Reviewed, UniProtKB/Swiss-Prot P33180 (TYRO_RHIME)

Names and origin

Protein names

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

Gene names

Name:	mepA
Synonyms:	melA

Encoded on

Plasmid pRmeGR4b

Organism

Rhizobium meliloti (Sinorhizobium meliloti)

Taxonomic identifier

382 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium

Protein attributes

Sequence length	494 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	L-tyrosine + L-dopa + O2 = L-dopa + dopaquinone + H2O.
Cofactor	Binds 2 copper ions per subunit By similarity.
Sequence similarities	Belongs to the tyrosinase family.

Ontologies

Keywords
Biological process	Melanin biosynthesis
Ligand	Copper Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	Plasmid
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 – 494	494	Tyrosinase		PRO_0000186735
Sites
	Metal binding	38	1	Copper A By similarity
	Metal binding	44	1	Copper A By similarity
	Metal binding	53	1	Copper A By similarity
	Metal binding	64	1	Copper A By similarity
	Metal binding	224	1	Copper B By similarity
	Metal binding	228	1	Copper B By similarity
	Metal binding	256	1	Copper B By similarity

Sequences

	Sequence		Length	Mass (Da)
	P33180-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: B39A1DFCC2C3E962	FASTA	494	54,109
	10 20 30 40 50 60 MTSADGQKDL QSYMDAVTAM LKLPPSDRRN WYRNGFIHLM DCPHGDWWFT SWHRGYLGYF 70 80 90 100 110 120 EETCRELSGN PDFALPYWDW TANPEVLPPL FGTILDPVNS SAYIPDHNRF QDIMQEPIKA 130 140 150 160 170 180 YWDSLSPAQL QQQNLRGYPD FDALWSDAMA SFANQPNARF LTAQNPKLNP ATQTAVDIDT 190 200 210 220 230 240 IKASLAPTTF ANDAGAPGLA FNSPVSSSHQ VAPVGFSILE GQPHNRVHMS VGGQSAPYGL 250 260 270 280 290 300 MSQNLSPLDP IFFLHHCNID RLWDVWTRKQ QAMGLPVGPT ADQQTQYDPE PYLFYVNADG 310 320 330 340 350 360 SPVSDKTRAA DYLEIGDFDY DYDPGSGEEV IPVATAGRSA PIPALEAAVS ASAAVAINKP 370 380 390 400 410 420 ATAKLTVSQE LVDVAAKPSE QSRQFAKVSI APPMDVGGLN FLVFISPEGT TPDLNPDGPD 430 440 450 460 470 480 FAGSFEFFGV RHHHTDTVSF TIPIDKALDR LIDDGRLKAG EPIDFAVVVA QEGKRVEGSM 490 PAKAQLTDIQ VGSF

References

[1]

"Melanin production by Rhizobium meliloti GR4 is linked to nonsymbiotic plasmid pRmeGR4b: cloning, sequencing, and expression of the tyrosinase gene mepA." Mercado-Blanco J., Garcia F., Fernandez-Lopez M., Olivares J. J. Bacteriol. 175:5403-5410(1993) [PubMed: 8366027] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: GR4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X69526 Genomic DNA. Translation: CAA49273.1.
PIR	A48657.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.14.18.1. 142.
Family and domain databases
InterPro	IPR008922. Di-copper_centre. IPR002227. Tyrosinase. [Graphical view]
Gene3D	G3DSA:1.10.1280.10. Di-copper_centre. 1 hit.
Pfam	PF00264. Tyrosinase. 1 hit. [Graphical view]
PRINTS	PR00092. TYROSINASE.
PROSITE	PS00497. TYROSINASE_1. 1 hit. PS00498. TYROSINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TYRO_RHIME

Accession

Primary (citable) accession number: P33180

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	September 22, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)