LMCO1_MYCTT
ID LMCO1_MYCTT Reviewed; 650 AA.
AC G2QFD0;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Laccase-like multicopper oxidase 1 {ECO:0000303|PubMed:21964414};
DE Short=LMCO {ECO:0000303|PubMed:30529567};
DE EC=1.-.-.- {ECO:0000269|PubMed:30529567};
DE Flags: Precursor;
GN Name=LMCO1 {ECO:0000303|PubMed:30529567}; ORFNames=MYCTH_2063133;
OS Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799)
OS (Sporotrichum thermophile).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothelomyces.
OX NCBI_TaxID=573729;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42464 / BCRC 31852 / DSM 1799;
RX PubMed=21964414; DOI=10.1038/nbt.1976;
RA Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., Reid I.,
RA Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., Coutinho P.M.,
RA Lombard V., Natvig D.O., Lindquist E., Schmutz J., Lucas S., Harris P.,
RA Powlowski J., Bellemare A., Taylor D., Butler G., de Vries R.P.,
RA Allijn I.E., van den Brink J., Ushinsky S., Storms R., Powell A.J.,
RA Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., LaBoissiere S.,
RA Clutterbuck A.J., Martinez D., Wogulis M., de Leon A.L., Rey M.W.,
RA Tsang A.;
RT "Comparative genomic analysis of the thermophilic biomass-degrading fungi
RT Myceliophthora thermophila and Thielavia terrestris.";
RL Nat. Biotechnol. 29:922-927(2011).
RN [2]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND BIOTECHNOLOGY.
RX PubMed=30529567; DOI=10.1016/j.nbt.2018.12.001;
RA Zerva A., Koutroufini E., Kostopoulou I., Detsi A., Topakas E.;
RT "A novel thermophilic laccase-like multicopper oxidase from
RT Thermothelomyces thermophila and its application in the oxidative
RT cyclization of 2',3,4-trihydroxychalcone.";
RL New Biotechnol. 49:10-18(2019).
CC -!- FUNCTION: Yellow laccase-like multicopper oxidase that is able to
CC oxidize a variety of phenolic compounds including standard laccase
CC substrates such as 2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic
CC acid) (ABTS) and 2,6-dimethoxyphenol (2,6-DMP) (PubMed:30529567). Can
CC be used for the bioconversion of 2',3,4-trihy-droxychalcone to 3',4'-
CC dihydroxy-aurone, a bioactive aurone recently shown to possess
CC inhibitory activity against several isoforms of the histone deacetylase
CC complex (HDAC) (PubMed:30529567). {ECO:0000269|PubMed:30529567}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2',3,4-trihydroxy-trans-chalcone + 2 H(+) + O2 = 2 3',4'-
CC dihydroxyaurone + 2 H2O; Xref=Rhea:RHEA:63848, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:144744,
CC ChEBI:CHEBI:144745; Evidence={ECO:0000269|PubMed:30529567};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63849;
CC Evidence={ECO:0000269|PubMed:30529567};
CC -!- ACTIVITY REGULATION: Retains almost half of its activity in presence of
CC high salt concentrations up to 100 mM NaCl (PubMed:30529567). Retains
CC also more than 85% of its original activity in the presence of 1 mM
CC EDTA, indicating a satisfactory resistance towards chelators, which is
CC rare among metal-containing enzyme (PubMed:30529567). The activity
CC drops significantly in the presence of NaN(3) or SDS (PubMed:30529567).
CC Appears more active in the presence of methanol compared to ethanol,
CC but acetone or DMSO addition severely affect remaining laccase activity
CC (PubMed:30529567). {ECO:0000269|PubMed:30529567}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.37 mM for ABTS {ECO:0000269|PubMed:30529567};
CC KM=2.41 mM for 2,6-dimethoxyphenol {ECO:0000269|PubMed:30529567};
CC pH dependence:
CC Optimum pH is 4.0. {ECO:0000269|PubMed:30529567};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:30529567};
CC -!- BIOTECHNOLOGY: The thermophilic yellow LMCO1 presents a number of
CC superior properties with potential use in industrial biocatalysis via
CC its ability to oxidize a variety of phenolic compounds.
CC {ECO:0000269|PubMed:30529567}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003005; AEO59159.1; -; Genomic_DNA.
DR RefSeq; XP_003664404.1; XM_003664356.1.
DR AlphaFoldDB; G2QFD0; -.
DR SMR; G2QFD0; -.
DR STRING; 573729.G2QFD0; -.
DR EnsemblFungi; AEO59159; AEO59159; MYCTH_2063133.
DR GeneID; 11514269; -.
DR KEGG; mtm:MYCTH_2063133; -.
DR VEuPathDB; FungiDB:MYCTH_2063133; -.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_8_3_1; -.
DR InParanoid; G2QFD0; -.
DR OrthoDB; 454773at2759; -.
DR Proteomes; UP000007322; Chromosome 4.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd13895; CuRO_3_AAO_like_2; 1.
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 InterPro; IPR035666; MCO_CuRO_3.
DR InterPro; IPR017762; Multicopper_oxidase_fun.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR PANTHER; PTHR11709:SF136; PTHR11709:SF136; 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 TIGRFAMs; TIGR03390; ascorbOXfungal; 1.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 1: Evidence at protein level;
KW Copper; Glycoprotein; Metal-binding; Oxidoreductase; Reference proteome;
KW Repeat; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..650
FT /note="Laccase-like multicopper oxidase 1"
FT /id="PRO_5003435549"
FT DOMAIN 41..151
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 162..360
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 439..595
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT BINDING 87
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 89
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 133
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 135
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 501
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 504
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 506
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 576
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 577
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 578
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 582
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 650 AA; 72050 MW; 3ACD2494280A299D CRC64;
MLLSKLSILL AKWLSVAVYA GTLVHDEQFI PDHILRVSVA QVPSACENRE DVVVNGTSPG
PAIHLLPGAR TWIRVYNDMN DRNLSMHWHG LSQRFAPFSD GTPSATQWPI PPGHFFDYEI
LTEPEDAGTY FYHSHVGMQA LSCTGPLIVE DCGSSPYHYD DERILLFQDH FQKSDLEMIQ
GLTSTQFTWT GETRGILLNG RGVSPNQAAV QGRPGEASGF FGSHRFSNFR AGDGTSNSWD
GIRGDDQIEP PTDCTLPVID VEPGKTYRLR FIGATGLSLL TMGFEDHNDL TIVQVDGSEY
NAPVTVDHIQ LGGGQRFDVL LRTKTAEELR CNGDKTTYFL QFETRDRPDP YRGYGVLRYN
LGTPVPAAPT TPALTLPAEV NNWLEYTFQP LHPSSSLSPT AEEVTRRVIL EAEQKIDPAT
GRLVWKLAHM TWTDMSRDKP VLVDIYERGE AAMPDYAAAL TNYGWDPATK LFPAKKDEVL
EIVIQNTGSH YSGASGIVET HPFHAHGQHF YDVGSGPGKY DPEANNAKLA SLGYRPIKRD
TTMVYRYGEG KVAPGEPAGW RAWRMKMNNP GVWMVHCHIL AHMIMGMETI WVVGDAEDIV
TIPLSVSQNY FTYGGSVYGN DTHAPEVYHY FDDTNKCCAA GAGDSEDSGH
