LAC2_PODAS
ID LAC2_PODAS Reviewed; 621 AA.
AC P78722;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Laccase-2;
DE EC=1.10.3.2 {ECO:0000250|UniProtKB:Q70KY3};
DE AltName: Full=Benzenediol:oxygen oxidoreductase 2;
DE AltName: Full=Diphenol oxidase 2;
DE AltName: Full=Laccase C;
DE AltName: Full=Laccase II;
DE AltName: Full=Urishiol oxidase 2;
DE Flags: Precursor;
GN Name=LAC2;
OS Podospora anserina (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora.
OX NCBI_TaxID=2587412;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RC STRAIN=ATCC 26003;
RX PubMed=8914515; DOI=10.1007/bf02172400;
RA Fernandez-Larrea J., Stahl U.;
RT "Isolation and characterization of a laccase gene from Podospora
RT anserina.";
RL Mol. Gen. Genet. 252:539-551(1996).
CC -!- FUNCTION: Probably involved in lignin degradation and in the
CC detoxification of lignin-derived products in its natural habitat
CC (herbivorous dung), which is rich in lignin of grasses and straw.
CC Probably involved in melanin synthesis and in perithecia development.
CC {ECO:0000303|PubMed:8914515}.
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:0000250|UniProtKB:Q70KY3};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:Q70KY3};
CC Note=Binds 4 Cu cations per monomer. {ECO:0000250|UniProtKB:Q70KY3};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q70KY3}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q70KY3}.
CC -!- DEVELOPMENTAL STAGE: Low basic levels throughout the growth phase;
CC increases at least 20-fold at the beginning of the autolytic phase and
CC decreases again thereafter. {ECO:0000269|PubMed:8914515}.
CC -!- INDUCTION: Under oxidative stress on the mycelium by aromatic
CC xenobiotics (guaiacol, hydroquinone, benzoquinone), and by copper salt
CC at a concentration of 1 mM (growing mycelium).
CC {ECO:0000269|PubMed:8914515}.
CC -!- PTM: Proteolytically processed at both its N-terminus and its C-
CC terminus.
CC -!- MISCELLANEOUS: Podospora anserina contains at least 3 laccase isozymes
CC named I, II, and III. They differ in their substrate specificity,
CC number of subunits, isoelectronic point and heat stability.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; Y08827; CAA70061.1; -; Genomic_DNA.
DR PIR; S72493; S72493.
DR AlphaFoldDB; P78722; -.
DR SMR; P78722; -.
DR CAZy; AA1; Auxiliary Activities 1.
DR VEuPathDB; FungiDB:PODANS_5_1200; -.
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; IEA:UniProtKB-EC.
DR GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
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; IPR002355; Cu_oxidase_Cu_BS.
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.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 2: Evidence at transcript level;
KW Copper; Disulfide bond; Glycoprotein; Lignin degradation;
KW Melanin biosynthesis; Metal-binding; Oxidoreductase; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..48
FT /evidence="ECO:0000255"
FT /id="PRO_0000002931"
FT CHAIN 49..605
FT /note="Laccase-2"
FT /id="PRO_0000002932"
FT PROPEP 606..621
FT /evidence="ECO:0000255"
FT /id="PRO_0000002933"
FT DOMAIN 78..201
FT /note="Plastocyanin-like 1"
FT DOMAIN 210..367
FT /note="Plastocyanin-like 2"
FT DOMAIN 430..566
FT /note="Plastocyanin-like 3"
FT BINDING 138
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 140
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 183
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 185
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="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 479
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 481
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 548
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 549
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 550
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 554
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 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..57
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT DISULFID 159..586
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT DISULFID 343..377
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
SQ SEQUENCE 621 AA; 68129 MW; 79F85E2ED25C1CA7 CRC64;
MMKSFFSAAA LLLGLVAPSA VLAAPSLPGV PREVTRDLLR PVEERQSSCH TAANRACWAP
GFDINTDYEV STPNTGVTRT YTLTLTEVDN WLGPDGVVKQ KVMLVNGDIF GPTITANWGD
WIQVNVINNL RTNGTSIHWH GLHQKGTNMH DGANGVTECP IPPKGGSRIY RFRAQQYGTS
WYHSHFSAQY GNGVVGTIVV NGPASVPYDI DLGVFPITDY YHKPADVLVE ETMNGGPPPS
DTVLFKGHGK NPQTGAGKFA NVTLTPGKRH RLRIINTSTH DHFQLKLQNH TMTIIAADMV
PVQAQTVDSL FLAVGQRYDV TIDANKSVGN YWFNATFGGG LACGASLNPH PAAVFRYQGA
PNTLPTNIGT PAADANCMDL NNLTPVVSRS VPTSGFTPRP NNTLPVSLTL GGTPLFVWKV
NGSSINVDWD KPIVDYVIAQ NTSYPPQANV ITVNSVNQWT YWLIENDPTG PFSIPHPMHL
HGHDFLVVGR SPDQPAGVPQ TRYRFNPATD MALLKSSNPV RRDVAMLPAN GWLLIAFKSD
NPGAWLFHCH IAWHVSGGLS VQYLERPNDL RNGFSQADKN QHNNNCNAWR AYWPTNPFPK
IDSGLKVKKW VGEHPDWYIK N
