ID   LNAB_ASPFN              Reviewed;         334 AA.
AC   B8NU00;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=NmrA-like family domain-containing oxidoreductase lnaB {ECO:0000303|PubMed:23281040};
DE            EC=1.-.-.- {ECO:0000305|PubMed:23281040};
DE   AltName: Full=Lna diastereomeric piperazines biosynthesis cluster protein B {ECO:0000303|PubMed:23281040};
GN   Name=lnaB {ECO:0000303|PubMed:23281040}; ORFNames=AFLA_101710;
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, INDUCTION, 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 lna 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   -!- INDUCTION: Expression is regulated by a complex signaling network which
CC       may include cross-pathway interactions mediated by sensing of the
CC       cluster final products or shared biosynthetic intermediates.
CC       {ECO:0000269|PubMed:23281040}.
CC   -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; EQ963484; EED46507.1; -; Genomic_DNA.
DR   RefSeq; XP_002384043.1; XM_002384002.1.
DR   AlphaFoldDB; B8NU00; -.
DR   SMR; B8NU00; -.
DR   EnsemblFungi; EED46507; EED46507; AFLA_101710.
DR   VEuPathDB; FungiDB:AFLA_101710; -.
DR   eggNOG; ENOG502SKP9; Eukaryota.
DR   HOGENOM; CLU_007383_8_5_1; -.
DR   OMA; FSSGPPC; -.
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   2: Evidence at transcript level;
KW   NADP; Oxidoreductase.
FT   CHAIN           1..334
FT                   /note="NmrA-like family domain-containing oxidoreductase
FT                   lnaB"
FT                   /id="PRO_0000446076"
FT   BINDING         12..17
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HBL8"
FT   BINDING         38..42
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HBL8"
FT   BINDING         59..60
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HBL8"
FT   BINDING         80..82
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HBL8"
FT   BINDING         138
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HBL8"
FT   BINDING         162..165
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HBL8"
SQ   SEQUENCE   334 AA;  36713 MW;  983406564F131E6C CRC64;
     MSPDRKLITI FGGTGKQGGS VAHSLLQNPD FRVRVITRNA QSDASRKLAA LGADIAQGDG
     FSGDEMLSAF SGSWGAFVNI NSDDKIFTTE GGPTEFDMGK IIVDSAVQAG VKHLVFSSGP
     PCTEMTNGRV RMKAMDMKNK IEQYARSLGS FETFTPIGAG WFLENFLGKE VAPVFGGFPY
     FPDDQGYLTF RVPYWGGDEH VPWLSISDDF GDIVQGIFLD PGRWNGHFVH GVSDIRSFEQ
     VVADFAAVTG NKARFQPILP TWEAFDTHGI QELEDVKLMF GFTQLTGGRY FGPEDTEVDT
     ARQLKQITGL KLGRPEGQHK LTSARDWFAA RFAN