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UniProtKB/Swiss-Prot entry Q9ZP19

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PPO1_IPOBA
Primary accession number Q9ZP19
Secondary accession number Q84V53
Integrated into Swiss-Prot on March 29, 2005
Sequence was last modified on May 1, 1999 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 40)
Name and origin of the protein
Protein name Polyphenol oxidase I, chloroplastic
Synonyms PPO-I
EC 1.10.3.1
Catechol oxidase I
Gene name
Name: co-1
From
Ipomoea batatas (Sweet potato) (Batate) [TaxID: 4120] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Root;
Gerdemann C., Eicken C., Meyer H., Spener F., Krebs B.;
"Cloning and characterization of cDNA coding for Ipomoea batatas catechol oxidase.";
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Bushbuck;
Greving J., Gerdemann C., Spener F., Krebs B.;
"Sequencing and cloning of genomic DNA encoding two isozymes of Ipomoea batatas catechol oxidase.";
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
[3]
 X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-345.
DOI=10.1038/4193; PubMed=9846879 [NCBI, ExPASy, EBI, Israel, Japan]
Klabunde T., Eicken C., Sacchettini J.C., Krebs B.;
"Crystal structure of a plant catechol oxidase containing a dicopper center.";
Nat. Struct. Biol. 5:1084-1090(1998).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ006097; CAA06855.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ309175; CAC83609.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
PDB
1BT1; X-ray; 2.70 A; A/B=1-345.[ExPASy / RCSB / EBI]
1BT2; X-ray; 2.70 A; A/B=1-345.[ExPASy / RCSB / EBI]
1BT3; X-ray; 2.50 A; A=1-345.[ExPASy / RCSB / EBI]
1BUG; X-ray; 2.70 A; A/B=1-345.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1BT1; -.
1BT2; -.
1BT3; -.
1BUG; -.
ModBase Q9ZP19.
Ontologies
GO
GO:0009507; Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0009579; Cellular component: thylakoid (inferred from electronic annotation from UniProtKB-KW).
GO:0004097; Molecular function: catechol oxidase activity (inferred from electronic annotation from EC).
GO:0005507; Molecular function: copper ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR008922; Di-copper_centre.
IPR002227; Tyrosinase.
Graphical view of domain structure.
Gene3D G3DSA:1.10.1280.10; Di-copper_centre; 1.
Pfam PF00264; Tyrosinase; 1.
Pfam graphical view of domain structure.
PRINTS PR00092; TYROSINASE.
PROSITE PS00497; TYROSINASE_1; 1.
BLOCKS Q9ZP19.
ProtoNet Q9ZP19.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Chloroplast; Copper; Metal-binding; Oxidoreductase; Plastid; Thioether bond; Thylakoid.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   496  496     Polyphenol oxidase I, chloroplastic. PRO_0000186741
METAL   88    88        Copper A. 
METAL   109   109        Copper A. 
METAL   118   118        Copper A. 
METAL   240   240        Copper B. 
METAL   244   244        Copper B. 
METAL   274   274        Copper B. 
DISULFID   11    28         
DISULFID   27    89         
CROSSLNK   92   109        2'-(S-cysteinyl)-histidine (Cys-His). 
CONFLICT   40    42        LPA -> IPV (in Ref. 2; CAC83609). 
CONFLICT   65    65        K -> R (in Ref. 2; CAC83609). 
CONFLICT   68    68        E -> D (in Ref. 2; CAC83609). 
CONFLICT   71    71        K -> R (in Ref. 2; CAC83609). 
CONFLICT   75    75        A -> G (in Ref. 2; CAC83609). 
CONFLICT   282   282        T -> A (in Ref. 2; CAC83609). 
CONFLICT   401   403        VGI -> EGV (in Ref. 2; CAC83609). 
CONFLICT   436   436        F -> S (in Ref. 2; CAC83609). 
CONFLICT   475   475        T -> A (in Ref. 2; CAC83609). 
CONFLICT   490   490        V -> I (in Ref. 2; CAC83609). 
HELIX   8    10  3      
STRAND   33    37  5      
STRAND   47    49  3      
HELIX   52    54  3      
HELIX   57    71  15      
HELIX   81    92  12      
STRAND   109   111  3      
HELIX   114   132  19      
HELIX   148   150  3      
HELIX   155   158  4      
HELIX   192   207  16      
HELIX   209   211  3      
HELIX   214   218  5      
HELIX   234   237  4      
HELIX   240   247  8      
TURN   256   259  4      
TURN   261   263  3      
HELIX   264   266  3      
HELIX   268   285  18      
HELIX   299   302  4      
STRAND   305   309  5      
STRAND   315   319  5      
HELIX   320   323  4      
HELIX   327   329  3      
STRAND   331   333  3      
Sequence information
Length: 496 AA [This is the length of the unprocessed precursor] Molecular weight: 55011 Da [This is the MW of the unprocessed precursor] CRC64: 806717DBF5B09705 [This is a checksum on the sequence] 
        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
Q9ZP19 in FASTA format

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