Reviewed, UniProtKB/Swiss-Prot Q00234 (TYRO_ASPOR)

Names and origin

Protein names

Recommended name:
    Tyrosinase
    EC=1.14.18.1
Alternative name(s):
    Monophenol monooxygenase

Gene names

Name:	melO
ORF Names:	AO090038000061

Organism

Aspergillus oryzae [Complete proteome]

Taxonomic identifier

5062 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	539 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds.
Catalytic activity	L-tyrosine + L-dopa + O2 = L-dopa + dopaquinone + H2O.
Cofactor	Binds 2 copper ions per subunit.
Enzyme regulation	Activated by acidifying treatment at pH 3.0.
Subunit structure	Homotetramer.
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the tyrosinase family.

Ontologies

Keywords
Biological process	Melanin biosynthesis
Ligand	Copper Metal-binding
Molecular function	Monooxygenase Oxidoreductase
PTM	Thioether bond
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	melanin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW monophenol monooxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 539	539	Tyrosinase		PRO_0000186733
Sites
	Metal binding	63	1	Copper A By similarity
	Metal binding	84	1	Copper A By similarity
	Metal binding	93	1	Copper A By similarity
	Metal binding	290	1	Copper B By similarity
	Metal binding	294	1	Copper B By similarity
	Metal binding	333	1	Copper B By similarity
Amino acid modifications
	Cross-link	82 ↔ 84		2'-(S-cysteinyl)-histidine (Cys-His) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q00234-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: CD2ECD702A018E15	FASTA	539	60,605
	10 20 30 40 50 60 MASVEPIKTF EIRQKGPVET KAERKSIRDL NEEELDKLIE AWRWIQDPAR TGEDSFFYLA 70 80 90 100 110 120 GLHGEPFRGA GYNNSHWWGG YCHHGNILFP TWHRAYLMAV EKALRKACPD VSLPYWDESD 130 140 150 160 170 180 DETAKKGIPL IFTQKEYKGK PNPLYSYTFS ERIVDRLAKF PDADYSKPQG YKTCRYPYSG 190 200 210 220 230 240 LCGQDDIAIA QQHNNFLDAN FNQEQITGLL NSNVTSWLNL GQFTDIEGKQ VKADTRWKIR 250 260 270 280 290 300 QCLLTEEYTV FSNTTSAQRW NDEQFHPLES GGKETEAKAT SLAVPLESPH NDMHLAIGGV 310 320 330 340 350 360 QIPGFNVDQY AGANGDMGEN DTASFDPIFY FHHCFIDYLF WTWQTMHKKT DASQITILPE 370 380 390 400 410 420 YPGTNSVDSQ GPTPGISGNT WLTLDTPLDP FRENGDKVTS NKLLTLKDLP YTYKAPTSGT 430 440 450 460 470 480 GSVFNDVPRL NYPLSPPILR VSGINRASIA GSFALAISQT DHTGKAQVKG IESVLSRWHV 490 500 510 520 530 QGCANCQTHL STTAFVPLFE LNEDDAKRKH ANNELAVHLH TRGNPGGQRV RNVTVGTMR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and nucleotide sequence of the protyrosinase gene, melO, from Aspergillus oryzae and expression of the gene in yeast cells." Fujita Y., Uraga Y., Ichishima E. Biochim. Biophys. Acta 1261:151-154(1995) [PubMed: 7893753] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: ATCC 22788 / RIB 128 / CBS 819.72 / IFO 30113 / JCM 2248.
[2]	"Genome sequencing and analysis of Aspergillus oryzae." Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H. Nature 438:1157-1161(2005) [PubMed: 16372010] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D37929 Genomic DNA. Translation: BAA07149.1. AP007169 Genomic DNA. Translation: BAE63910.1.
PIR	S53529.
RefSeq	XP_001825043.1.
3D structure databases
SMR	Q00234. Positions 23-417.
ModBase	Search...
Genome annotation databases
GeneID	5997138.
GenomeReviews	Gene locus melO in contig AP007169_GR.
KEGG	aor:AO090038000061.
Phylogenomic databases
OrthoDB	EOG9PP00S.
Enzyme and pathway databases
BRENDA	1.14.18.1. 2240.
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

TYRO_ASPOR

Accession

Primary (citable) accession number: Q00234
Secondary accession number(s): Q2U3F5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	January 19, 2010
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)