LAC2_FOMPI
ID LAC2_FOMPI Reviewed; 530 AA.
AC S8FGV1;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Laccase-2 {ECO:0000303|PubMed:34116754};
DE EC=1.10.3.2 {ECO:0000269|PubMed:34116754};
DE AltName: Full=FpLCC2 {ECO:0000303|PubMed:34116754};
DE Flags: Precursor;
GN Name=LCC2 {ECO:0000303|PubMed:34116754};
GN ORFNames=FOMPIDRAFT_51906 {ECO:0000312|EMBL:EPT00641.1};
OS Fomitopsis pinicola (strain FP-58527) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fomitopsis.
OX NCBI_TaxID=743788 {ECO:0000312|Proteomes:UP000015241};
RN [1] {ECO:0000312|Proteomes:UP000015241}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FP-58527 {ECO:0000312|Proteomes:UP000015241};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=34116754; DOI=10.1016/j.enzmictec.2021.109801;
RA Csarman F., Obermann T., Zanjko M.C., Man P., Halada P., Seiboth B.,
RA Ludwig R.;
RT "Functional expression and characterization of two laccases from the brown
RT rot Fomitopsis pinicola.";
RL Enzyme Microb. Technol. 148:109801-109801(2021).
CC -!- FUNCTION: In vitro, has activity towards 2,2'-azino-bis(3-
CC ethylbenzthiazoline-6-sulfonic acid) (ABTS), 2,6-dimethoxy-phenol, and
CC guaiacol (PubMed:34116754). Although brown rot fungi preferentially
CC degrade hemicellulose and cellulose, the enzyme may contribute to
CC generating small amounts of lignin breakdown products required for
CC catalytic reactions (PubMed:34116754). {ECO:0000269|PubMed:34116754,
CC ECO:0000303|PubMed:34116754}.
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:34116754};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000305|PubMed:34116754};
CC Note=Binds 4 Cu cations per monomer. {ECO:0000250|UniProtKB:Q70KY3};
CC -!- ACTIVITY REGULATION: Inhibited by chloride ions (PubMed:34116754).
CC Inhibited by citrate (PubMed:34116754). Inhibited by oxalate
CC (PubMed:34116754). Activated by acetate (PubMed:34116754).
CC {ECO:0000269|PubMed:34116754}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20.1 uM for 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
CC (ABTS) (at pH 3.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:34116754};
CC KM=22.4 uM for 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
CC (ABTS) (at pH 5.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:34116754};
CC KM=64.4 uM for 2,6-dimethoxy-phenol (at pH 3.0 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:34116754};
CC KM=8.0 uM for 2,6-dimethoxy-phenol (at pH 5.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:34116754};
CC KM=1790.0 uM for guaiacol (at pH 3.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:34116754};
CC KM=918 uM for guaiacol (at pH 5.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:34116754};
CC Note=kcat is 315 sec(-1) with 2,2'-azino-bis(3-ethylbenzthiazoline-6-
CC sulfonic acid) (ABTS) as substrate (at pH 3.0 and 30 degrees
CC Celsius). kcat is 42.6 sec(-1) with 2,2'-azino-bis(3-
CC ethylbenzthiazoline-6-sulfonic acid) (ABTS) as substrate (at pH 5.0
CC and 30 degrees Celsius). kcat is 155 sec(-1) with 2,6-dimethoxy-
CC phenol as substrate (at pH 3.0 and 30 degrees Celsius). kcat is 14.8
CC sec(-1) with 2,6-dimethoxy-phenol as substrate (at pH 5.0 and 30
CC degrees Celsius). cat is 48 sec(-1) with guaiacol as substrate (at pH
CC 3.0 and 30 degrees Celsius). kcat is 16.7 sec(-1) with guaiacol as
CC substrate (at pH 5.0 and 30 degrees Celsius).;
CC pH dependence:
CC Optimum pH is 2.5 or below with 2,2'-azino-bis(3-ethylbenzthiazoline-
CC 6-sulfonic acid) (ABTS) or 2,6-dimethoxy-phenol as substrate, and 3.5
CC with guaiacol as substrate.;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34116754}.
CC -!- INDUCTION: Expressed during growth on spruce wood (at protein level).
CC {ECO:0000269|PubMed:34116754}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; KE504147; EPT00641.1; -; Genomic_DNA.
DR SMR; S8FGV1; -.
DR STRING; 743788.S8FGV1; -.
DR EnsemblFungi; EPT00641; EPT00641; FOMPIDRAFT_51906.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_2_1_1; -.
DR OMA; HLMYEGV; -.
DR OrthoDB; 454773at2759; -.
DR Proteomes; UP000015241; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IDA:UniProtKB.
DR Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
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; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; SSF49503; 3.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
PE 1: Evidence at protein level;
KW Copper; Disulfide bond; Glycoprotein; Metal-binding; Oxidoreductase;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..530
FT /note="Laccase-2"
FT /evidence="ECO:0000255"
FT /id="PRO_5004563660"
FT DOMAIN 36..154
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 167..311
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 379..504
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT BINDING 88
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 90
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 133
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 135
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 BINDING 428
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 431
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 433
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 BINDING 484
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 BINDING 485
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 486
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 490
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 109..520
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT DISULFID 141..228
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
SQ SEQUENCE 530 AA; 58324 MW; 669A0729701DA387 CRC64;
MLLSSAFVGS CLAILNFAAA VSAQGGLSRT TLNIVNKVIS PDGYSRDSVL ANGIHPGPLI
SGNKGDTFQI NVNNQLHDNS MNTSTTVHWH GIDQHHTNWA DGPAFVTQCP IVPEHSFLYN
FTVPDQAGTF WYHSHESVQY CDGLRGPLVV YDPEDPHKDL YDVDDDTTII SLSDWYHSPA
HELLPGPIPP NSTLINSLGR PDGSDLPVTI IEVDPTKRYR FRLISMACHP YFDFSIDGHN
MTIIEADGSN TEPLSDIDQI RIYPAQRYSF VLEPNQTPGD YWIRAAPLQL GNTSNPDTTT
SLGLAILRYT NRSGYAQAAS VDPYDISQTP IPVNPLLEQN LHAYGDVPEL DEECDDCKLT
FDFAFNFTAV DFTVNGTSYV NPTVPVLLQI LNGTYTAQEL LPHHSVYTLP RNKTIEITMP
GAVTGGPHPM HLHGHSFYVI QSMGSDTTNT VNPVLRDTVA VGGATGDNVV IRFRTDNPGP
WIMHCHIDFH LALGFAVVLA EAPQDVAEYV SPIPTWDELC PIWDNAPSHN
