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A7BHQ9

- TYRO_PHONA

UniProt

A7BHQ9 - TYRO_PHONA

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Protein

Tyrosinase

Gene

tyr1

Organism
Pholiota nameko
Status
Reviewed - Annotation score: 5 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.By similarity

Catalytic activityi

2 L-dopa + O2 = 2 dopaquinone + 2 H2O.1 Publication
L-tyrosine + O2 = dopaquinone + H2O.1 Publication

Cofactori

Binds 2 copper ions per subunit.1 Publication

Kineticsi

  1. KM=1930 µM for L-dopa1 Publication
  2. KM=119 µM for t-butylphenol1 Publication
  3. KM=30.6 µM for p-cresol1 Publication
  4. KM=163 µM for t-butylcatechol1 Publication
  5. KM=1240 µM for 3-(3,4-dihydroxyphenyl) propionic acid1 Publication
  6. KM=122 µM for dopamine1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi58 – 581Copper ABy similarity
Metal bindingi86 – 861Copper ABy similarity
Metal bindingi95 – 951Copper ABy similarity
Metal bindingi258 – 2581Copper BBy similarity
Metal bindingi262 – 2621Copper BBy similarity
Metal bindingi287 – 2871Copper BBy similarity

GO - Molecular functioni

  1. copper ion binding Source: UniProtKB
  2. monophenol monooxygenase activity Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Melanin biosynthesis

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
TyrosinaseImported1 Publication (EC:1.14.18.1)
Gene namesi
Name:tyr1Imported
OrganismiPholiota nameko
Taxonomic identifieri61267 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesStrophariaceaePholiota

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 387387Tyrosinase1 PublicationPRO_0000352767Add
BLAST
Propeptidei388 – 6252381 PublicationPRO_0000352768Add
BLAST

Post-translational modificationi

The N-terminus is blocked.1 Publication

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliA7BHQ9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi367 – 45185Ala-richSequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the tyrosinase family.Sequence Analysis

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
InterProiIPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamiPF00264. Tyrosinase. 1 hit.
[Graphical view]
PRINTSiPR00092. TYROSINASE.
SUPFAMiSSF48056. SSF48056. 1 hit.
PROSITEiPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A7BHQ9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSRVVITGVS GTIANRLEIN DFVKNDKFFS LYIQALQVMS SVPPQENVRS
60 70 80 90 100
FFQIGGIHGL PYTPWDGITG DQPFDPNTQW GGYCTHGSVL FPTWHRPYVL
110 120 130 140 150
LYEQILHKHV QDIAATYTTS DKAAWVQAAA NLRQPYWDWA ANAVPPDQVI
160 170 180 190 200
VSKKVTITGS NGHKVEVDNP LYHYKFHPID SSFPRPYSEW PTTLRQPNSS
210 220 230 240 250
RPNATDNVAK LRNVLRASQE NITSNTYSML TRVHTWKAFS NHTVGDGGST
260 270 280 290 300
SNSLEAIHDG IHVDVGGGGH MGDPAVAAFD PIFFLHHCNV DRLLSLWAAI
310 320 330 340 350
NPGVWVSPGD SEDGTFILPP EAPVDVSTPL TPFSNTETTF WASGGITDTT
360 370 380 390 400
KLGYTYPEFN GLDLGNAQAV KAAIGNIVNR LYGASVFSGF AAATSAIGAG
410 420 430 440 450
SVASLAADVP LEKAPAPAPE AAAQPPVPAP AHVEPAVRAV SVHAAAAQPH
460 470 480 490 500
AEPPVHVSAG GHPSPHGFYD WTARIEFKKY EFGSSFSVLL FLGPVPEDPE
510 520 530 540 550
QWLVSPNFVG AHHAFVNSAA GHCANCRSQG NVVVEGFVHL TKYISEHAGL
560 570 580 590 600
RSLNPEVVEP YLTNELHWRV LKADGSVGQL ESLEVSVYGT PMNLPVGAMF
610 620
PVPGNRRHFH GITHGRVGGS RHAIV
Length:625
Mass (Da):67,499
Last modified:September 11, 2007 - v1
Checksum:i26E8AEFA285F871B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131I → V in BAF74396. (PubMed:17617709)Curated
Sequence conflicti151 – 1511V → A in BAF74396. (PubMed:17617709)Curated
Sequence conflicti272 – 2721G → A in BAF74396. (PubMed:17617709)Curated
Sequence conflicti425 – 4251P → S in BAF74396. (PubMed:17617709)Curated
Sequence conflicti528 – 5281S → N in BAF74396. (PubMed:17617709)Curated

Mass spectrometryi

Molecular mass is 42424.39 Da from positions 1 - 387. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB275646 mRNA. Translation: BAF74395.1.
AB275647 mRNA. Translation: BAF74396.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB275646 mRNA. Translation: BAF74395.1 .
AB275647 mRNA. Translation: BAF74396.1 .

3D structure databases

ProteinModelPortali A7BHQ9.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

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

Publicationsi

  1. "Purification, characterization, and molecular cloning of tyrosinase from Pholiota nameko."
    Kawamura-Konishi Y., Tsuji M., Hatana S., Asanuma M., Kakuta D., Kawano T., Mukouyama E.B., Goto H., Suzuki H.
    Biosci. Biotechnol. Biochem. 71:1752-1760(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 154-164; 175-195; 351-362 AND 384-387, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MASS SPECTROMETRY.
    Tissue: Fruiting body1 Publication.

Entry informationi

Entry nameiTYRO_PHONA
AccessioniPrimary (citable) accession number: A7BHQ9
Secondary accession number(s): A7BHR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: September 11, 2007
Last modified: October 1, 2014
This is version 27 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

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3