LAC1_FOMPI
ID LAC1_FOMPI Reviewed; 539 AA.
AC S8FIE4;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Laccase-1 {ECO:0000303|PubMed:34116754};
DE EC=1.10.3.2 {ECO:0000269|PubMed:34116754};
DE AltName: Full=FpLCC1 {ECO:0000303|PubMed:34116754};
DE Flags: Precursor;
GN Name=LCC1 {ECO:0000303|PubMed:34116754};
GN Synonyms=Fplcc4 {ECO:0000312|EMBL:EPT01171.1};
GN ORFNames=FOMPIDRAFT_45001 {ECO:0000312|EMBL:EPT01171.1};
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=59.5 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=50.9 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=448.0 uM for 2,6-dimethoxy-phenol (at pH 3.0 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:34116754};
CC KM=35.1 uM for 2,6-dimethoxy-phenol (at pH 5.0 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:34116754};
CC KM=2140.0 uM for guaiacol (at pH 3.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:34116754};
CC KM=891 uM for guaiacol (at pH 5.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:34116754};
CC Note=kcat is 409 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 23.1 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 102 sec(-1) with 2,6-dimethoxy-
CC phenol as substrate (at pH 3.0 and 30 degrees Celsius). kcat is 7.89
CC sec(-1) with 2,6-dimethoxy-phenol as substrate (at pH 5.0 and 30
CC degrees Celsius). cat is 85.1 sec(-1) with guaiacol as substrate (at
CC pH 3.0 and 30 degrees Celsius). kcat is 13.2 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 poplar 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; KE504144; EPT01171.1; -; Genomic_DNA.
DR SMR; S8FIE4; -.
DR STRING; 743788.S8FIE4; -.
DR EnsemblFungi; EPT01171; EPT01171; FOMPIDRAFT_45001.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_2_1_1; -.
DR OMA; MMKTTTR; -.
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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..539
FT /note="Laccase-1"
FT /evidence="ECO:0000255"
FT /id="PRO_5004563691"
FT DOMAIN 37..154
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 166..309
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 374..495
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 421
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 424
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 426
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 476
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 477
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 478
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 482
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 78
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 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 233
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 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 109..513
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT DISULFID 141..228
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
SQ SEQUENCE 539 AA; 58991 MW; 07BA54A0B8AC63DD CRC64;
MAFTAISLFL AALGVINTAF AQSAVIGPVT DLDIINAEVN LDGFPRQAVL AGGTFPGPLI
KGNKGDNFRI NVHDFLYNET MDVTTTIHWH GIFQRHTNWA DGPAFVTQCP IAPGNSFLYN
FTVPNQAGTF WYHSHEGLQY CDGLRGPFVV YDPEDPHRDL YDVDDESTVI TLADWYHEAA
SLIVPPADPD SVLINGRGRQ ANDTTSPLAV INVEYGKRYR IRLISVSCDP YFNFTIDGHN
FTIIEADGEN TDPLPGVDQI QIFAAQRYSF ILDANQPIDN YWIRVIPEQV GANGTAATPP
GLAVLHYLGA PPFDPKANAS QVPISVNPLL EQNLHALGAT GVPDLDPSCA ECNITLDFTF
NTPLFFVNGV TYKSPTVPVL LQILNGSFTA QDLMPEGSVY TLPRNKTIQI NMPGGVLGIP
HPLHLHGHSF SVIRSANSDE TNLYNPVRRD TVSIGTNGSF VAIRFTTDNP GPWFLHCHID
FHLAAGFAVV MAEDPMDVPG YVKPIPPAWD KLCPIYDALP ANEQILQPEA ANLSTYPQK
