ID   LNAE_ASPFN              Reviewed;         371 AA.
AC   B8NTZ8;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=NADP-dependent oxidoreductase lnaE {ECO:0000303|PubMed:23281040};
DE            EC=1.-.-.- {ECO:0000305|PubMed:23281040};
DE   AltName: Full=Lna diastereomeric piperazines biosynthesis cluster protein E {ECO:0000303|PubMed:23281040};
GN   Name=lnaE {ECO:0000303|PubMed:23281040}; ORFNames=AFLA_101690;
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 lna 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EQ963484; EED46505.1; -; Genomic_DNA.
DR   RefSeq; XP_002384041.1; XM_002384000.1.
DR   AlphaFoldDB; B8NTZ8; -.
DR   SMR; B8NTZ8; -.
DR   STRING; 5059.CADAFLAP00011906; -.
DR   EnsemblFungi; EED46505; EED46505; AFLA_101690.
DR   VEuPathDB; FungiDB:AFLA_101690; -.
DR   eggNOG; KOG1196; Eukaryota.
DR   HOGENOM; CLU_026673_29_1_1; -.
DR   OMA; ENPCEFD; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR041694; ADH_N_2.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR045010; MDR_fam.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43205; PTHR43205; 2.
DR   Pfam; PF16884; ADH_N_2; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   NADP; Oxidoreductase.
FT   CHAIN           1..371
FT                   /note="NADP-dependent oxidoreductase lnaE"
FT                   /id="PRO_0000446081"
FT   BINDING         172..175
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9EQZ5"
FT   BINDING         198
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9EQZ5"
FT   BINDING         214
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9EQZ5"
FT   BINDING         237
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9EQZ5"
FT   BINDING         277..283
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9EQZ5"
FT   BINDING         307..309
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9EQZ5"
SQ   SEQUENCE   371 AA;  41600 MW;  B43CE83DFEC2CF73 CRC64;
     MTRVTMDQDT ENKVLVIKNM DSGYLVAGEQ VTLEDVSYDA TEPLAEDELM VQLLYATYDL
     FKRDLASSSA DATELRGRKP VETMSIAQVI KSNNKQFQEG DMVIGRLPVQ QYVLIKADDA
     TELKLLENPC EFDDIRLFLS VLGVPGLLAF SSLYEIGRPK KGETILIAGA SDEIGQLVGQ
     MARLEGLKVF GSVESDEKLD FLITELGFDG GFNYAKESPY EALPRLVPNG IDIYYDNLSW
     MSRLNIGGLD THFDLLGSRH LNAAFSSMRR YGRIMFYGTI AEQTVLDPII GMFLHNTVLK
     RLTIRGFGLS DPSFGKKWGK LHMERMQQWV KEEKLKIPTF EITGMDNAAK AFVEAFYSSE
     NTHTHTILAV T