ID   LAC1_PLEOS     STANDARD;      PRT;   529 AA.
AC   Q12729;
DT   01-NOV-1997 (Rel. 35, Created)
DT   01-NOV-1997 (Rel. 35, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   Laccase 1 precursor (EC 1.10.3.2) (Benzenediol:oxygen oxidoreductase)
DE   (Urishiol oxidase) (Diphenol oxidase).
GN   Name=POX1;
OS   Pleurotus ostreatus (Oyster mushroom) (White-rot fungus).
OC   Eukaryota; Fungi; Basidiomycota; Hymenomycetes; Homobasidiomycetes;
OC   Agaricales; Pleurotaceae; Pleurotus.
OX   NCBI_TaxID=5322;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Florida; TISSUE=Mycelium;
RX   MEDLINE=95314294; PubMed=7793961;
RA   Giardina P., Cannio R., Martirani L., Marzullo L., Palmieri G.,
RA   Sannia G.;
RT   "Cloning and sequencing of a laccase gene from the lignin-degrading
RT   basidiomycete Pleurotus ostreatus.";
RL   Appl. Environ. Microbiol. 61:2408-2413(1995).
CC   -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC       products (By similarity).
CC   -!- CATALYTIC ACTIVITY: 4 benzenediol + O(2) = 4 benzosemiquinone + 2
CC       H(2)O.
CC   -!- COFACTOR: Binds 4 Cu-ions per molecule. Three distinct Cu centers
CC       known as type 1 or blue, type 2 or normal, and type 3 or coupled
CC       binuclear (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC   -!- SIMILARITY: Contains 3 plastocyanin-like domains.
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DR   EMBL; Z34847; CAA84356.1; -.
DR   EMBL; Z22591; CAA80305.1; -.
DR   PIR; S49120; S49120.
DR   HSSP; Q12718; 1GYC.
DR   InterPro; IPR001117; Cu-oxidase.
DR   InterPro; IPR002355; Cu_ox_copper_BS.
DR   InterPro; IPR008972; Cupredoxin.
DR   Pfam; PF00394; Cu-oxidase; 1.
DR   PROSITE; PS00079; MULTICOPPER_OXIDASE1; 2.
DR   PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
KW   Copper; Glycoprotein; Lignin degradation; Metal-binding;
KW   Multigene family; Oxidoreductase; Repeat; Signal.
FT   SIGNAL        1     23       Potential.
FT   CHAIN        24    529       Laccase 1.
FT   DOMAIN       25    159       Plastocyanin-like 1.
FT   DOMAIN      170    312       Plastocyanin-like 2.
FT   DOMAIN      380    499       Plastocyanin-like 3.
FT   METAL        96     96       Copper (type 2) (By similarity).
FT   METAL        98     98       Copper (type 3) (By similarity).
FT   METAL       141    141       Copper (type 3) (By similarity).
FT   METAL       143    143       Copper (type 3) (By similarity).
FT   METAL       425    425       Copper (type 1) (By similarity).
FT   METAL       428    428       Copper (type 2) (By similarity).
FT   METAL       430    430       Copper (type 3) (By similarity).
FT   METAL       481    481       Copper (type 3) (By similarity).
FT   METAL       482    482       Copper (type 1) (By similarity).
FT   METAL       483    483       Copper (type 3) (By similarity).
FT   METAL       487    487       Copper (type 1) (By similarity).
FT   CARBOHYD     57     57       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    239    239       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    282    282       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    465    465       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   529 AA;  56580 MW;  40110AFC4886882F CRC64;
     MFPGARILAT LTLALHLLHG THAAIGPTGD MYIVNEDVSP DGFTRSAVVA RSDPTTNGTS
     ETLTGVLVQG NKGDNFQLNV LNQLSDTTML KTTSIHWHGF FQSGSTWADG PAFVNQCPIA
     SGNSFLYDFN VPDQAGTFWY HSHLSTQYCD GLRGPFIVYD PSDPHLSLYD VDNADTIITL
     EDWYHVVAPQ NAVLPTADST LINGKGRFAG GPTSALAVIN VESNKRYRFR LISMSCDPNF
     TFSIDGHSLQ VIEADAVNIV PIVVDSIQIF AGQRYSFVLN ANQTVDNYWI RADPNLGSTG
     FDGGINSAIL RYAGATEDDP TTTSSTSTPL EETNLVPLEN PGAPGPAVPG GADININLAM
     AFDVTNFELT INGSPFKAPT APVLLQILSG ATTAASLLPS GSIYSLEANK VVEISIPALA
     VGGPHPFHLH GHTFDVIRSA GSTTYNFDTP ARRDVVNTGT DANDNVTIRF VTDNPGPWFL
     HCHIDWHLEI GLAVVFAEDV TSITAPPAAW DDLCPIYDAL SDSDKGGIA
//