PGMH_ASPTN
ID PGMH_ASPTN Reviewed; 483 AA.
AC Q0CJC3;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=ATEG_06211;
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, 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; CH476601; EAU33972.1; -; Genomic_DNA.
DR RefSeq; XP_001215389.1; XM_001215389.1.
DR STRING; 33178.CADATEAP00002980; -.
DR EnsemblFungi; EAU33972; EAU33972; ATEG_06211.
DR GeneID; 4321298; -.
DR VEuPathDB; FungiDB:ATEG_06211; -.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_018354_10_0_1; -.
DR OMA; GIVGLEW; -.
DR OrthoDB; 350817at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
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; Reference proteome.
FT CHAIN 1..483
FT /note="FAD-linked oxidoreductase pgmH"
FT /id="PRO_0000456014"
FT DOMAIN 54..215
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ SEQUENCE 483 AA; 53668 MW; 81ADAE65D70F428C CRC64;
MDPNIMWQAR NDGSGLLEED IQQLRSSIRG TVVLKNEASE EEYNAAVTRW NNVSIRLATL
VVYVEDEQDI VKCVEFVNKH YLDVAVCSHG RHSYHGASSS TGMVIDLGRM RKVSVDKEAM
TVTAQGGCIA RDVELPLEAE GLAAVFGAVN ETGVGFLTGA HGLAADNLVS ARMVLANGQV
VTASDDENSD LFWAIRGAGP NFGIVTEFKY RVHKQGPVFW QMLFYSPDKL KDCVSIVNQM
HNISLAQKGG DFQVMMCYLT PPGYPDLHPG LRIFYNGPEE KAKELAAPAY ALGPLSVSGG
MCSFSDTTRI PPYLEFEGFD RYAASSAHLD YPLDEDLLLE VFTMFRNVIH KYGHHLLHPS
KCILDLRNYE KVASVPIDAT AYSGRFDVAW MIPDLQWDDP AMDSTMRMEV TSITAHIRER
VREAKGDHVS GPRDATAIYP NISAGGEEKA KSVFGPNLPR LRVLKRKYDP NFIWNKWFPI
VPA
