ID   LNBB_ASPFN              Reviewed;         335 AA.
AC   B8NWW2;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=NmrA-like family domain-containing oxidoreductase lnbB {ECO:0000303|PubMed:23281040};
DE            EC=1.-.-.- {ECO:0000305|PubMed:23281040};
DE   AltName: Full=Lnb diastereomeric piperazines biosynthesis cluster protein B {ECO:0000303|PubMed:23281040};
GN   Name=lnaB {ECO:0000303|PubMed:23281040}; ORFNames=AFLA_121490;
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: NmrA-like family domain-containing oxidoreductase; part of
CC       the lnb gene cluster that mediates the biosynthesis of diastereomeric
CC       piperazines. Lna and lnb clusters encode sets of enzymes that produce
CC       overlapping sets of previously undescribed metabolites such as
CC       piperazinomycin-like metabolites or morpholine (PubMed:23281040). The
CC       lna and lnb biosynthetic pathways appear to be part of a signaling
CC       network that controls the formation of sclerotia, a resilient
CC       overwintering structure (PubMed:23281040). One primary function of the
CC       non-canonical nonribosomal peptide synthetases lnaA and lnbA consists
CC       in the reduction of L-tyrosine (PubMed:23281040). The presence in the
CC       clusters of tailoring enzymes such as the oxidoreductases lnaB, lnbB,
CC       lnaE or lnbE, as well as of the cytochrome P450 monooxygenases lnaC,
CC       lnaD, or lnbC, might explain formation of various diastereomeric
CC       piperazines (PubMed:23281040). {ECO:0000269|PubMed:23281040}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:23281040}.
CC   -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; EQ963485; EED45920.1; -; Genomic_DNA.
DR   RefSeq; XP_002384856.1; XM_002384815.1.
DR   AlphaFoldDB; B8NWW2; -.
DR   SMR; B8NWW2; -.
DR   STRING; 5059.CADAFLAP00012721; -.
DR   EnsemblFungi; EED45920; EED45920; AFLA_121490.
DR   VEuPathDB; FungiDB:AFLA_121490; -.
DR   eggNOG; ENOG502SKP9; Eukaryota.
DR   HOGENOM; CLU_007383_8_5_1; -.
DR   OMA; GNEEMPF; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR008030; NmrA-like.
DR   Pfam; PF05368; NmrA; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   NADP; Oxidoreductase.
FT   CHAIN           1..335
FT                   /note="NmrA-like family domain-containing oxidoreductase
FT                   lnbB"
FT                   /id="PRO_0000446077"
FT   BINDING         14..18
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HBL8"
FT   BINDING         41..45
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HBL8"
FT   BINDING         62..63
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HBL8"
FT   BINDING         83..85
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HBL8"
FT   BINDING         142
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HBL8"
FT   BINDING         166..169
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HBL8"
SQ   SEQUENCE   335 AA;  37067 MW;  A89C138D41F465DD CRC64;
     MTVTATERIV TVFGTGNQAG AVARALLADK TSQFKVRAIS RHPDSASSRT LSALGVQVVK
     ADGWNLEELT RAFADTWAAF VNTNSDDPLF LQKGDGPTEF DLGKNIIDSL VAAKVQHLVY
     SCFASSVEQT KGKLFIKPME MKYQALKYAR ETGHFATTCG IYAAWYYEQF LDKATADVFG
     GFPTTPDEEG YITFRAPLWG DDEHPSFVSI THDFGDMVHG ILLEPEQWDG KSVPAASDVM
     TFEQLAQTLQ NATGRKSRYI PLPSWEDFGR GIPELDDHKL LFAFTQATGG RYFGDVPTET
     KTALRLKRRA AEAQGKSGNE ANLLSMEEWF KTNFA