EPAF_ASPNC
ID EPAF_ASPNC Reviewed; 346 AA.
AC A2QTF1;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Dehydrogenase orf1 {ECO:0000303|PubMed:30384904};
DE EC=1.-.-.- {ECO:0000305|PubMed:30384904};
DE AltName: Full=Pestalamide A biosynthesis cluster protein orf1 {ECO:0000303|PubMed:30384904};
GN Name=orf1 {ECO:0000303|PubMed:30384904}; ORFNames=An09g01880;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
RN [2]
RP IDENTIFICATION, FUNCTION, AND PATHWAY.
RX PubMed=30384904; DOI=10.1016/j.micres.2018.10.004;
RA Wang B., Li X., Yu D., Chen X., Tabudravu J., Deng H., Pan L.;
RT "Deletion of the epigenetic regulator GcnE in Aspergillus niger FGSC A1279
RT activates the production of multiple polyketide metabolites.";
RL Microbiol. Res. 217:101-107(2018).
CC -!- FUNCTION: Dehydrogenase; part of the gene cluster that mediates the
CC biosynthesis of nigerpyrone and its derivatives carbonarone A and
CC pestalamide A (PubMed:30384904). The biosynthesis pathway begins with
CC the polyketide assembly by epaA to form phenylacetyl triketide
CC precursor from successive condensation of two malonyl-CoA, presumably
CC with one phenylacetyl-CoA starter unit produced by the phenylacetyl-CoA
CC ligase epaB (PubMed:30384904). For the nigerpyrone biosynthesis, the
CC reactive polyketide chain is released as an aldehyde through the R-
CC domain. A nonenzymatic cyclization and dehydration may create
CC nigerpyrone (PubMed:30384904). For the biosynthesis of carbonarone A
CC and pestalamide A, an extra methyl group is added through the C-
CC methyltransferase domain. Several further steps involving the
CC dehydrogenase orf1, the cytochrome P450 monooxygenase orf2 and the FAD-
CC dependent monooxygenase orf3 are required to form a carbonarone A
CC precursor which is converted to carbonarone A via cyclization
CC (PubMed:30384904). The O-acetyltransferase epaC could catalyze the
CC transfer of 2-methylsuccinyl-CoA, a common intermediate in the
CC ethylmalonyl-CoA pathway, to generate the final product pestalamide A
CC (Probable). {ECO:0000269|PubMed:30384904, ECO:0000305|PubMed:30384904}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:30384904}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AM270194; CAK40126.1; -; Genomic_DNA.
DR RefSeq; XP_001393503.1; XM_001393466.1.
DR AlphaFoldDB; A2QTF1; -.
DR SMR; A2QTF1; -.
DR PaxDb; A2QTF1; -.
DR EnsemblFungi; CAK40126; CAK40126; An09g01880.
DR GeneID; 4983719; -.
DR KEGG; ang:ANI_1_1136084; -.
DR VEuPathDB; FungiDB:An09g01880; -.
DR HOGENOM; CLU_026673_16_5_1; -.
DR Proteomes; UP000006706; Chromosome 1L.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR013149; ADH-like_C.
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 Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW NADP; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..346
FT /note="Dehydrogenase orf1"
FT /id="PRO_0000446159"
FT BINDING 43..48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 133..140
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 170..173
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 193..196
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 211
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 251..252
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 269..273
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 336..337
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
SQ SEQUENCE 346 AA; 36234 MW; D61CB7FEC2BB6DB0 CRC64;
MPTNFAAIVP GKNQSLVVQE APYPTAGENR IVVRVHALAV NAVDYATQMM GETLFPWVTY
PLVLGEDIAG EVVAIGPGVT RFKPGDRVVG HAVGTNSNNS AEGAFQQYVV LLENMASPLP
HALEYQQAAV VPLAFSTAIV GLFQKDYLGL QIPSLTPTRT GKTLLIWGGA TSVGCNAIQL
AVAAGYEVIT TCSPHNFDLV KSLGATAAFD YKKPSIRDDL REAFRGKTCA GALAIAGVVP
QTRNEAAEAC LNLVAESEGD KFVALSMPAP PNVPDGVSCK FIFASTVKDN EVSHQLYGYL
GEALAHGSFI AAPEAEVVGT GLEAVQGALN ALKQGVSAKK LVVTLP
