LEPG_ASPFN
ID LEPG_ASPFN Reviewed; 398 AA.
AC B8NJH1;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Trans-enoyl reductase lepG {ECO:0000303|PubMed:26051490};
DE EC=1.-.-.- {ECO:0000305};
DE AltName: Full=Leporins biosynthesis protein A {ECO:0000303|PubMed:26051490};
GN Name=lepG {ECO:0000303|PubMed:26051490}; ORFNames=AFLA_066920;
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: Trans-enoyl reductase; part of the gene cluster 23 that
CC mediates the 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 -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9Y7D0}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production od leporins B and C or any
CC other potential open ring 2-pyridone (PubMed:26051490).
CC {ECO:0000269|PubMed:26051490}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; EQ963479; EED49870.1; -; Genomic_DNA.
DR RefSeq; XP_002380251.1; XM_002380210.1.
DR AlphaFoldDB; B8NJH1; -.
DR SMR; B8NJH1; -.
DR STRING; 5059.CADAFLAP00008116; -.
DR EnsemblFungi; EED49870; EED49870; AFLA_066920.
DR VEuPathDB; FungiDB:AFLA_066920; -.
DR eggNOG; KOG1198; Eukaryota.
DR HOGENOM; CLU_026673_16_1_1; -.
DR OMA; PARLVWH; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
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.
FT CHAIN 1..398
FT /note="Trans-enoyl reductase lepG"
FT /id="PRO_0000438445"
FT BINDING 93..96
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 178..185
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 212..215
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 235..238
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 253
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 300..301
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 320..324
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 389..390
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
SQ SEQUENCE 398 AA; 43340 MW; 159E54C18A1B40ED CRC64;
MKHRRYKLDD SNLLLSSPCA VASCWYSENP ATLSPPRPRH TMPASVHFEI SATQRAIKIK
GPGQASVEKG CPVPACQPED ILVRVVCVAL NPVDWKSADL SPSLDATWGT DFSGEVVVVG
EACQSRFALG DSVCGAAFGN NPEDATQGAF AEYVAIPGEL VYKIPPDISF EQAATVGTGL
ATAGLTLYQT LGLSWPDQPV QDAQYVLVYG GGTASGCFMI QLLRLSGYIP VTTCSAKSFD
RVKQLGAAEA FDYHSPGCGS EIREYTENSI KYAVDCITNI DSMKCCYTAI GSSGGQYVAL
DPFPIRGHTR RNVKARWIIG YTIYGRPINW KHPFKRDAQP QDREFAKRWY PVAQRLLDEG
KLQLHPLQVE TGGLPGVIEG ANRSRKHQVT GVKLVYCV
