PFMAI_PESFW
ID PFMAI_PESFW Reviewed; 282 AA.
AC W3XC32;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Trihydroxynaphthalene reductase PfmaI {ECO:0000303|PubMed:31116900};
DE EC=1.1.1.- {ECO:0000305|PubMed:31116900};
DE AltName: Full=Conidial pigment biosynthesis protein I {ECO:0000303|PubMed:31116900};
GN Name=Pfmaj {ECO:0000303|PubMed:31116900}; ORFNames=PFICI_05460;
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.
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, 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: Trihydroxynaphthalene reductase 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 -!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
CC {ECO:0000305|PubMed:31116900}.
CC -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC transcription factor PfmaF. {ECO:0000269|PubMed:28517364,
CC ECO:0000269|PubMed:31116900}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {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; KI912111; ETS83584.1; -; Genomic_DNA.
DR RefSeq; XP_007832232.1; XM_007834041.1.
DR AlphaFoldDB; W3XC32; -.
DR SMR; W3XC32; -.
DR STRING; 1229662.W3XC32; -.
DR EnsemblFungi; ETS83584; ETS83584; PFICI_05460.
DR GeneID; 19270473; -.
DR KEGG; pfy:PFICI_05460; -.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_3_1; -.
DR OMA; HEHQPRV; -.
DR OrthoDB; 913128at2759; -.
DR UniPathway; UPA00785; -.
DR Proteomes; UP000030651; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 2: Evidence at transcript level;
KW Melanin biosynthesis; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..282
FT /note="Trihydroxynaphthalene reductase PfmaI"
FT /id="PRO_0000447724"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 33..41
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 61..62
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 86..88
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 178..182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 211..213
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
SQ SEQUENCE 282 AA; 29907 MW; 9E05AE8CD85D5264 CRC64;
MPGVTSERTA SRFDAIPGPL GLASASLEGK VALVTGAGRG IGREMAMELG RRGAKVIVNY
ANSSESAQEV VNAIKKSGSD AVAIKANVSD VDQIVSLFDQ AVKVWGKLHI VCSNSGVVSF
GHVKDVTPEE FDRVFTINTR GQFFVAREAY KHLEVGGRLI LMGSITGQAK GVPKHAVYSG
SKGAIETFVR CMAVDFGDKK ITVNAVAPGG IKTDMYHAVC REYIPGGTEL DDEAVDEYAS
TWSPLGRVGL PIDIARCVCF LASQDGEWVN GKVLGIDGHA MM
