ID   LNBE_ASPFN              Reviewed;         377 AA.
AC   B8NWW6;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=NADP-dependent oxidoreductase lnbE {ECO:0000303|PubMed:23281040};
DE            EC=1.-.-.- {ECO:0000305|PubMed:23281040};
DE   AltName: Full=Lnb diastereomeric piperazines biosynthesis cluster protein E {ECO:0000303|PubMed:23281040};
GN   Name=lnbE {ECO:0000303|PubMed:23281040}; ORFNames=AFLA_121530;
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, FUNCTION, AND PATHWAY.
RX   PubMed=23281040; DOI=10.1002/anie.201207456;
RA   Forseth R.R., Amaike S., Schwenk D., Affeldt K.J., Hoffmeister D.,
RA   Schroeder F.C., Keller N.P.;
RT   "Homologous NRPS-like gene clusters mediate redundant small-molecule
RT   biosynthesis in Aspergillus flavus.";
RL   Angew. Chem. Int. Ed. 52:1590-1594(2013).
CC   -!- FUNCTION: NADP-dependent oxidoreductase; part of the lnb gene cluster
CC       that mediates the biosynthesis of diastereomeric piperazines. Lna and
CC       lnb clusters encode sets of enzymes that produce overlapping sets of
CC       previously undescribed metabolites such as piperazinomycin-like
CC       metabolites or morpholine (PubMed:23281040). The lna and lnb
CC       biosynthetic pathways appear to be part of a signaling network that
CC       controls the formation of sclerotia, a resilient overwintering
CC       structure (PubMed:23281040). One primary function of the non-canonical
CC       nonribosomal peptide synthetases lnaA and lnbA consists in the
CC       reduction of L-tyrosine (PubMed:23281040). The presence in the clusters
CC       of tailoring enzymes such as the oxidoreductases lnaB, lnbB, lnaE or
CC       lnbE, as well as of the cytochrome P450 monooxygenases lnaC, lnaD, or
CC       lnbC, might explain formation of various diastereomeric piperazines
CC       (PubMed:23281040). {ECO:0000269|PubMed:23281040}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:23281040}.
CC   -!- SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD family.
CC       {ECO:0000305}.
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DR   EMBL; EQ963485; EED45924.1; -; Genomic_DNA.
DR   RefSeq; XP_002384860.1; XM_002384819.1.
DR   AlphaFoldDB; B8NWW6; -.
DR   SMR; B8NWW6; -.
DR   STRING; 5059.CADAFLAP00012725; -.
DR   EnsemblFungi; EED45924; EED45924; AFLA_121530.
DR   VEuPathDB; FungiDB:AFLA_121530; -.
DR   eggNOG; KOG0134; Eukaryota.
DR   HOGENOM; CLU_012153_0_0_1; -.
DR   OMA; AYVHLYY; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001155; OxRdtase_FMN_N.
DR   InterPro; IPR045247; Oye-like.
DR   PANTHER; PTHR22893; PTHR22893; 1.
DR   Pfam; PF00724; Oxidored_FMN; 1.
PE   3: Inferred from homology;
KW   NADP; Oxidoreductase.
FT   CHAIN           1..377
FT                   /note="NADP-dependent oxidoreductase lnbE"
FT                   /id="PRO_0000446082"
FT   BINDING         170..173
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9EQZ5"
FT   BINDING         257..263
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9EQZ5"
FT   BINDING         293..295
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9EQZ5"
SQ   SEQUENCE   377 AA;  41706 MW;  9173E3B0BC8979F4 CRC64;
     MMSKLFTPLQ VGFCQLKHRV IMAPLTRFRA DDNNVPLPIA KEYYSQRASV PGTLIIAEAT
     YISLAAGGYP NVPGIWSPEQ IARWKEITDA VHAQGSYIFL QLWALGRVGD ADTLKQDGFD
     LISSSAVPVD AGEPVPRAMT EEEIKQYIAL YAQAARNAVM AGFDGVELHG GNGYLVDQFT
     QDTCNRRTDS WGGSIPNRSR FAVEVTRAMV QAIGSERVAV KLTPWNDQQG MKMKDMEQQF
     LHLITSLKEL KLAYLHLTNP RVSVDEDVPL QGPPDGHPLE DNAGFVKAWG ETSPVFLGGG
     YTPQSAKHTL DVDYPLNEIG AVFGRLFISN PDLPLRLRDG LPFTPYDRDS FYTPLSPIGY
     SDYPFSDQAV DLIPVRV