Curated

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
InterProiIPR016213. Polyphenol_oxidase.
IPR022740. 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]
PIRSFiPIRSF000290. PPO_plant. 1 hit.
PRINTSiPR00092. TYROSINASE.
SUPFAMiSSF48056. SSF48056. 1 hit.
PROSITEiPS00497. TYROSINASE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9MB14-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASFTTSPCT SAAPKTPKSL SSSATISSPL PKPSQIHIAT AKRTHHFKVS
60 70 80 90 100
CNAPNGDSQP KLDRRDVLLG LGGLAGAASL INNPLAFAEP IHAPEISKCV
110 120 130 140 150
VPPKDLPPDA IVDNCCPPLA TNVIPYKVPK TSPSAMKIRP AIHRMDKEYI
160 170 180 190 200
AKFEKAIRLM KELPADDPRN FYQQALVHCA YCNGGYVQTD YPDKEIQVHN
210 220 230 240 250
SWLFFPFHRW YLYFYERILG KLIGDPTFGL PFWNWDTPAG MLIPQYFRNQ
260 270 280 290 300
NSPLYDENRN QSHLPLVMDL GYAGTDTDVT DQERISNNLA LMYKSMVTNA
310 320 330 340 350
GTAELFLGKP YKAGDDPVNK GGGSIENIPH TPVHRWVGDV KPRTQNGEDM
360 370 380 390 400
GNFYSAGRDI LFYCHHSNVD RMWTIWQQLG GKGRRRDFTD SDWLDATFIF
410 420 430 440 450
YDENKQAVRV RVGDALDNQK LGYKYEFTNL PWLNSKPLPT KKKTGLAARS
460 470 480 490 500
KAPFVTDVFP LTLDKVVQVK VPRPKKSRSK EEKEAEEEIL EIQGIEVAID
510 520 530 540 550
QYAKFDVYLN DEDEPEAGKE KAEYAGSFAH LPHKHTGSKK IRTSLSLGLN
560 570 580
EPLEDLGAED DDAVLVTLAP KVGGGVVTVE NIKIVYGS
Length:588
Mass (Da):65,651
Last modified:March 29, 2005 - v2
Checksum:iF0DF1A03FDC33AC2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti130K → R in CAC29040 (Ref. 2) Curated1
Sequence conflicti277T → N in CAC29040 (Ref. 2) Curated1
Sequence conflicti493Q → E in BAA92317 (Ref. 1) Curated1
Sequence conflicti563A → P in CAC83610 (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB038994 mRNA. Translation: BAA92317.1.
AJ245880 mRNA. Translation: CAC29040.1.
AJ309176 Genomic DNA. Translation: CAC83610.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB038994 mRNA. Translation: BAA92317.1.
AJ245880 mRNA. Translation: CAC29040.1.
AJ309176 Genomic DNA. Translation: CAC83610.1.

3D structure databases

ProteinModelPortaliQ9MB14.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
InterProiIPR016213. Polyphenol_oxidase.
IPR022740. 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]
PIRSFiPIRSF000290. PPO_plant. 1 hit.
PRINTSiPR00092. TYROSINASE.
SUPFAMiSSF48056. SSF48056. 1 hit.
PROSITEiPS00497. TYROSINASE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPPO2_IPOBA
AccessioniPrimary (citable) accession number: Q9MB14
Secondary accession number(s): Q84V52, Q9ARD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: October 5, 2016
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.