USTL_USTVR
ID USTL_USTVR Reviewed; 653 AA.
AC A0A4Y6F0M8; A0A063C933; A0A1B5L626;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 1.
DT 03-AUG-2022, entry version 10.
DE RecName: Full=Laccase ustL {ECO:0000303|PubMed:31050129};
DE EC=1.10.3.- {ECO:0000269|PubMed:31050129};
DE AltName: Full=Ustilaginoidins biosynthesis cluster protein L {ECO:0000303|PubMed:31050129};
DE Flags: Precursor;
GN Name=ustL {ECO:0000303|PubMed:31050129}; ORFNames=UV8b_2091, UVI_02036220;
OS Ustilaginoidea virens (Rice false smut fungus) (Villosiclava virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Ustilaginoidea.
OX NCBI_TaxID=1159556;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=IPU010;
RX PubMed=31050129; DOI=10.1002/anie.201903759;
RA Obermaier S., Thiele W., Fuertges L., Mueller M.;
RT "Enantioselective phenol coupling by laccases in the biosynthesis of fungal
RT dimeric naphthopyrones.";
RL Angew. Chem. Int. Ed. 58:9125-9128(2019).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UV-8b;
RX PubMed=24846013; DOI=10.1038/ncomms4849;
RA Zhang Y., Zhang K., Fang A., Han Y., Yang J., Xue M., Bao J., Hu D.,
RA Zhou B., Sun X., Li S., Wen M., Yao N., Ma L.J., Liu Y., Zhang M.,
RA Huang F., Luo C., Zhou L., Li J., Chen Z., Miao J., Wang S., Lai J.,
RA Xu J.R., Hsiang T., Peng Y.L., Sun W.;
RT "Specific adaptation of Ustilaginoidea virens in occupying host florets
RT revealed by comparative and functional genomics.";
RL Nat. Commun. 5:3849-3849(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IPU010;
RX PubMed=27151791; DOI=10.1128/genomea.00306-16;
RA Kumagai T., Ishii T., Terai G., Umemura M., Machida M., Asai K.;
RT "Genome sequence of Ustilaginoidea virens IPU010, a rice pathogenic fungus
RT causing false smut.";
RL Genome Announc. 4:0-0(2016).
CC -!- FUNCTION: Laccase; part of the gene cluster that mediates the
CC biosynthesis of ustilaginoidins, dimeric gamma-naphthopyrones isolated
CC from different fungal species (PubMed:31050129). The first step in the
CC biosynthesis of ustilaginoidins is the production of gamma-
CC naphthopyrone precursor YWA1 by the non-reducing polyketide synthase
CC ustP, via condensation of one acetyl-CoA starter unit with 6 malonyl-
CC CoA units (PubMed:31050129). YWA1 is then probably substrate of the
CC ustZ to yield norrubrofusarin via a dehydration reaction (Probable). A
CC key enzyme in the biosynthetic pathway is the laccase ustL, which
CC catalyzes the oxidative dimerization of norrubrofusarin to
CC ustilaginoidin A (PubMed:31050129). It can produce the M- and P-
CC atropisomers in varying amounts, depending on the reaction conditions
CC (PubMed:31050129). For the biosynthesis of 3-methylustilaginoid in
CC derivatives such as chaetochromin A, a methylated derivative of YWA1 is
CC required (Probable). The C-methylation is considered to be catalyzed by
CC ustM, the phosphopantetheine attachment site of which indicates that it
CC acts on the growing polyketide chain before release of the product
CC (Probable). For the biosynthesis of chaetochromin A, it is assumed that
CC saturation of the D2 double bond takes place before dimerization, and
CC is probably catalyzed by an external reductase because no candidate
CC gene was identified within the cluster (Probable).
CC {ECO:0000269|PubMed:31050129, ECO:0000305|PubMed:31050129}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 norrubrofusarin + O2 = 2 H2O + 2 ustilaginoidin A;
CC Xref=Rhea:RHEA:62688, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:145839, ChEBI:CHEBI:145840;
CC Evidence={ECO:0000269|PubMed:31050129};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62689;
CC Evidence={ECO:0000269|PubMed:31050129};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:31050129}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=GAO19027.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=KDB16999.1; Type=Erroneous gene model prediction; Evidence={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; MK210203; QDF21479.1; -; mRNA.
DR EMBL; JHTR01000008; KDB16999.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BBTG02000019; GAO19027.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A0A4Y6F0M8; -.
DR SMR; A0A4Y6F0M8; -.
DR STRING; 1159556.A0A4Y6F0M8; -.
DR EnsemblFungi; KDB16999; KDB16999; UV8b_2091.
DR HOGENOM; CLU_006504_5_0_1; -.
DR OrthoDB; 454773at2759; -.
DR Proteomes; UP000054053; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; 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; Glycoprotein; Metal-binding; Oxidoreductase; Repeat; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..653
FT /note="Laccase ustL"
FT /id="PRO_0000448922"
FT DOMAIN 31..143
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 173..362
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 463..594
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
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 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 277
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 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 623
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 653 AA; 72757 MW; D1A622239BC0A1D9 CRC64;
MTSLTGLALL LCVLASQSWA ARVQKTLRIA WEKGAPNGQS REMIFTNGVF PGPELIFDED
DDVEITVHND MNRNTTVHWH GIAQEGTPWA DGVIGLSQQP IRPGESFVYR FKASPPGTHW
YHSHERMTLV DGLHGAFFIR PKRDMKDLWS KISNDPKDID AMSKAALDPK LMVLSDWSRF
TSEEYWKAIE DSKLLLFCVD SILLNGHGEV YCPPQEFLVN QTQWGPQHFT FPDQNVTDKG
CFPAVEEGIQ GPWVNQSLPE KIPAHIQSGC VPSAGSNYTV EVDPADGWVS MNFIAAASNK
QVDFSIDEHP MWIYEVDGNY VQPHKFVAAA ITAGERFSVM VKLDKQPGRY TIRLPDSGAT
QVISGFANMV YKGAEHVSPP TKPYVTYGGL SGRPETDTES YAPYNISADY MPPWPANPPA
ATADEEYLLV MGRAGSSFQY TMNTNYLYPM DFKADRPLLH YPNQTVGTED EKLVIRTKNG
SWVDLILQVA VLPGDGAAFE HMMHKHGSKT WRIGNGAGVW KYKSVAEAIA AEPESFNLKD
PGLRDSWLTM FSPVPAGGYW SVFRYQVTNP GPWLFHCHFE LHAMGGMSIA LLDGVDVWPQ
VPEEYAVRHH PSQGTQTLAA TPNASKPWYN GMLNFMQAVL GILPGQGSEE LRR
