Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9MB14

- PPO2_IPOBA

UniProt

Q9MB14 - PPO2_IPOBA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Polyphenol oxidase II, chloroplastic

Gene

co-2

Organism
Ipomoea batatas (Sweet potato) (Convolvulus batatas)
Status
Reviewed - 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

Binds 2 copper ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi178 – 1781Copper ABy similarity
Metal bindingi199 – 1991Copper ABy similarity
Metal bindingi208 – 2081Copper ABy similarity
Metal bindingi330 – 3301Copper BBy similarity
Metal bindingi334 – 3341Copper BBy similarity
Metal bindingi366 – 3661Copper BBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. pigment biosynthetic process Source: InterPro
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

  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
Transit peptidei1 – 5050ChloroplastSequence AnalysisAdd
BLAST
Transit peptidei51 – 8838ThylakoidBy similarityAdd
BLAST
Chaini89 – 588500Polyphenol oxidase II, chloroplasticPRO_0000035909Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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.
SMRiQ9MB14. Positions 90-433.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti130 – 1301K → R in CAC29040. 1 PublicationCurated
Sequence conflicti277 – 2771T → N in CAC29040. 1 PublicationCurated
Sequence conflicti493 – 4931Q → E in BAA92317. 1 PublicationCurated
Sequence conflicti563 – 5631A → P in CAC83610. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AB038994 mRNA. Translation: BAA92317.1 .
AJ245880 mRNA. Translation: CAC29040.1 .
AJ309176 Genomic DNA. Translation: CAC83610.1 .

3D structure databases

ProteinModelPortali Q9MB14.
SMRi Q9MB14. Positions 90-433.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 1.10.1280.10. 1 hit.
InterProi IPR016213. Polyphenol_oxidase.
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 ]
PIRSFi PIRSF000290. PPO_plant. 1 hit.
PRINTSi PR00092. TYROSINASE.
SUPFAMi SSF48056. SSF48056. 1 hit.
PROSITEi PS00497. TYROSINASE_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Ipomoea batatas polyphenol oxidase I mRNA."
    Hashimoto H., Nozue M., Tanaka I.
    Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Sequence and structural implications of two isozymes of Ipomoea batatas catechol oxidase differing in catalase activity."
    Gerdemann C., Eicken C., Magrini A., Meier H.E., Spener F., Krebs B.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 89-588.
    Strain: cv. Bushbuck.
    Tissue: Root.
  3. "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] OF 89-588.
    Strain: cv. Bushbuck.

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 29, 2014
This is version 53 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

External Data

Dasty 3