PFMAJ_PESFW
ID PFMAJ_PESFW Reviewed; 191 AA.
AC W3XEE6;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Scytalone dehydratase PfmaJ {ECO:0000303|PubMed:31116900};
DE EC=4.2.1.94 {ECO:0000305|PubMed:28517364};
DE AltName: Full=Conidial pigment biosynthesis protein J {ECO:0000303|PubMed:31116900};
GN Name=Pfmaj {ECO:0000303|PubMed:31116900}; ORFNames=PFICI_02498;
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 INDUCTION, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
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: Scytalone dehydratase involved the biosynthesis of
CC dihydroxynaphthalene (DHN)-melanin, a bluish-green pigment forming a
CC dark layer in the conidial wall that protects the conidia from UV
CC radiations (PubMed:28517364). The first step of the pathway is the
CC production of the pentaketide 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-
CC THN or T4HN) by the polyketide synthase PfmaE though condensation of
CC acetyl-CoA with malonyl-CoA. T4HN is not stable and easily oxidizes
CC into the stable form flaviolin (PubMed:28517364). T4HN is also
CC substrate of the 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 -!- CATALYTIC ACTIVITY:
CC Reaction=scytalone = 1,3,8-trihydroxynaphthalene + H2O;
CC Xref=Rhea:RHEA:24396, ChEBI:CHEBI:15377, ChEBI:CHEBI:16945,
CC ChEBI:CHEBI:18393; EC=4.2.1.94;
CC Evidence={ECO:0000269|PubMed:31116900};
CC -!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
CC {ECO:0000269|PubMed:31116900}.
CC -!- SUBUNIT: Homotrimer (By similarity). Each subunit contains an active
CC site, located in the central part of the hydrophobic core of the
CC monomer, which functions independently (By similarity).
CC {ECO:0000250|UniProtKB:P56221}.
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250|UniProtKB:P56221}.
CC -!- INDUCTION: Expression is positively regulazed by the cluster-specific
CC transcription factor pfmaF. {ECO:0000269|PubMed:31116900}.
CC -!- SIMILARITY: Belongs to the scytalone dehydratase family. {ECO:0000305}.
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DR EMBL; KI912110; ETS84473.1; -; Genomic_DNA.
DR RefSeq; XP_007829270.1; XM_007831079.1.
DR AlphaFoldDB; W3XEE6; -.
DR SMR; W3XEE6; -.
DR STRING; 1229662.W3XEE6; -.
DR EnsemblFungi; ETS84473; ETS84473; PFICI_02498.
DR GeneID; 19267511; -.
DR KEGG; pfy:PFICI_02498; -.
DR eggNOG; ENOG502SNND; Eukaryota.
DR HOGENOM; CLU_101889_0_0_1; -.
DR OMA; RKCIAPT; -.
DR OrthoDB; 1377897at2759; -.
DR UniPathway; UPA00785; -.
DR Proteomes; UP000030651; Unassembled WGS sequence.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030411; F:scytalone dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR004235; Scytalone_dehydratase.
DR Pfam; PF02982; Scytalone_dh; 1.
DR PIRSF; PIRSF024851; SCD1; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
PE 1: Evidence at protein level;
KW Endosome; Lyase; Melanin biosynthesis; Reference proteome.
FT CHAIN 1..191
FT /note="Scytalone dehydratase PfmaJ"
FT /id="PRO_0000445356"
FT ACT_SITE 80
FT /evidence="ECO:0000250|UniProtKB:P56221"
FT ACT_SITE 105
FT /evidence="ECO:0000250|UniProtKB:P56221"
FT BINDING 25
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P56221"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P56221"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P56221"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P56221"
SQ SEQUENCE 191 AA; 21808 MW; E3AB81A9509C48FC CRC64;
MVNGNITFDD YLGLQQCLVE WADSYDSKDW SRLRKCIAPT LRIDYRSFLD KLWEAMPAEE
FIAMISDKAV LGDPLLMTQH FIGGTKWEKI SDTEVVGVHQ LRVPHQRYTD ETRSTVAVKG
HAHSTNTHWY RKVNGEWKFA GLCPEIRWGE FDFDKVFASG REAFGTEDTA AEGISAKHQQ
QQHGRVTVSA V
