LACF_GANAU
ID LACF_GANAU Reviewed; 237 AA.
AC C0HLV7;
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 {ECO:0000303|PubMed:34467865};
DE Short=Galacc-F {ECO:0000303|PubMed:34467865};
DE EC=1.10.3.2 {ECO:0000269|PubMed:34467865};
DE AltName: Full=Benzenediol:oxygen oxidoreductase S {ECO:0000303|PubMed:34467865};
DE AltName: Full=Diphenol oxidase S {ECO:0000303|PubMed:34467865};
DE AltName: Full=Urishiol oxidase S {ECO:0000303|PubMed:34467865};
DE Flags: Fragment;
OS Ganoderma australe (Bracket fungus) (Polyporus australis).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Ganoderma.
OX NCBI_TaxID=34457 {ECO:0000303|PubMed:34467865};
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP BIOTECHNOLOGY.
RX PubMed=34467865; DOI=10.1016/j.jenvman.2021.113619;
RA Si J., Wu Y., Ma H.F., Cao Y.J., Sun Y.F., Cui B.K.;
RT "Selection of a pH- and temperature-stable laccase from Ganoderma australe
RT and its application for bioremediation of textile dyes.";
RL J. Environ. Manage. 299:113619-113619(2021).
CC -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC products (By similarity). Multicopper oxidase that catalyzes the
CC oxidation of a variety of substrates, including phenolic and non-
CC phenolic compounds (PubMed:34467865). Has highest activity towards
CC 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), also
CC active towards hydroquinone, phenol, gallic acid, catechol, guaiacol,
CC levodopa, 2,6-dimethoxyphenol (2,6-DMP), tyrosine, ferulic acid and
CC veratryl alcohol (PubMed:34467865). {ECO:0000250|UniProtKB:D0VWU3,
CC ECO:0000269|PubMed:34467865}.
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:34467865};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000269|PubMed:34467865};
CC Note=Binds 4 Cu cations per monomer. {ECO:0000250|UniProtKB:D0VWU3};
CC -!- ACTIVITY REGULATION: Activity is promoted by magnesium, Fe(2+), nickel,
CC zinc and cadmium ions (PubMed:34467865). Completely inhibited by IAA
CC (cysteine protease inhibitor), PMSF (serine protease inhibitor) and DEP
CC (histidine protease inhibitor) (PubMed:34467865). Inhibited by CTAB,
CC SDS and EDTA (PubMed:34467865). Inhibited by lithium, sodium, aluminum,
CC potassium, calcium, manganese, Fe(3+), barium and mercury ions
CC (PubMed:34467865). {ECO:0000269|PubMed:34467865}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=164.14 uM for ABTS (at pH 6.0 and 55 degrees Celsius)
CC {ECO:0000269|PubMed:34467865};
CC KM=156.55 uM for ABTS (at 55 degrees Celsius in the presence of 5 mM
CC NaCl) {ECO:0000269|PubMed:34467865};
CC KM=147.48 uM for ABTS (at 55 degrees Celsius in the presence of 10 mM
CC NaCl) {ECO:0000269|PubMed:34467865};
CC KM=150.56 uM for ABTS (at 55 degrees Celsius in the presence of 15 mM
CC NaCl) {ECO:0000269|PubMed:34467865};
CC KM=159.75 uM for ABTS (at 55 degrees Celsius in the presence of 20 mM
CC NaCl) {ECO:0000269|PubMed:34467865};
CC KM=201.34 uM for ABTS (at 55 degrees Celsius in the presence of 25 mM
CC NaCl) {ECO:0000269|PubMed:34467865};
CC KM=203.47 uM for ABTS (at 55 degrees Celsius in the presence of 30 mM
CC NaCl) {ECO:0000269|PubMed:34467865};
CC KM=211.20 uM for ABTS (at 55 degrees Celsius in the presence of 50 mM
CC NaCl) {ECO:0000269|PubMed:34467865};
CC KM=214.50 uM for ABTS (at 55 degrees Celsius in the presence of 70 mM
CC NaCl) {ECO:0000269|PubMed:34467865};
CC KM=217.08 uM for ABTS (at 55 degrees Celsius in the presence of 90 mM
CC NaCl) {ECO:0000269|PubMed:34467865};
CC KM=221.65 uM for ABTS (at 55 degrees Celsius in the presence of 0.1 M
CC NaCl) {ECO:0000269|PubMed:34467865};
CC KM=226.07 uM for ABTS (at 55 degrees Celsius in the presence of 0.3 M
CC NaCl) {ECO:0000269|PubMed:34467865};
CC KM=228.12 uM for ABTS (at 55 degrees Celsius in the presence of 0.5 M
CC NaCl) {ECO:0000269|PubMed:34467865};
CC KM=236.04 uM for ABTS (at 55 degrees Celsius in the presence of 0.7 M
CC NaCl) {ECO:0000269|PubMed:34467865};
CC KM=243.32 uM for ABTS (at 55 degrees Celsius in the presence of 0.9 M
CC NaCl) {ECO:0000269|PubMed:34467865};
CC KM=249.91 uM for ABTS (at 55 degrees Celsius in the presence of 1 M
CC NaCl) {ECO:0000269|PubMed:34467865};
CC KM=258.45 uM for ABTS (at 55 degrees Celsius in the presence of 3 M
CC NaCl) {ECO:0000269|PubMed:34467865};
CC KM=269.54 uM for ABTS (at 55 degrees Celsius in the presence of 5 M
CC NaCl) {ECO:0000269|PubMed:34467865};
CC KM=274.22 uM for ABTS (at 55 degrees Celsius in the presence of 7 M
CC NaCl) {ECO:0000269|PubMed:34467865};
CC KM=282.78 uM for ABTS (at 55 degrees Celsius in the presence of 9 M
CC NaCl) {ECO:0000269|PubMed:34467865};
CC KM=170.67 uM for catechol (at pH 6.0 and 55 degrees Celsius)
CC {ECO:0000269|PubMed:34467865};
CC KM=188.98 uM for 2,6-dimethylphenol (at pH 6.0 and 55 degrees
CC Celsius) {ECO:0000269|PubMed:34467865};
CC KM=183.45 uM for levodopa (at pH 6.0 and 55 degrees Celsius)
CC {ECO:0000269|PubMed:34467865};
CC KM=195.65 uM for ferulic acid (at pH 6.0 and 55 degrees Celsius)
CC {ECO:0000269|PubMed:34467865};
CC KM=169.04 uM for gallic acid (at pH 6.0 and 55 degrees Celsius)
CC {ECO:0000269|PubMed:34467865};
CC KM=172.91 uM for guaiacol (at pH 6.0 and 55 degrees Celsius)
CC {ECO:0000269|PubMed:34467865};
CC KM=165.79 uM for hydroquinone (at pH 6.0 and 55 degrees Celsius)
CC {ECO:0000269|PubMed:34467865};
CC KM=168.45 uM for phenol (at pH 6.0 and 55 degrees Celsius)
CC {ECO:0000269|PubMed:34467865};
CC KM=192.07 uM for tyrosine (at pH 6.0 and 55 degrees Celsius)
CC {ECO:0000269|PubMed:34467865};
CC KM=206.43 uM for veratryl alcohol (at pH 6.0 and 55 degrees Celsius)
CC {ECO:0000269|PubMed:34467865};
CC Note=kcat is 273 sec(-1) for ABTS oxidation (at pH 6.0 and 55 degrees
CC Celsius) (PubMed:34467865). kcat is 259 sec(-1) for catechol
CC oxidation (at pH 6.0 and 55 degrees Celsius) (PubMed:34467865). kcat
CC is 237 sec(-1) for 2,6-dimethylphenol oxidation (at pH 6.0 and 55
CC degrees Celsius) (PubMed:34467865). kcat is 244 sec(-1) for levodopa
CC oxidation (at pH 6.0 and 55 degrees Celsius) (PubMed:34467865). kcat
CC is 217 sec(-1) for ferulic acid oxidation (at pH 6.0 and 55 degrees
CC Celsius) (PubMed:34467865). kcat is 262 sec(-1) for gallic acid
CC oxidation (at pH 6.0 and 55 degrees Celsius) (PubMed:34467865). kcat
CC is 256 sec(-1) for guaiacol oxidation (at pH 6.0 and 55 degrees
CC Celsius) (PubMed:34467865). kcat is 270 sec(-1) for hydroquinone
CC oxidation (at pH 6.0 and 55 degrees Celsius) (PubMed:34467865). kcat
CC is 264 sec(-1) for phenol oxidation (at pH 6.0 and 55 degrees
CC Celsius) (PubMed:34467865). kcat is 220 sec(-1) for tyrosine
CC oxidation (at pH 6.0 and 55 degrees Celsius) (PubMed:34467865). kcat
CC is 220 sec(-1) for tyrosine oxidation (at pH 6.0 and 55 degrees
CC Celsius) (PubMed:34467865). kcat is 201 sec(-1) for veratryl alcohol
CC oxidation (at pH 6.0 and 55 degrees Celsius) (PubMed:34467865). kcat
CC is 282 sec(-1) for ABTS oxidation (at 55 degrees Celsius in the
CC presence of 5 mM NaCl) (PubMed:34467865). kcat is 294 sec(-1) for
CC ABTS oxidation (at 55 degrees Celsius in the presence of 10 mM NaCl)
CC (PubMed:34467865). kcat is 289 sec(-1) for ABTS oxidation (at 55
CC degrees Celsius in the presence of 15 mM NaCl) (PubMed:34467865).
CC kcat is 279 sec(-1) for ABTS oxidation (at 55 degrees Celsius in the
CC presence of 20 mM NaCl) (PubMed:34467865). kcat is 235 sec(-1) for
CC ABTS oxidation (at 55 degrees Celsius in the presence of 25 mM NaCl)
CC (PubMed:34467865). kcat is 233 sec(-1) for ABTS oxidation (at 55
CC degrees Celsius in the presence of 30 mM NaCl) (PubMed:34467865).
CC kcat is 226 sec(-1) for ABTS oxidation (at 55 degrees Celsius in the
CC presence of 50 mM NaCl) (PubMed:34467865). kcat is 222 sec(-1) for
CC ABTS oxidation (at 55 degrees Celsius in the presence of 70 mM NaCl)
CC (PubMed:34467865). kcat is 218 sec(-1) for ABTS oxidation (at 55
CC degrees Celsius in the presence of 90 mM NaCl) (PubMed:34467865).
CC kcat is 215 sec(-1) for ABTS oxidation (at 55 degrees Celsius in the
CC presence of 0.1 M NaCl) (PubMed:34467865). kcat is 209 sec(-1) for
CC ABTS oxidation (at 55 degrees Celsius in the presence of 0.3 M NaCl)
CC (PubMed:34467865). kcat is 207 sec(-1) for ABTS oxidation (at 55
CC degrees Celsius in the presence of 0.5 M NaCl) (PubMed:34467865).
CC kcat is 201 sec(-1) for ABTS oxidation (at 55 degrees Celsius in the
CC presence of 0.7 M NaCl) (PubMed:34467865). kcat is 197 sec(-1) for
CC ABTS oxidation (at 55 degrees Celsius in the presence of 0.9 M NaCl)
CC (PubMed:34467865). kcat is 194 sec(-1) for ABTS oxidation (at 55
CC degrees Celsius in the presence of 1 M NaCl) (PubMed:34467865). kcat
CC is 185 sec(-1) for ABTS oxidation (at 55 degrees Celsius in the
CC presence of 3 M NaCl) (PubMed:34467865). kcat is 176 sec(-1) for ABTS
CC oxidation (at 55 degrees Celsius in the presence of 5 M NaCl)
CC (PubMed:34467865). kcat is 161 sec(-1) for ABTS oxidation (at 55
CC degrees Celsius in the presence of 7 M NaCl) (PubMed:34467865). kcat
CC is 152 sec(-1) for ABTS oxidation (at 55 degrees Celsius in the
CC presence of 9 M NaCl) (PubMed:34467865).
CC {ECO:0000269|PubMed:34467865};
CC pH dependence:
CC Optimum pH is 6 (PubMed:34467865). Retains over 72 percent activity
CC in the pH range 5 to 8 (PubMed:34467865). Retains activity above 89%
CC after incubation at pH 6 for 72 hours (PubMed:34467865). Retains
CC activity above 61% after incubation at pH 5-8 for 72 hours
CC (PubMed:34467865). {ECO:0000269|PubMed:34467865};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius (PubMed:34467865).
CC Thermostable (PubMed:34467865). Retains over 84 percent activity when
CC incubated for 3 hours at temperatures between 10-60 degrees Celsius
CC (PubMed:34467865). {ECO:0000269|PubMed:34467865};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34467865}.
CC -!- MASS SPECTROMETRY: Mass=47729.97; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:34467865};
CC -!- BIOTECHNOLOGY: Could be used in the treatment of dye effluents
CC (PubMed:34467865). Able to decolorize structurally multifarious
CC synthetic dyes, including metal-complex dyes, in the absence of redox
CC mediators (PubMed:34467865). Shows the highest removal efficiency for
CC metal-containing dye Acid Black 172, followed by Congo Red, Remazol
CC Brilliant Blue R, Reactive Brilliant Blue X-BR, Indigo Blue, Neutral
CC Red, Naphthol Green B, Methylene Blue, and Crystal Violet
CC (PubMed:34467865). Displays higher decolorization rates towards Acid
CC Black 172 when immobilized on composite nanoparticles (Fe3O4@Chitosan)
CC (PubMed:34467865). {ECO:0000269|PubMed:34467865}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR SMR; C0HLV7; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
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..237
FT /note="Laccase"
FT /id="PRO_0000453610"
FT DOMAIN 4..86
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 99..237
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 65
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 67
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 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 73..161
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:34467865"
FT NON_TER 237
FT /evidence="ECO:0000303|PubMed:34467865"
SQ SEQUENCE 237 AA; 26096 MW; 8E2A7556E262D5B3 CRC64;
FQLNVIANNN NHTMLTQTTI HCHGFFQGTN SADGHAFVNC CPIASGHSFL YDFSHPDQHG
TFCYHSHLST QYCCGLRGHF VVYDPSDPHC GLYDVDHDST VITLSDWYHV AAKLGHSFCL
GADSTLINGS GRSTGDCAAS LTVISVTQGK RYRFHLVSLS CDPNHTFSID GHDMSVIEVD
SIASQHVTVD SIQIFAGQRY SFVLTANQSI NNYWIRANPS FGNIGFHDGI NSAILRY
