PFMAD_PESFW
ID PFMAD_PESFW Reviewed; 584 AA.
AC W3X7K0;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Multicopper oxidase PfmaD {ECO:0000303|PubMed:28517364};
DE EC=1.-.-.- {ECO:0000305|PubMed:28517364};
DE AltName: Full=Conidial pigment biosynthesis cluster protein D {ECO:0000303|PubMed:28517364};
DE Flags: Precursor;
GN Name=PfmaD {ECO:0000303|PubMed:28517364}; ORFNames=PFICI_07100;
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, DISRUPTION PHENOTYPE, INDUCTION, 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 INDUCTION, AND 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: Multicopper oxidase; part of the gene cluster that mediates
CC the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green
CC pigment forming a dark layer in the conidial wall that protects the
CC conidia from UV radiations (PubMed:28517364). The first step of the
CC pathway is the production of the pentaketide 1,3,6,8-
CC tetrahydroxynaphthalene (1,3,6,8-THN or T4HN) by the polyketide
CC synthase PfmaE though condensation of acetyl-CoA with malonyl-CoA. T4HN
CC is not stable and easily oxidizes into the stable form flaviolin
CC (PubMed:28517364). T4HN is also substrate of the hydroxynaphthalene
CC reductase PfmaG to yield scytalone (PubMed:28517364). The scytalone
CC dehydratase PfmaJ then reduces scytalone to 1,3,8-THN
CC (PubMed:31116900). 1,3,8-THN is then substrate of the
CC hydroxynaphthalene reductase PfmaI to yield vermelone (Probable).
CC Vermelone is further converted by the multicopper oxidase PfmaD to 1,8-
CC DHN (Probable). Finally the laccase PFICI_06862 transforms 1,8-DHN to
CC DHN-melanin (Probable). The roles of the 5-oxoprolinase PfmaA and the
CC proline iminopeptidase PfmaB within the cluster have not been
CC 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:0000269|PubMed:28517364}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q4WZB4}. Cell
CC surface {ECO:0000250|UniProtKB:Q4WZB4}.
CC -!- INDUCTION: Expression is positively regulazed by the cluster-specific
CC transcription factor pfmaF. {ECO:0000269|PubMed:28517364,
CC ECO:0000269|PubMed:31116900}.
CC -!- DISRUPTION PHENOTYPE: Does not affect the production of scytalone.
CC {ECO:0000269|PubMed:28517364}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; KI912112; ETS82098.1; -; Genomic_DNA.
DR RefSeq; XP_007833872.1; XM_007835681.1.
DR AlphaFoldDB; W3X7K0; -.
DR SMR; W3X7K0; -.
DR STRING; 1229662.W3X7K0; -.
DR EnsemblFungi; ETS82098; ETS82098; PFICI_07100.
DR GeneID; 19272113; -.
DR KEGG; pfy:PFICI_07100; -.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_7_3_1; -.
DR OMA; GNLHPWH; -.
DR OrthoDB; 525810at2759; -.
DR UniPathway; UPA00785; -.
DR Proteomes; UP000030651; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; 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:0006811; P:ion transport; IEA:InterPro.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd13877; CuRO_2_Fet3p_like; 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; IPR044130; CuRO_2_Fet3-like.
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; 2.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 2: Evidence at transcript level;
KW Copper; Melanin biosynthesis; Metal-binding; Oxidoreductase;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..584
FT /note="Multicopper oxidase PfmaD"
FT /id="PRO_5004834759"
FT DOMAIN 29..144
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 154..277
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 364..491
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT REGION 426..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 79
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 81
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 411
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 414
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 416
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 472
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 473
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 474
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 478
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
SQ SEQUENCE 584 AA; 64884 MW; E39C79F8CFDD877C CRC64;
MWTARLSSIA VLTQVVGTWA DTITLNWEIT WVNAAPDGFH RPVIGVNGKW PCPPIHATVG
DTVVINMKNS LGNQTTGLHF HGINQLDTNY MDGASMVNSC PVVPGSSMTY SFTADEPGTY
WYHSHNMAQY PDGLRGPLII HDDNDPFDGE FDNEVILTIS DWYHQQTLTL VQNMLVSSND
QWRPPLPDGM IVNEGGNTDI ELDIGTTTRV RILNFGALTA FMLRFGSRDM DVIMTDASYV
QRETIHQLRI APGQRYDVLV SATKKDKGKN IPYLISMDLN RDFTVSGTWT FNQTGYLITD
AKAPCTAKEV VQQWRPFDEA LFTPLDEMPL LGPLDRTWTL NFALCKDMNN IPRMCFNDQT
YVMQKTPTLY TAATVGNANT DPSVYGAVLP FIIEYGDVLE IVINNLDPAI HPFHLHGHQF
QVVERPESGS GSFDGSSTAN PVPPRRDVIS INGGSYARLR ITADNPGVFL FHCHIEWHVE
MGLTATLIEA PEMLDGYDIP QAMIDSCKAQ GYPVAGNAAG DTINVWDDSG YLTDPPSTYS
GSQWPVPKGG NSQKSRPRRK PSGQSSQTRQ ISNMSGEFQH RITW
