PGMF_ASPTN
ID PGMF_ASPTN Reviewed; 356 AA.
AC Q0CJC5;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Trans-enoyl reductase pgmF {ECO:0000303|PubMed:35351612};
DE EC=1.-.-.- {ECO:0000305|PubMed:35351612};
DE AltName: Full=Pigmented naphthoquinones biosynthesis cluster protein F {ECO:0000303|PubMed:35351612};
GN Name=pgmF {ECO:0000303|PubMed:28471414}; ORFNames=ATEG_06209;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) 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, AND DISRUPTION PHENOTYPE.
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). The pathway
CC begins with the biosynthesis of the cyclized heptaketide 3-acetonyl-
CC 1,6,8-trihydroxy-2-naphthaldehyde by the NR-PKS pgmA. The C-6 hydroxyl
CC group is further methylated by the O-methyltransferase pgmB to yield
CC fusarubinaldehyde which is in turn oxidized by the cytochrome P450
CC monooxygenase pgmC at C-9. The C-1 hydroxyl group is then methylated
CC spontaneously. Although pgmE, pgmD and pgmH are essential for the
CC production of pleosporalin A, it is not the case for the 2 other final
CC products and it remains difficult to assign a specific function to each
CC enzyme. PgmF and pgmG seem not to be involved in pigment biosynthesis
CC although they were regulated by the cluster-specific transcription
CC factor pgmR (PubMed:35351612) (Probable). {ECO:0000269|PubMed:28471414,
CC ECO:0000269|PubMed:35351612, ECO:0000305|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: Does not affect the production of the
CC naphthoquinones derived pigments. {ECO:0000269|PubMed:35351612}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; CH476601; EAU33970.1; -; Genomic_DNA.
DR RefSeq; XP_001215387.1; XM_001215387.1.
DR STRING; 33178.CADATEAP00002978; -.
DR EnsemblFungi; EAU33970; EAU33970; ATEG_06209.
DR GeneID; 4321478; -.
DR VEuPathDB; FungiDB:ATEG_06209; -.
DR eggNOG; KOG1198; Eukaryota.
DR HOGENOM; CLU_026673_3_3_1; -.
DR OMA; LVTYQCL; -.
DR OrthoDB; 727365at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW NADP; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..356
FT /note="Trans-enoyl reductase pgmF"
FT /id="PRO_0000456010"
FT BINDING 57..60
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 175..178
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 198..201
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 216
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 261..262
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 342..343
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
SQ SEQUENCE 356 AA; 38390 MW; 5B766FED153C5A8D CRC64;
MASTVPSTMK AWQFSSAYPT IEANLKLNNN APLPDGAKNL GPDQVLVKVI AAGLNPVDFK
FAEIPWLGRF IVGSPSTPGM DFAGRVVATG PNTKSVAVED LKPGQLVFGR LDSPCKFGTL
AEYTIAPRKG CVAIPPGARV IETACVASVG LTAYQSIVYR LKDHAGKRVF LNGGSGGCGT
FGIQIAKQMG CHVTTSCSTP NVDLCRSLGA DTVIDYKKTD VIAELKKMQP FDLVVDNVGV
PTDLYWAAPS FTNPGAPYVQ VGALAVTPGF ILGNFFKARW PGWLGGGKRP WEFMHIESNV
QDYEQLGRWM QEGKLRAVVD EVFGMQDDGA VKAYQKLRTG RAKGKIIVKI DETWED
