PFMAG_PESFW
ID PFMAG_PESFW Reviewed; 277 AA.
AC W3XAA0;
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=Tetrahydroxynaphthalene reductase PfmaG {ECO:0000303|PubMed:31116900};
DE EC=1.1.1.252 {ECO:0000269|PubMed:31116900};
DE AltName: Full=Conidial pigment biosynthesis cluster protein G {ECO:0000303|PubMed:28517364};
GN Name=PfmaG {ECO:0000303|PubMed:28517364}; ORFNames=PFICI_07103;
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, 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: Tetrahydroxynaphthalene reductase; part of the gene cluster
CC that mediates the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a
CC bluish-green pigment forming a dark layer in the conidial wall that
CC protects the conidia from UV radiations (PubMed:28517364). The first
CC step of the 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 -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + scytalone = H(+) + NADPH + naphthalene-1,3,6,8-
CC tetrol; Xref=Rhea:RHEA:21908, ChEBI:CHEBI:15378, ChEBI:CHEBI:16945,
CC ChEBI:CHEBI:18365, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.252; Evidence={ECO:0000269|PubMed:31116900};
CC -!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
CC {ECO:0000269|PubMed:28517364, ECO:0000269|PubMed:31116900}.
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: Abolishes the production of scytalone.
CC {ECO:0000269|PubMed:28517364}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; KI912112; ETS82101.1; -; Genomic_DNA.
DR RefSeq; XP_007833875.1; XM_007835684.1.
DR AlphaFoldDB; W3XAA0; -.
DR SMR; W3XAA0; -.
DR STRING; 1229662.W3XAA0; -.
DR EnsemblFungi; ETS82101; ETS82101; PFICI_07103.
DR GeneID; 19272116; -.
DR KEGG; pfy:PFICI_07103; -.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_3_1; -.
DR OMA; KHMVDAG; -.
DR OrthoDB; 913128at2759; -.
DR UniPathway; UPA00785; -.
DR Proteomes; UP000030651; Unassembled WGS sequence.
DR GO; GO:0047039; F:tetrahydroxynaphthalene reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Melanin biosynthesis; NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..277
FT /note="Tetrahydroxynaphthalene reductase PfmaG"
FT /id="PRO_0000445353"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 28..36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 56..57
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 81..83
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 173..177
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 206..208
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
SQ SEQUENCE 277 AA; 29271 MW; 2189B82652992463 CRC64;
MSPSAIHNIT SDLPSSQQHR PFAGKVALIT GSGRGIGRGI ALELGKRGAS CIINYAKSAG
AANEVVAELA KLGSKSIALQ ADISKPADVA ALFEKALKHY GHIDFAISNS GMEVWCEETE
VTPELFDQVF NLNTRGQFFV AQNALKHCSE GGRIILTSSI AAQMTGIPNH ALYAGSKAAV
EGFARSFAVD CGRKRITCNA LAPGGIQTDM FDENSWHYVP GGYQGMNIDT IKDGLAKMCP
LNRVGTPADI GKIVCMLVSD EGEWINGQVL RCSGGGV
