ID   PGMD_ASPTE              Reviewed;         312 AA.
AC   A0A1W5SR39;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2017, sequence version 1.
DT   03-AUG-2022, entry version 11.
DE   RecName: Full=Short chain dehydrogenase pgmD {ECO:0000303|PubMed:35351612};
DE            EC=1.1.1.- {ECO:0000305|PubMed:35351612};
DE   AltName: Full=Pigmented naphthoquinones biosynthesis cluster protein D {ECO:0000303|PubMed:35351612};
GN   Name=pgmD {ECO:0000303|PubMed:28471414};
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 [GENOMIC DNA], 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   [2]
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: Short chain dehydrogenase; 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   -!- 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 short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; KX470748; ARB51365.1; -; mRNA.
DR   VEuPathDB; FungiDB:ATEG_06207; -.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..312
FT                   /note="Short chain dehydrogenase pgmD"
FT                   /id="PRO_0000456007"
FT   ACT_SITE        207
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         45..53
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         72..73
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         104..106
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         207..211
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         240..243
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
SQ   SEQUENCE   312 AA;  34056 MW;  E9E3A29E4170B3E8 CRC64;
     MAQPELDLSK APAHWGMNFT ETTHQQPSRS IDPSNVTFPQ GYTVVVIGAG KGIGEHIAKA
     YVQARAENII ITSRTGSDLD RVKKELETLA QQTGQAVKVS TLVQDATKPE SYTKLKDLLE
     EGFNGRLDTL VFCAGGGPVG TLWTPRIDET DVDEWNESIA LNFTGSYYAA KYLVPLMLRP
     QSQGKTIVNI TSAASHFTGG NITPASYSIG KLALNRFTQI LGENYADQGL VVVAVHPGSS
     PTPGALGSMP PSLHNILTDD QGLCGAVCVW ISKKKREWIS GRYICATWDM DELESKKEEI
     VKEDKLKWRM AV