LAC1_NEUCR
ID LAC1_NEUCR Reviewed; 619 AA.
AC P06811; P10574; Q7RV60;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Laccase;
DE EC=1.10.3.2 {ECO:0000250|UniProtKB:Q70KY3};
DE AltName: Full=Benzenediol:oxygen oxidoreductase;
DE AltName: Full=Diphenol oxidase;
DE AltName: Full=Urishiol oxidase;
DE Flags: Precursor;
GN Name=lacc; ORFNames=NCU04528;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Oak Ridge, and TS;
RX PubMed=2961749; DOI=10.1016/s0021-9258(19)35436-5;
RA Germann U.A., Mueller G., Hunziker P.E., Lerch K.;
RT "Characterization of two allelic forms of Neurospora crassa laccase.
RT Amino- and carboxyl-terminal processing of a precursor.";
RL J. Biol. Chem. 263:885-896(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 379-619.
RX PubMed=2947240; DOI=10.1073/pnas.83.23.8854;
RA Germann U.A., Lerch K.;
RT "Isolation and partial nucleotide sequence of the laccase gene from
RT Neurospora crassa: amino acid sequence homology of the protein to human
RT ceruloplasmin.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:8854-8858(1986).
CC -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC products. {ECO:0000250|UniProtKB:Q70KY3}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q70KY3}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; M18333; AAA33591.1; -; Genomic_DNA.
DR EMBL; M18334; AAA33592.1; -; Genomic_DNA.
DR EMBL; CM002242; EAA27703.1; -; Genomic_DNA.
DR EMBL; M14554; AAA33590.1; -; Genomic_DNA.
DR PIR; A28523; KSNCLO.
DR PIR; B28523; KSNCLT.
DR RefSeq; XP_956939.1; XM_951846.3.
DR AlphaFoldDB; P06811; -.
DR SMR; P06811; -.
DR STRING; 5141.EFNCRP00000005387; -.
DR CAZy; AA1; Auxiliary Activities 1.
DR EnsemblFungi; EAA27703; EAA27703; NCU04528.
DR GeneID; 3873077; -.
DR KEGG; ncr:NCU04528; -.
DR VEuPathDB; FungiDB:NCU04528; -.
DR HOGENOM; CLU_006504_3_2_1; -.
DR InParanoid; P06811; -.
DR OMA; LVQWLVN; -.
DR Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
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:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0046274; P:lignin catabolic 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 1: Evidence at protein level;
KW Copper; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Lignin degradation; Metal-binding; Oxidoreductase; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..49
FT /id="PRO_0000002921"
FT CHAIN 50..606
FT /note="Laccase"
FT /id="PRO_0000002922"
FT PROPEP 607..619
FT /id="PRO_0000002923"
FT DOMAIN 84..207
FT /note="Plastocyanin-like 1"
FT DOMAIN 216..373
FT /note="Plastocyanin-like 2"
FT DOMAIN 431..566
FT /note="Plastocyanin-like 3"
FT BINDING 144
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 146
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 189
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 191
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 480
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 482
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 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55..63
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT DISULFID 165..586
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT DISULFID 349..383
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT VARIANT 17
FT /note="S -> P (in strain: Oak Ridge)"
FT VARIANT 21
FT /note="G -> A (in strain: Oak Ridge)"
FT VARIANT 98
FT /note="I -> L (in strain: TS)"
FT VARIANT 114
FT /note="K -> N (in strain: TS)"
FT VARIANT 292
FT /note="S -> L (in strain: Oak Ridge)"
FT VARIANT 317
FT /note="F -> L (in strain: TS)"
FT VARIANT 320
FT /note="V -> I (in strain: TS)"
FT VARIANT 346..347
FT /note="SK -> ND (in strain: TS)"
FT VARIANT 351
FT /note="D -> T (in strain: TS)"
FT VARIANT 355
FT /note="H -> K (in strain: TS)"
FT VARIANT 374
FT /note="Q -> K (in strain: TS)"
FT VARIANT 379
FT /note="V -> P (in strain: TS)"
FT VARIANT 439
FT /note="L -> M (in strain: TS)"
SQ SEQUENCE 619 AA; 68148 MW; DD7C67B9135FC08A CRC64;
MKFLGIAALV AGLLAPSLVL GAPAPGTEGV NLLTPVDKRQ DSQAERYGGG GGGGCNSPTN
RQCWSPGFNI NTDYELGTPN TGKTRRYKLT LTETDNWIGP DGVIKDKVMM VNDKIIGPTI
QADWGDYIEI TVINKLKSNG TSIHWHGMHQ RNSNIQDGVN GVTECPIPPR GGSKVYRWRA
TQYGTSWYHS HFSAQYGNGI VGPIVINGPA SANYDVDLGP FPLTDYYYDT ADRLVLLTQH
AGPPPSNNVL FNGFAKHPTT GAGQYATVSL TKGKKHRLRL INTSVENHFQ LSLVNHSMTI
ISADLVPVQP YKVDSLFLGV GQRYDVIIDA NQAVGNYWFN VTFGGSKLCG DSDNHYPAAI
FRYQGAPKAL PTNQGVAPVD HQCLDLNDLK PVLQRSLNTN SIALNTGNTI PITLDGFVWR
VNGTAININW NKPVLEYVLT GNTNYSQSDN IVQVEGVNQW KYWLIENDPD GAFSLPHPIH
LHGHDFLILG RSPDVTAISQ TRYVFDPAVD MARLNGNNPT RRDTAMLPAK GWLLIAFRTD
NPGSWLMHCH IAWHVSGGLS NQFLERAQDL RNSISPADKK AFNDNCDAWR AYFPDNAPFP
KDDSGLRSGV KAREVKMKW
