Reviewed, UniProtKB/Swiss-Prot P55023 (TYRO_STRLN)

Names and origin

Protein names

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

Gene names

Name:	melC2
Synonyms:	mel

Organism

Streptomyces lincolnensis

Taxonomic identifier

1915 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	273 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

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 By similarity.
Sequence similarities	Belongs to the tyrosinase family.

Ontologies

Keywords
Biological process	Melanin biosynthesis
Ligand	Copper Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Gene Ontology (GO)
Biological process	melanin biosynthetic process from tyrosine 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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 273	272	Tyrosinase		PRO_0000186739
Sites
	Metal binding	37	1	Copper A By similarity
	Metal binding	53	1	Copper A By similarity
	Metal binding	62	1	Copper A By similarity
	Metal binding	189	1	Copper B By similarity
	Metal binding	193	1	Copper B By similarity
	Metal binding	215	1	Copper B By similarity

Sequences

	Sequence		Length	Mass (Da)
	P55023-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: E9D8616C99DD4DB9	FASTA	273	30,854
	10 20 30 40 50 60 MTVRKNQATL TADEKRRFVT AVLSSSAARY DTFVTTHNEF IVADTDNGER TGHRSPSFLP 70 80 90 100 110 120 WHRRFLLEFE RALQSVDASV ALPYWDWSTD RSARSSLWAP DFLGGTGRSR NGRVTDGPFR 130 140 150 160 170 180 AATGVWPITV RLDGRTYLRR ALGGAGRELP TRAEVDSVLS IPTYDMAPWN SASDGFRNHL 190 200 210 220 230 240 EGWRGVNLHN RVHVWVGGQM ATGVSPNDPV FWLHHAYIDK LWAQWQRRHR TPAYVPAAGT 250 260 270 PDVVDLDETM KPWHDSSPAD LLDHTGHYTF DTD

References

[1]	Zhang H.Z., Piepersberg W. Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 78-11.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X95703 Genomic DNA. Translation: CAA65000.1.
3D structure databases
HSSP	HSSP built from PDB template 1JS8 based on UniProtKB O61363.
SMR	P55023. Positions 2-271.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.14.18.1. 289191.
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_STRLN

Accession

Primary (citable) accession number: P55023

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	January 20, 2009
This is version 43 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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