ID A0A498KEZ2_MALDO Unreviewed; 623 AA.
AC A0A498KEZ2;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Laccase {ECO:0000256|ARBA:ARBA00012297, ECO:0000256|RuleBase:RU361119};
DE EC=1.10.3.2 {ECO:0000256|ARBA:ARBA00012297, ECO:0000256|RuleBase:RU361119};
DE AltName: Full=Benzenediol:oxygen oxidoreductase {ECO:0000256|RuleBase:RU361119};
DE AltName: Full=Diphenol oxidase {ECO:0000256|RuleBase:RU361119};
DE AltName: Full=Urishiol oxidase {ECO:0000256|RuleBase:RU361119};
GN ORFNames=DVH24_038386 {ECO:0000313|EMBL:RXI04112.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXI04112.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXI04112.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXI04112.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC products. {ECO:0000256|RuleBase:RU361119}.
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:0000256|ARBA:ARBA00000349,
CC ECO:0000256|RuleBase:RU361119};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|RuleBase:RU361119};
CC Note=Binds 4 Cu cations per monomer. {ECO:0000256|RuleBase:RU361119};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000256|ARBA:ARBA00004271, ECO:0000256|RuleBase:RU361119}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609, ECO:0000256|RuleBase:RU361119}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXI04112.1}.
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DR EMBL; RDQH01000329; RXI04112.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498KEZ2; -.
DR STRING; 3750.A0A498KEZ2; -.
DR Proteomes; UP000290289; Chromosome 3.
DR GO; GO:0048046; C:apoplast; 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 CDD; cd13849; CuRO_1_LCC_plant; 1.
DR CDD; cd13875; CuRO_2_LCC_plant; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR001117; Cu-oxidase_2nd.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR034288; CuRO_1_LCC.
DR InterPro; IPR034285; CuRO_2_LCC.
DR InterPro; IPR017761; Laccase.
DR NCBIfam; TIGR03389; laccase; 1.
DR PANTHER; PTHR11709:SF68; LACCASE-13; 1.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 2.
DR SUPFAM; SSF49503; Cupredoxins; 3.
PE 3: Inferred from homology;
KW Apoplast {ECO:0000256|ARBA:ARBA00022523, ECO:0000256|RuleBase:RU361119};
KW Copper {ECO:0000256|RuleBase:RU361119};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Lignin degradation {ECO:0000256|ARBA:ARBA00023185,
KW ECO:0000256|RuleBase:RU361119};
KW Metal-binding {ECO:0000256|RuleBase:RU361119};
KW Oxidoreductase {ECO:0000256|RuleBase:RU361119};
KW Reference proteome {ECO:0000313|Proteomes:UP000290289};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU361119};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU361119};
KW Signal {ECO:0000256|RuleBase:RU361119}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU361119"
FT CHAIN 25..623
FT /note="Laccase"
FT /evidence="ECO:0000256|RuleBase:RU361119"
FT /id="PRO_5019614366"
FT DOMAIN 33..85
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 117..179
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 192..343
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 450..565
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 623 AA; 69168 MW; EB0E9FFF268F3F98 CRC64;
MEASTFTLLL GLAFLTFLAS FSAAEDHFHE FVVEAKPVRR LCRTHTTITV NGQFPGPTLE
VRNGDSIAVK VTNRAKYNIT IHWYSFIIVY DSFEFSAVAK RSHLVQWQMP SPMSGRHGLK
QQRNPWADGP EYVTQCPIQP GATYTYRFTI TDQEGTLWWH AHSRWLRATV YGALIIYPRL
GSPYPFPMPK REVPLLLGEW FDRNPLDVQR LAAFTGGAPN VSDAYTINGQ PGDLYRCSKQ
ETIRIPVESG ESLLLRVVNS ALNQELFFTV ANHQLTVVSA DAAYTKPFTT RVIMLGPGQT
TDVLVTANQP PARYYVAARA YQTAQNAPFD NTTTTAILEY KNAACSKNGK PLAPLLPRLP
AYNDTATSTA FTAQLKSPSQ VKVPTQIDEN LYFIVGLGLN NCTVPNSPRC QGPNNTRFAA
SMNNVSFVFP RSTSLMQAAY SGVPGVFTTD FPPVPPVQFN YTGNVPRGLW SPRRGTKLYK
LKYGANVQIV LQDTSIVTTE DHPMHLHGYH FYVIGSGFGN YNPRTDPAKF NLIDPPQRNT
IGTPPGGWVA IRFKADNPGN MLISCLADAL SLRCTSLPGF GNGFSSRERK RTTTVCNSSS
SRSTAMLNYQ QKITLVVGFH YRN
//
