ID   PGMH_ASPTE              Reviewed;         492 AA.
AC   A0A5M3Z5R2;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2020, sequence version 1.
DT   03-AUG-2022, entry version 7.
DE   RecName: Full=FAD-linked oxidoreductase pgmH {ECO:0000303|PubMed:28471414};
DE            EC=1.1.1.- {ECO:0000305|PubMed:35351612};
DE   AltName: Full=Pigmented naphthoquinones biosynthesis cluster protein H {ECO:0000303|PubMed:28471414};
GN   Name=pgmH {ECO:0000303|PubMed:28471414}; ORFNames=ATETN484_0009059200;
OS   Aspergillus terreus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=33178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN-484;
RA   Kanamasa S., Takahashi H.;
RT   "Aspergillus terreus TN-484 whole genome shotgun sequence.";
RL   Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION, FUNCTION, AND INDUCTION.
RC   STRAIN=MUCL38669;
RX   PubMed=28471414; DOI=10.3390/microorganisms5020022;
RA   Palonen E.K., Raina S., Brandt A., Meriluoto J., Keshavarz T., Soini J.T.;
RT   "Melanisation of Aspergillus terreus-is butyrolactone I involved in the
RT   regulation of both DOPA and DHN types of pigments in submerged culture?";
RL   Microorganisms 5:0-0(2017).
RN   [3]
RP   FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=35351612; DOI=10.1016/j.fgb.2022.103690;
RA   Tang S., Men P., Zhang W., Li H., Li Z., Huang X., Lu X.;
RT   "Identification of a polyketide biosynthesis gene cluster by
RT   transcriptional regulator activation in Aspergillus terreus.";
RL   Fungal Genet. Biol. 160:103690-103690(2022).
CC   -!- FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that
CC       mediates the biosynthesis of pleosporalin A, ascomycone A, as well as a
CC       third cryptic naphthoquinone derived pigment, all responsible for the
CC       coloration of conidia (PubMed:28471414, PubMed:35351612). Essential for
CC       the production of pleosporalin A, but not the 2 other final products
CC       (PubMed:35351612). The pathway begins with the biosynthesis of the
CC       cyclized heptaketide 3-acetonyl-1,6,8-trihydroxy-2-naphthaldehyde by
CC       the NR-PKS pgmA. The C-6 hydroxyl group is further methylated by the O-
CC       methyltransferase pgmB to yield fusarubinaldehyde which is in turn
CC       oxidized by the cytochrome P450 monooxygenase pgmC at C-9. The C-1
CC       hydroxyl group is then methylated spontaneously. Although pgmE, pgmD
CC       and pgmH are essential for the production of pleosporalin A, it is not
CC       the case for the 2 other final products and it remains difficult to
CC       assign a specific function to each enzyme. PgmF and pgmG seem not to be
CC       involved in pigment biosynthesis although they were regulated by the
CC       cluster-specific transcription factor pgmR (PubMed:35351612)
CC       (Probable). {ECO:0000269|PubMed:28471414, ECO:0000269|PubMed:35351612,
CC       ECO:0000305|PubMed:35351612}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q5BEJ5};
CC   -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:35351612}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:35351612}.
CC   -!- INDUCTION: Expression is significantly up-regulated at the end of late
CC       growth phase, in the presence of Butyrolactone I (PubMed:28471414).
CC       Expression is positively regulated by the pgm cluster-specific
CC       transcription factor pgmR (PubMed:35351612).
CC       {ECO:0000269|PubMed:28471414, ECO:0000269|PubMed:35351612}.
CC   -!- DISRUPTION PHENOTYPE: Only abolishes the production of pleosporalin A
CC       but not of the 2 other final products. {ECO:0000269|PubMed:35351612}.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; BKZM02000009; GES63905.1; -; Genomic_DNA.
DR   VEuPathDB; FungiDB:ATEG_06211; -.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN           1..492
FT                   /note="FAD-linked oxidoreductase pgmH"
FT                   /id="PRO_0000456015"
FT   DOMAIN          54..224
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ   SEQUENCE   492 AA;  54399 MW;  2B094C270AF9F21A CRC64;
     MDPNILWQAR NDGSALQEED IQQLRSSIRG TVVLKNEASE EEYNAAVTRW NNVSIRLATL
     VVYVEDEQDI VKCVEFVNKH YLDVAVCSHG RHSYHGASSS TGMVIDLGRM RRVSVDKEAM
     TVTAQGGCIA RDVELPLEAE GLATVFGAVN ETGIGGLTLG GGVGFLTGAH GLAADNLVSA
     RMVLANGQVV TASDDENSDL FWAIRGAGPN FGIVTEFKYR VHKQGPVFWQ MLFYSPDKLK
     DCVSIVNQMH NISLAQKGGD FQVMMAYLTP PGYPDLHPGL RIFYNGPEEK AKELAAPAYA
     LGPLSVSGGM CNFSDTTRIP PYLEFEGFDR YAASSAHLDY PLDENLLLEV FTMFRNVIHK
     YGHHLLHPSK CILDLRNYEK VASVPIDATA YSGRFDVAWM IPDLQWDDPA MDSTMRMEVT
     SITAHIRERV REAKGGHVNG PRDATAIYPN ISAGGEEKAK SVFGPNLPRL QVLKRKYDPD
     FIWNKWFPIV PA