ID   NANB_ASPNN              Reviewed;         417 AA.
AC   A0A6G9KH50;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   12-AUG-2020, sequence version 1.
DT   25-MAY-2022, entry version 6.
DE   RecName: Full=Acetyltransferase nanB {ECO:0000303|PubMed:32182055};
DE            EC=2.3.1.- {ECO:0000269|PubMed:32182055};
DE   AltName: Full=Nanangelenin A biosynthesis cluster protein B {ECO:0000303|PubMed:32182055};
DE   Flags: Precursor;
GN   Name=nanB {ECO:0000303|PubMed:32182055}; ORFNames=FE257_001449;
OS   Aspergillus nanangensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=2582783;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RC   STRAIN=CBS 146238 / FRR 6048 / MST FP2251;
RX   PubMed=32182055; DOI=10.1021/jacs.0c01605;
RA   Li H., Gilchrist C.L.M., Phan C.S., Lacey H.J., Vuong D., Moggach S.A.,
RA   Lacey E., Piggott A.M., Chooi Y.H.;
RT   "Biosynthesis of a new benzazepine alkaloid nanangelenin A from Aspergillus
RT   nanangensis involves an unusual l-kynurenine-incorporating NRPS catalyzing
RT   regioselective lactamization.";
RL   J. Am. Chem. Soc. 142:7145-7152(2020).
CC   -!- FUNCTION: Acetyltransferase; part of the gene cluster that mediates the
CC       biosynthesis of the benzazepine alkaloid nanangelenin A which contains
CC       an unprecedented 3,4-dihydro-1-benzazepine-2,5-dione-N-prenyl-N-
CC       acetoxy-anthranilamide scaffold (PubMed:32182055). The first step of
CC       nanangelenin biosynthesis is catalyzed by the indoleamine 2,3-
CC       dioxygenase nanC which produces N-formyl-kynurenine through the
CC       catabolism of tryptophan (PubMed:32182055). The two-module NRPS nanA
CC       then utilizes anthranilate (Ant) and L-kynurenine (L-Kyn) to assemble
CC       the dipeptide product nanangelenin B (PubMed:32182055). The first
CC       adenylation domain of nanA (A1) loads anthranilate onto the T1 domain,
CC       while A2 loads kynurenine, generated through spontaneous nonenzymatic
CC       deformylation of the nanC-supplied N-formyl-kynurenine
CC       (PubMed:32182055). The peptide bond formation between the tethered
CC       amino acids is catalyzed by the first condensation domain (C1) between
CC       anthranilate's carbonyl carbon and kynurenine's aliphatic primary amine
CC       (PubMed:32182055). The second C domain (C2) catalyzes the final
CC       cyclization event between the aromatic amine of kynurenine and the
CC       tethered carbonyl carbon, yielding nanangelenin B (PubMed:32182055).
CC       The terminal T3 domain enhances the catalytic efficiency of C2,
CC       suggesting the T2-tethered Ant-L-Kyn is transferred to T3 prior to
CC       cyclization by C2 (PubMed:32182055). Once released from nanA,
CC       nanangelenin B is then prenylated by the prenyltransferase nanD to form
CC       nanangelenin C (PubMed:32182055). Nanangelenin C is then N-hydroxylated
CC       by the FAD-dependent monooxygenase nanF and further acetylated by the
CC       acetyltransferase nanB to yield nanangelenin F (PubMed:32182055).
CC       Finally, the N-methyltransferase nanE methylates the amide nitrogen of
CC       1-benzazepine to convert nanangelenin F into nanangelenin A
CC       (PubMed:32182055). NanE is also able to methylate most of the
CC       intermediates of the pathway such as nanangelenin B and nanangelenin C
CC       to produce nanangelenin D and nanangelenin E, respectively
CC       (PubMed:32182055). {ECO:0000269|PubMed:32182055}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:32182055}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the wax synthase family. {ECO:0000305}.
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DR   EMBL; MT024570; QIQ51362.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A6G9KH50; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   InterPro; IPR044851; Wax_synthase.
DR   InterPro; IPR032805; Wax_synthase_dom.
DR   PANTHER; PTHR31595; PTHR31595; 1.
DR   Pfam; PF13813; MBOAT_2; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Membrane; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..417
FT                   /note="Acetyltransferase nanB"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5026038360"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        284..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        307..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        356..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        389..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   417 AA;  47228 MW;  B0A12A8E447046CD CRC64;
     MRPSTTTLSL LVFLISSILL ATTGKNSIIR YTYFPILLII CHLQLTNPPV NTASNIFDGS
     FEGTTLLNGL QQLNILVLTG VDVNDESGSS VFRRLKSALI YPFNARGVGT KYQIKNLPVL
     SSFICKEKQG ESGLSSFLSS ARYRFAIRQL AVSAWQYLLA DIGFSLLKNI PTEKRLEYYG
     PEEEWMPQSL DQLRVRIEAT LVFWVTLKAF AEIQSKIATA LLTAVGVTSP HDWPPFFGSL
     REAYTLRGFW GKWWHQQLRW PLTSYSNFIT RRVLKLTRSP LERYLNNALV FAQSGIVHVY
     FNWIKGVQDG DVGCMAFYIS FVAGYFLEDH VQGLWRKAFD RTSAQESSLW LLERLVGALW
     VATFLTIVTP WWVYPFLRLS SSLKMPYSFV DVFGFQGALT VVFMGAAALR IGLNAEP