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Q00234

- TYRO_ASPOR

UniProt

Q00234 - TYRO_ASPOR

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Protein
Tyrosinase
Gene
melO, AO090038000061
Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds.

Catalytic activityi

2 L-dopa + O2 = 2 dopaquinone + 2 H2O.
L-tyrosine + O2 = dopaquinone + H2O.

Cofactori

Binds 2 copper ions per subunit.

Enzyme regulationi

Activated by acidifying treatment at pH 3.0.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi63 – 631Copper A By similarity
Metal bindingi84 – 841Copper A By similarity
Metal bindingi93 – 931Copper A By similarity
Metal bindingi290 – 2901Copper B By similarity
Metal bindingi294 – 2941Copper B By similarity
Metal bindingi333 – 3331Copper B By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. monophenol monooxygenase activity Source: ASPGD

GO - Biological processi

  1. melanin biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Melanin biosynthesis

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosinase (EC:1.14.18.1)
Alternative name(s):
Monophenol monooxygenase
Gene namesi
Name:melO
ORF Names:AO090038000061
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006564: Chromosome 6

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 539539Tyrosinase
PRO_0000186733Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki82 ↔ 842'-(S-cysteinyl)-histidine (Cys-His) By similarity

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Thioether bond

Proteomic databases

PRIDEiQ00234.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi5062.CADAORAP00008707.

Structurei

3D structure databases

ProteinModelPortaliQ00234.

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.

Phylogenomic databases

HOGENOMiHOG000250264.
OMAiENDTASF.
OrthoDBiEOG7JX3D0.

Family and domain databases

Gene3Di1.10.1280.10. 3 hits.
InterProiIPR016216. Monophenol_mOase_fun.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamiPF00264. Tyrosinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000340. MPO_fungal. 1 hit.
PRINTSiPR00092. TYROSINASE.
SUPFAMiSSF48056. SSF48056. 2 hits.
PROSITEiPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q00234-1 [UniParc]FASTAAdd to Basket

« Hide

MASVEPIKTF EIRQKGPVET KAERKSIRDL NEEELDKLIE AWRWIQDPAR    50
TGEDSFFYLA GLHGEPFRGA GYNNSHWWGG YCHHGNILFP TWHRAYLMAV 100
EKALRKACPD VSLPYWDESD DETAKKGIPL IFTQKEYKGK PNPLYSYTFS 150
ERIVDRLAKF PDADYSKPQG YKTCRYPYSG LCGQDDIAIA QQHNNFLDAN 200
FNQEQITGLL NSNVTSWLNL GQFTDIEGKQ VKADTRWKIR QCLLTEEYTV 250
FSNTTSAQRW NDEQFHPLES GGKETEAKAT SLAVPLESPH NDMHLAIGGV 300
QIPGFNVDQY AGANGDMGEN DTASFDPIFY FHHCFIDYLF WTWQTMHKKT 350
DASQITILPE YPGTNSVDSQ GPTPGISGNT WLTLDTPLDP FRENGDKVTS 400
NKLLTLKDLP YTYKAPTSGT GSVFNDVPRL NYPLSPPILR VSGINRASIA 450
GSFALAISQT DHTGKAQVKG IESVLSRWHV QGCANCQTHL STTAFVPLFE 500
LNEDDAKRKH ANNELAVHLH TRGNPGGQRV RNVTVGTMR 539
Length:539
Mass (Da):60,605
Last modified:November 1, 1996 - v1
Checksum:iCD2ECD702A018E15
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D37929 Genomic DNA. Translation: BAA07149.1.
AP007169 Genomic DNA. Translation: BAE63910.1.
PIRiS53529.
RefSeqiXP_001825043.1. XM_001824991.2.

Genome annotation databases

EnsemblFungiiCADAORAT00008890; CADAORAP00008707; CADAORAG00008890.
GeneIDi5997138.
KEGGiaor:AOR_1_92074.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D37929 Genomic DNA. Translation: BAA07149.1 .
AP007169 Genomic DNA. Translation: BAE63910.1 .
PIRi S53529.
RefSeqi XP_001825043.1. XM_001824991.2.

3D structure databases

ProteinModelPortali Q00234.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5062.CADAORAP00008707.

Proteomic databases

PRIDEi Q00234.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAORAT00008890 ; CADAORAP00008707 ; CADAORAG00008890 .
GeneIDi 5997138.
KEGGi aor:AOR_1_92074.

Phylogenomic databases

HOGENOMi HOG000250264.
OMAi ENDTASF.
OrthoDBi EOG7JX3D0.

Family and domain databases

Gene3Di 1.10.1280.10. 3 hits.
InterProi IPR016216. Monophenol_mOase_fun.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view ]
Pfami PF00264. Tyrosinase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000340. MPO_fungal. 1 hit.
PRINTSi PR00092. TYROSINASE.
SUPFAMi SSF48056. SSF48056. 2 hits.
PROSITEi PS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 42149 / RIB 40.

Entry informationi

Entry nameiTYRO_ASPOR
AccessioniPrimary (citable) accession number: Q00234
Secondary accession number(s): Q2U3F5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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