LACS_TRAHI
ID LACS_TRAHI Reviewed; 238 AA.
AC C0HLV6; C0HLU3;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 1.
DT 03-AUG-2022, entry version 4.
DE RecName: Full=Laccase-S {ECO:0000303|PubMed:34093489};
DE Short=ThLacc-S {ECO:0000303|PubMed:34093489};
DE EC=1.10.3.2 {ECO:0000269|PubMed:34093489};
DE AltName: Full=Benzenediol:oxygen oxidoreductase S {ECO:0000305|PubMed:34093489};
DE AltName: Full=Diphenol oxidase S {ECO:0000305|PubMed:34093489};
DE AltName: Full=Urishiol oxidase S {ECO:0000305|PubMed:34093489};
DE Flags: Fragment;
OS Trametes hirsuta (White-rot fungus) (Coriolus hirsutus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=5327 {ECO:0000303|PubMed:34093489};
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION,
RP MASS SPECTROMETRY, AND BIOTECHNOLOGY.
RX PubMed=34093489; DOI=10.3389/fmicb.2021.670163;
RA Si J., Ma H., Cao Y., Cui B., Dai Y.;
RT "Introducing a Thermo-Alkali-Stable, Metallic Ion-Tolerant Laccase Purified
RT From White Rot Fungus Trametes hirsuta.";
RL Front. Microbiol. 12:670163-670163(2021).
CC -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC products (By similarity). Has activity towards 2,2'-azino-bis(3-
CC ethylbenzothiazoline-6-sulfonic acid) (ABTS) (PubMed:34093489).
CC {ECO:0000250|UniProtKB:D0VWU3, ECO:0000269|PubMed:34093489}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O;
CC Xref=Rhea:RHEA:11276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17594, ChEBI:CHEBI:17977; EC=1.10.3.2;
CC Evidence={ECO:0000269|PubMed:34093489};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000269|PubMed:34093489};
CC Note=Binds 4 Cu cations per monomer. {ECO:0000250|UniProtKB:D0VWU3};
CC -!- ACTIVITY REGULATION: Activity is strongly promoted by toluene
CC (PubMed:34093489). Activity is promoted by magnesium, potassium,
CC cadmium, zinc, nickel, sodium, lead and manganese ions
CC (PubMed:34093489). Completely inhibited by IAA (cysteine protease
CC inhibitor), PMSF (serine protease inhibitor), DEP (histidine protease
CC inhibitor) and NAI (tyrosine protease inhibitor) (PubMed:34093489).
CC Inhibited by ethanol, acetone, SDS, and EDTA (PubMed:34093489).
CC Activity is strongly inhibited by mercury ions (PubMed:34093489). Also
CC inhibited by lithium, aluminum, calcium, barium and iron ions
CC (PubMed:34093489). {ECO:0000269|PubMed:34093489}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=87.47 uM for ABTS (at pH 6.0 and 50 degrees Celsius);
CC Note=kcat is 129.37 sec(-1) for ABTS oxidation (at pH 6.0 and 50
CC degrees Celsius). {ECO:0000269|PubMed:34093489};
CC pH dependence:
CC Optimum pH is 6 at 25 degrees Celsius (PubMed:34093489). Retains over
CC 60 percent activity in the pH range from 4 to 10 (PubMed:34093489).
CC Retains activity above 50% after incubation at pH 5-10 for 72 hours
CC (PubMed:34093489). {ECO:0000269|PubMed:34093489};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius (PubMed:34093489). Retains
CC over 57 percent activity when incubated for 2 hours at temperatures
CC between 30-65 degrees Celsius (PubMed:34093489).
CC {ECO:0000269|PubMed:34093489};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:34093489}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34093489}.
CC -!- MASS SPECTROMETRY: Mass=56976.37; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:34093489};
CC -!- BIOTECHNOLOGY: Able to metabolize the endocrine disrupting chemical
CC (EDC) 17beta-estradiol (E2), and so could be used in biotechnological
CC and industrial applications that require the biodegradation and
CC bioremediation of the environmental pollutant.
CC {ECO:0000269|PubMed:34093489}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR SMR; C0HLV6; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0052716; F:hydroquinone:oxygen oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.420; -; 2.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; SSF49503; 2.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
PE 1: Evidence at protein level;
KW Copper; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Lignin degradation; Metal-binding; Oxidoreductase; Secreted.
FT CHAIN 1..238
FT /note="Laccase-S"
FT /id="PRO_0000453427"
FT DOMAIN 4..87
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 100..238
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT BINDING 21
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 23
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 66
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 68
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 74..162
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:34093489"
FT NON_TER 238
FT /evidence="ECO:0000303|PubMed:34093489"
SQ SEQUENCE 238 AA; 27055 MW; 79668D388A8F4456 CRC64;
FQLNVIANMN NHTMLKQTSI HWHCHFQKGT NWADGHAFVN ACPIASGHSF LYDFTAPDQH
GTFWYHSHLS TQYCDGLRGH FVVYDPADPH HDLYDVDDEH TIITLADWYH VAAKLGHHFQ
LGADSTLING SGRFAGDPTA HLTVIYVTQG KRYRFHLVSL SCDPNHVFSI DSNHMTVIEA
DAVSHEHCTV DSIQIYAGQR YSFHLTVDQD VDNYWIRAHP SFGTYSFHDG INSAIARY
