PFMAY_PESFW
ID PFMAY_PESFW Reviewed; 592 AA.
AC W3X732;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Laccase PFICI_06862 {ECO:0000303|PubMed:28517364};
DE EC=1.10.3.- {ECO:0000305|PubMed:28517364};
DE AltName: Full=Conidial pigment biosynthesis oxidase PFICI_06862 {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=PFICI_06862;
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140;
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
RN [2]
RP FUNCTION, AND PATHWAY.
RX PubMed=28517364; DOI=10.1111/mmi.13711;
RA Zhang P., Wang X., Fan A., Zheng Y., Liu X., Wang S., Zou H., Oakley B.R.,
RA Keller N.P., Yin W.B.;
RT "A cryptic pigment biosynthetic pathway uncovered by heterologous
RT expression is essential for conidial development in Pestalotiopsis fici.";
RL Mol. Microbiol. 105:469-483(2017).
RN [3]
RP FUNCTION.
RX PubMed=31116900; DOI=10.1111/mmi.14281;
RA Zhang P., Zhou S., Wang G., An Z., Liu X., Li K., Yin W.B.;
RT "Two transcription factors cooperatively regulate DHN melanin biosynthesis
RT and development in Pestalotiopsis fici.";
RL Mol. Microbiol. 112:649-666(2019).
CC -!- FUNCTION: Laccase involved the biosynthesis of dihydroxynaphthalene
CC (DHN)-melanin, a bluish-green pigment forming a dark layer in the
CC conidial wall that protects the conidia from UV radiations
CC (PubMed:28517364). The first step of the pathway is the production of
CC the pentaketide 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN or T4HN)
CC by the polyketide synthase PfmaE though condensation of acetyl-CoA with
CC malonyl-CoA. T4HN is not stable and easily oxidizes into the stable
CC form flaviolin (PubMed:28517364). T4HN is also substrate of the
CC hydroxynaphthalene reductase PfmaG to yield scytalone
CC (PubMed:28517364). The scytalone dehydratase PfmaJ then reduces
CC scytalone to 1,3,8-THN (PubMed:31116900). 1,3,8-THN is then substrate
CC of the hydroxynaphthalene reductase PfmaI to yield vermelone
CC (Probable). Vermelone is further converted by the multicopper oxidase
CC PfmaD to 1,8-DHN (Probable). Finally the laccase PFICI_06862 transforms
CC 1,8-DHN to DHN-melanin (Probable). The roles of the 5-oxoprolinase
CC PfmaA and the proline iminopeptidase PfmaB within the cluster have not
CC been elucidated yet (Probable). {ECO:0000269|PubMed:28517364,
CC ECO:0000269|PubMed:31116900, ECO:0000305|PubMed:28517364,
CC ECO:0000305|PubMed:31116900}.
CC -!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
CC {ECO:0000305|PubMed:28517364}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250|UniProtKB:E9RBR0}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; KI912112; ETS81860.1; -; Genomic_DNA.
DR RefSeq; XP_007833634.1; XM_007835443.1.
DR AlphaFoldDB; W3X732; -.
DR SMR; W3X732; -.
DR STRING; 1229662.W3X732; -.
DR EnsemblFungi; ETS81860; ETS81860; PFICI_06862.
DR GeneID; 19271875; -.
DR KEGG; pfy:PFICI_06862; -.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_5_4_1; -.
DR OMA; DEHEFYV; -.
DR OrthoDB; 454773at2759; -.
DR UniPathway; UPA00785; -.
DR Proteomes; UP000030651; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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.
PE 3: Inferred from homology;
KW Copper; Glycoprotein; Melanin biosynthesis; Metal-binding; Oxidoreductase;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..592
FT /note="Laccase PFICI_06862"
FT /evidence="ECO:0000255"
FT /id="PRO_5004834745"
FT DOMAIN 32..142
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 173..350
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 445..563
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT BINDING 78
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 80
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 123
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 125
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 475
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 592 AA; 66213 MW; C9ED63FCAFEC1542 CRC64;
MYIQTQFASL LLLAGTSLAS QVRKYNFTIT SQWSSGDGHG RPVFMINGQS PGPLIEADEG
DEIEVFVDNQ LAAETTMHWH GIYQIDRPWN DGVPGVTQYS MQPRDTYTYR FTVQQQYGSY
FYHGHFGPAF ADGMRGPMWI APAAWRPRPY ELISDSSHDV EQMKKAEKHP FHVVISDWNA
EPMDILLVMY RDTGIVPWCS NSIVLNGKGR TYCHSAELIE SVGGPGRNTL GCLMQPDQEL
YSNEQVCEAT QTDLEIFQAE EGHEWIWINF IHSGAHHELQ ISVDEHEIVV VAADGEFTYP
QRVHAANCNL GERISILVHL NQKPGDYAIR VTSLRQEQVI QGLGILRYPG SSHGAQEAEP
PATKPWVHLN GTLISDKLQQ MDEMKLAPFP SRPPPPQSDH TLKFFVNMTG TGSWALNIGP
HQAFRQQLPP LLWEEDSRGV TTYESDVQGG SMQNGSVVDI IFTNGANVNS QHPFHKHNNK
AWVIGTGTGG FPWDTVDEAI QQGGMADSFN FVDPPIRDGC RLGNTTGDWT VIRYDIAFPA
ASMLHCHMIH HFGAGQQVVL LEGVESMAKI PAEMKDRVHS NFRPPLRYGP LD
