Reviewed, UniProtKB/Swiss-Prot Q00024 (PPO1_AGABI)

Names and origin

Protein names

Recommended name:
    Polyphenol oxidase
      Short name=PPO
    EC=1.10.3.1
Alternative name(s):
    Catechol oxidase

Gene names

Name:

ppo1

Organism

Agaricus bisporus (Common mushroom)

Taxonomic identifier

5341 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Agaricomycetidae › Agaricales › Agaricaceae › Agaricus

Protein attributes

Sequence length	568 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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 By similarity.
Sequence similarities	Belongs to the tyrosinase family.

Ontologies

Keywords
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Thioether bond
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	catechol oxidase activity Inferred from electronic annotation. Source: EC copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 568	568	Polyphenol oxidase		PRO_0000186740
Sites
	Metal binding	57	1	Copper A By similarity
	Metal binding	85	1	Copper A By similarity
	Metal binding	94	1	Copper A By similarity
	Metal binding	257	1	Copper B By similarity
	Metal binding	261	1	Copper B By similarity
	Metal binding	286	1	Copper B By similarity
Amino acid modifications
	Cross-link	83 ↔ 85		2'-(S-cysteinyl)-histidine (Cys-His) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q00024-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: F5CBADB73533685A	FASTA	568	63,898
	10 20 30 40 50 60 MSHLLVSPLG GGVQPRLEIN NFVKNDRQFS LYVQALDRMY ATPQNETASY FQVAGVHGYP 70 80 90 100 110 120 LIPFDDAVGP TEFSPFDQWT GYCTHGSTLF PTWHRPYVLI LEQILSGHAQ QIADTYTVNK 130 140 150 160 170 180 SEWKKAATEF RHPYWDWASN SVPPPEVISL PKVTITTPNG QKTSVANPLM RYTFNSVNDG 190 200 210 220 230 240 GFYGPYNQWD TTLRQPDSTG VNAKDNVNRL KSVLKNAQAS LTRATYDMFN RVTTWPHFSS 250 260 270 280 290 300 HTPASGGSTS NSIEAIHDNI HVLVGGNGHM SDPSVAPFDP IFFLHHANVD RLIALWSAIR 310 320 330 340 350 360 YDVWTSPGDA QFGTYTLRYK QSVDESTDLA PWWKTQNEYW KSNELRSTES LGYTYPEFVG 370 380 390 400 410 420 LDMYNKDAVN KTISRKVAQL YGPQRGGQRS LVEDLSNSHA RRSQRPAKRS RLGQLLKGLF 430 440 450 460 470 480 SDWSAQIKFN RHEVGQSFSV CLFLGNVPED PREWLVSPNL VGARHAFVRS VKTDHVAEEI 490 500 510 520 530 540 GFIPINQWIA EHTGLPSFAV DLVKPLLAQG LQWRVLLADG TPAELDSLEV TILEVPSELT 550 560 DDEPNPRSRP PRYHKDITHG KRGGCREA

References

[1]

"Cloning, expression and characterisation of two tyrosinase cDNAs from Agaricus bisporus." Wichers H., Recourt K., Hendriks M., Ebbelaar C.E.M., Biancone G., Hoeberichts F., Mooibroek H., Soler-Rivas C. Appl. Microbiol. Biotechnol. 61:336-341(2003) [PubMed: 12743763] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Horst U1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X85113 mRNA. Translation: CAA59432.1.
PIR	S53017.
3D structure databases
SMR	Q00024. Positions 16-431.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.10.3.1. 984.
Family and domain databases
InterPro	IPR008922. Di-copper_centre. IPR016216. Monophenol_mOase_fun. IPR002227. Tyrosinase. [Graphical view]
Gene3D	G3DSA:1.10.1280.10. Di-copper_centre. 1 hit.
Pfam	PF00264. Tyrosinase. 1 hit. [Graphical view]
PIRSF	PIRSF000340. MPO_fungal. 1 hit.
PRINTS	PR00092. TYROSINASE.
PROSITE	PS00497. TYROSINASE_1. 1 hit. PS00498. TYROSINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PPO1_AGABI

Accession

Primary (citable) accession number: Q00024

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1996
Last modified:	January 19, 2010
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)