ID   LEPF_ASPFN              Reviewed;         361 AA.
AC   B8NJH0;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Oxidoreductase lepF {ECO:0000303|PubMed:26051490};
DE            EC=1.-.-.- {ECO:0000305|PubMed:26051490};
DE   AltName: Full=Leporins biosynthesis protein F {ECO:0000303|PubMed:26051490};
GN   Name=lepF {ECO:0000303|PubMed:26051490}; ORFNames=AFLA_066910;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
RN   [2]
RP   IDENTIFICATION OF THE GENE CLUSTER 23, AND FUNCTION.
RX   PubMed=20447271; DOI=10.1111/j.1364-3703.2009.00594.x;
RA   Georgianna D.R., Fedorova N.D., Burroughs J.L., Dolezal A.L., Bok J.W.,
RA   Horowitz-Brown S., Woloshuk C.P., Yu J., Keller N.P., Payne G.A.;
RT   "Beyond aflatoxin: four distinct expression patterns and functional roles
RT   associated with Aspergillus flavus secondary metabolism gene clusters.";
RL   Mol. Plant Pathol. 11:213-226(2010).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=26051490; DOI=10.1016/j.fgb.2015.05.010;
RA   Cary J.W., Uka V., Han Z., Buyst D., Harris-Coward P.Y., Ehrlich K.C.,
RA   Wei Q., Bhatnagar D., Dowd P.F., Martens S.L., Calvo A.M., Martins J.C.,
RA   Vanhaecke L., Coenye T., De Saeger S., Di Mavungu J.D.;
RT   "An Aspergillus flavus secondary metabolic gene cluster containing a hybrid
RT   PKS-NRPS is necessary for synthesis of the 2-pyridones, leporins.";
RL   Fungal Genet. Biol. 81:88-97(2015).
CC   -!- FUNCTION: Oxidoreductase; part of the gene cluster 23 that mediates the
CC       biosynthesis of a family of 2-pyridones known as leporins
CC       (PubMed:20447271, PubMed:26051490). The hybrid PKS-NRPS synthetase lepA
CC       and the enoyl reductase lepG are responsible for fusion of
CC       phenylalanine with a hexaketide and subsequent release of the stable
CC       tetramic acid precursor, pre-leporin C (PubMed:26051490). Because lepA
CC       lacks a designated enoylreductase (ER) domain, the required activity is
CC       provided the enoyl reductase lepG (PubMed:26051490). It is possible
CC       that the dehydrogenase lepF also participates in production of pre-
CC       leporin C (PubMed:26051490). Cytochrome P450 monooxygenase lepH is then
CC       required for the ring expansion step to yield leporin C
CC       (PubMed:26051490). Leporin C is then presumably further oxidized by the
CC       N-hydroxylase lepD to form leporin B (PubMed:26051490). LepI may
CC       possess a function in biosynthesis upstream of lepA (PubMed:26051490).
CC       Leporin B is further oxidized in the presence of ferric ion to give the
CC       leporin B trimer-iron chelate, but whether or not this reaction is
CC       catalyzed by an enzyme in the pathway or by ferric ion is not
CC       determined yet (PubMed:26051490). {ECO:0000269|PubMed:26051490,
CC       ECO:0000305|PubMed:20447271}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Results in a significant reduction in leporin C
CC       and absence of detectable amounts of leporin B (PubMed:26051490).
CC       {ECO:0000269|PubMed:26051490}.
CC   -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; EQ963479; EED49869.1; -; Genomic_DNA.
DR   RefSeq; XP_002380250.1; XM_002380209.1.
DR   AlphaFoldDB; B8NJH0; -.
DR   SMR; B8NJH0; -.
DR   EnsemblFungi; EED49869; EED49869; AFLA_066910.
DR   VEuPathDB; FungiDB:AFLA_066910; -.
DR   HOGENOM; CLU_044999_0_2_1; -.
DR   OMA; FLTAGYA; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Membrane; Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..361
FT                   /note="Oxidoreductase lepF"
FT                   /id="PRO_0000438453"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   361 AA;  40936 MW;  4CD6F92F522CF9F3 CRC64;
     MVSLREIRAH NAGLRDAWAG HRHVSLFVGA TKGIGLATIM ELIQRIDEPT VYIVCRSTAQ
     FAQRIAELQR LNRRAKLVAL YGQISLLSEV DRICNLVLRK ESQLDLLFMS PGYLPNGHPS
     YTPEGLEELA SLAYYCRLRF TVNLLPLLER TAKTNYPDEP SNRRPRVFSV LNGGNERALP
     FVPEDLQSEK SYTMLNHVAH TTLMNTLALE HLAHKKPSVD FVHESPGKVQ TDIVASFLQS
     PERTRSRLVL WRWLKGMLML VLQAVLLPVF YVVAMPLAES GERRLYEATV DLSQQWQKQL
     QSPPYNGIVA APGFYRMKHT SDIVMDDTVL QAYRALGMPE RAWEHTMAVF RSVLDKGSGK
     K