ID   TYRO_RHIML              Reviewed;         494 AA.
AC   P33180;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Tyrosinase;
DE            EC=1.14.18.1;
DE   AltName: Full=Monophenol monooxygenase;
GN   Name=mepA; Synonyms=melA;
OS   Rhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti).
OG   Plasmid pRmeGR4b.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=382;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=GR4;
RX   PubMed=8366027; DOI=10.1128/jb.175.17.5403-5410.1993;
RA   Mercado-Blanco J., Garcia F., Fernandez-Lopez M., Olivares J.;
RT   "Melanin production by Rhizobium meliloti GR4 is linked to nonsymbiotic
RT   plasmid pRmeGR4b: cloning, sequencing, and expression of the tyrosinase
RT   gene mepA.";
RL   J. Bacteriol. 175:5403-5410(1993).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone; Xref=Rhea:RHEA:34287,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57504,
CC         ChEBI:CHEBI:57924; EC=1.14.18.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tyrosine + O2 = H2O + L-dopaquinone; Xref=Rhea:RHEA:18117,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57924,
CC         ChEBI:CHEBI:58315; EC=1.14.18.1;
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000250|UniProtKB:Q9ZP19};
CC       Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:Q9ZP19};
CC   -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
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DR   EMBL; X69526; CAA49273.1; -; Genomic_DNA.
DR   PIR; A48657; A48657.
DR   AlphaFoldDB; P33180; -.
DR   SMR; P33180; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004503; F:tyrosinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR   InterPro; IPR008922; Di-copper_centre_dom_sf.
DR   InterPro; IPR002227; Tyrosinase_Cu-bd.
DR   PANTHER; PTHR11474:SF76; TYROSINASE; 1.
DR   PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR   Pfam; PF00264; Tyrosinase; 1.
DR   PRINTS; PR00092; TYROSINASE.
DR   SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR   PROSITE; PS00497; TYROSINASE_1; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
PE   3: Inferred from homology;
KW   Copper; Melanin biosynthesis; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Plasmid.
FT   CHAIN           1..494
FT                   /note="Tyrosinase"
FT                   /id="PRO_0000186735"
FT   BINDING         38
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         53
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         64
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         224
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         228
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         256
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
SQ   SEQUENCE   494 AA;  54109 MW;  B39A1DFCC2C3E962 CRC64;
     MTSADGQKDL QSYMDAVTAM LKLPPSDRRN WYRNGFIHLM DCPHGDWWFT SWHRGYLGYF
     EETCRELSGN PDFALPYWDW TANPEVLPPL FGTILDPVNS SAYIPDHNRF QDIMQEPIKA
     YWDSLSPAQL QQQNLRGYPD FDALWSDAMA SFANQPNARF LTAQNPKLNP ATQTAVDIDT
     IKASLAPTTF ANDAGAPGLA FNSPVSSSHQ VAPVGFSILE GQPHNRVHMS VGGQSAPYGL
     MSQNLSPLDP IFFLHHCNID RLWDVWTRKQ QAMGLPVGPT ADQQTQYDPE PYLFYVNADG
     SPVSDKTRAA DYLEIGDFDY DYDPGSGEEV IPVATAGRSA PIPALEAAVS ASAAVAINKP
     ATAKLTVSQE LVDVAAKPSE QSRQFAKVSI APPMDVGGLN FLVFISPEGT TPDLNPDGPD
     FAGSFEFFGV RHHHTDTVSF TIPIDKALDR LIDDGRLKAG EPIDFAVVVA QEGKRVEGSM
     PAKAQLTDIQ VGSF
//