LAC1_GALSP
ID LAC1_GALSP Reviewed; 23 AA.
AC P86351;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=Laccase-1 {ECO:0000250|UniProtKB:Q12718, ECO:0000303|Ref.1};
DE Short=Lac1 {ECO:0000303|Ref.1};
DE EC=1.10.3.2 {ECO:0000269|Ref.1};
DE AltName: Full=Benzenediol:oxygen oxidoreductase 1 {ECO:0000250|UniProtKB:Q12718};
DE AltName: Full=Diphenol oxidase 1 {ECO:0000250|UniProtKB:Q12718};
DE AltName: Full=Urishiol oxidase 1 {ECO:0000250|UniProtKB:Q12718};
DE Flags: Fragments;
OS Galerina sp.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Strophariaceae; Galerina;
OC unclassified Galerina.
OX NCBI_TaxID=671179;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=HC1 / DSM 22662 {ECO:0000269|Ref.1};
RX DOI=10.1016/j.procbio.2010.07.013;
RA Ibrahim V., Mendoza L., Mamo G., Hatti-Kaul R.;
RT "Blue laccase from Galerina sp.: properties and potential for Kraft lignin
RT demethylation.";
RL Process Biochem. 46:379-384(2010).
CC -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC products. Demethylates eucalyptus hard wood lignin. Has high activity
CC against the non-phenolic heterocyclic compound ABTS, and lower activity
CC against the phenolic substrates syringic acid, caffeic acid,
CC syringaldazine, vanillic acid, catechol and levodihydroxyphenylalanine.
CC {ECO:0000269|Ref.1}.
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|Ref.1};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:Q12718, ECO:0000269|Ref.1};
CC Note=Binds 4 Cu cations per monomer. {ECO:0000250|UniProtKB:Q12718,
CC ECO:0000269|Ref.1};
CC -!- ACTIVITY REGULATION: Strongly inhibited by sodium azide, sodium
CC cyanide, Li(+), Sn(+), Hg(2+), and the disulfide-reducing agents beta-
CC mercaptoethanol, dithiothreitol and thioglycolic acid. Moderately
CC inhibited by Mn(2+) and Fe(2+), inhibition by these metal ions is
CC stronger at 0.1 mM than at 1 mM. Moderately inhibited by Cu(2+).
CC {ECO:0000269|Ref.1}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14 uM for ABTS {ECO:0000269|Ref.1};
CC KM=0.8 uM for syringaldazine {ECO:0000269|Ref.1};
CC pH dependence:
CC Optimum pH is 3.0 with ABTS as substrate, activity decreases sharply
CC as pH increases, and no activity is seen at pH 7.0. Optimum pH is 4.0
CC with syringic acid as substrate, 5.0 with caffeic acid,
CC syringaldazine, vanillic acid or catechol as substrate, and 6.0 with
CC levodihydroxyphenylalanine as substrate. Inactive after 3 hours
CC incubation at pH 2.0, retains 20% of its activity after 24 hours at
CC pH 3.0 and 90% of its activity after 24 hours at pH 9.0.
CC {ECO:0000269|Ref.1};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius. Shows 50% of its maximal
CC activity at 20 degrees Celsius. Has a half-life of 53 minutes at 50
CC degrees Celsius, 23 minutes at 60 degrees Celsius, and less than 2
CC minutes at 70 degrees Celsius. {ECO:0000269|Ref.1};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is: 4,
CC its MW is: 64 kDa. {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000255}.
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DR AlphaFoldDB; P86351; -.
DR SABIO-RK; P86351; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0052716; F:hydroquinone:oxygen oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Copper; Direct protein sequencing; Lignin degradation; Metal-binding;
KW Oxidoreductase; Secreted.
FT CHAIN <1..>23
FT /note="Laccase-1"
FT /id="PRO_0000399056"
FT NON_CONS 11..12
FT /evidence="ECO:0000303|Ref.1"
FT NON_TER 1
FT /evidence="ECO:0000303|Ref.1"
FT NON_TER 23
FT /evidence="ECO:0000303|Ref.1"
SQ SEQUENCE 23 AA; 2303 MW; 1CF71949A9EC8945 CRC64;
GPSTDLVIGN KGFDGGIDSA ILR
