ID   SWNN_ARTBC              Reviewed;         318 AA.
AC   D4AU28;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Oxidoreductase swnN {ECO:0000303|PubMed:28381497};
DE            EC=1.3.1.- {ECO:0000305|PubMed:28381497};
DE   AltName: Full=Swainsonine biosynthesis gene cluster protein N {ECO:0000303|PubMed:28381497};
GN   Name=swnN {ECO:0000303|PubMed:28381497}; ORFNames=ARB_07841;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
RN   [2]
RP   IDENTIFICATION, AND PATHWAY.
RX   PubMed=28381497; DOI=10.1534/g3.117.041384;
RA   Cook D., Donzelli B.G., Creamer R., Baucom D.L., Gardner D.R., Pan J.,
RA   Moore N., Jaromczyk J.W., Schardl C.L.;
RT   "Swainsonine biosynthesis genes in diverse symbiotic and pathogenic
RT   fungi.";
RL   G3 (Bethesda) 7:1791-1797(2017).
CC   -!- FUNCTION: Aminotransferase; part of the gene cluster that mediates the
CC       biosynthesis of swainsonine (SW), a cytotoxic fungal alkaloid and a
CC       potential cancer therapy drug (PubMed:28381497). Swainsonine production
CC       occurs via a multibranched pathway and is dispensable for fungal
CC       colonization of plants and infection of insect hosts (By similarity).
CC       The first step of swainsonine biosynthesis is the production of the
CC       precursor pipecolic acid (PA) via conversion of L-lysine (Lys) to 1-
CC       piperideine-6-carboxylate (P6C) by the aminotransferase swnA, the
CC       latter being further reduced to PA by the reductase swnR (By
CC       similarity). The PKS-NRPS hybrid synthetase swnK uptakes and
CC       condensates PA and malonyl-CoA with and without skipping of the
CC       ketoreductase (KR) domain in order to produce 3 intermediates, 1-
CC       oxoindolizidine, (1S)-1-hydroxyindolizin, and (1R)-1-hydroxyindolizine;
CC       with the transisomer (1S)-1-hydroxyindolizin being predominant (By
CC       similarity). The terminal thioester reductase (TE) domain of swnK is
CC       involved in reduction of the thioester bond to release the intermediate
CC       aldehydes (By similarity). The oxidoreductase swnN could contribute to
CC       the reduction of 1-oxoindolizidine to (1S)-1-hydroxyindolizin and (1R)-
CC       1-hydroxyindolizine, contributing to the major route of SW production
CC       (By similarity). The dioxygenase swnH2 would be responsible for the
CC       oxidization of (1R)-1-hydroxyindolizine into (1R,2S)-1,2-
CC       dihydroxyindolizine and of (1S)-1-hydroxyindolizin to yield both
CC       (1R,2S)-1,2-dihydroxyindolizine and (1S,2S)-1,2-dihydroxyindolizine (By
CC       similarity). The dioxygenase swnH1 then performs the conversion of the
CC       1,2-dihydroxyindolizine epimers to SW (By similarity).
CC       {ECO:0000250|UniProtKB:E9F8L8, ECO:0000250|UniProtKB:E9F8L9,
CC       ECO:0000250|UniProtKB:E9F8M1, ECO:0000250|UniProtKB:E9F8M3,
CC       ECO:0000250|UniProtKB:E9F8M4, ECO:0000269|PubMed:28381497}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:28381497}.
CC   -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC       reductase subfamily. {ECO:0000305}.
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DR   EMBL; ABSU01000010; EFE33481.1; -; Genomic_DNA.
DR   RefSeq; XP_003014121.1; XM_003014075.1.
DR   AlphaFoldDB; D4AU28; -.
DR   EnsemblFungi; EFE33481; EFE33481; ARB_07841.
DR   GeneID; 9521538; -.
DR   KEGG; abe:ARB_07841; -.
DR   eggNOG; ENOG502SIXU; Eukaryota.
DR   HOGENOM; CLU_044876_0_0_1; -.
DR   OMA; HPQLTWT; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..318
FT                   /note="Oxidoreductase swnN"
FT                   /id="PRO_0000441189"
SQ   SEQUENCE   318 AA;  35384 MW;  69914F91AD43B3DD CRC64;
     MAVVAVAGGT GGKGVPGAAN EPRRYAVDYD NVEEMRNVLK ENNVEVVVSA LLLSDESVAK
     SQINLIRAAA ESGTVTKFIP SEYYIDFHSP IPGSDLFTNF QIEAEEELMR HPQLTWTLIR
     VGIFLDHLTM PFNPKPTYIT PYWVFVDIEH EECVFPGDGS QPLVLSHSTD LAAYIECLVG
     LPSNEWPRES LVASNKIQVK DLQDLIKKTT GTLCGHLGIC IRTFLILAIG REFKVTYDSV
     ESIQKGQITP LTSNRPVFDD PQKGKLFQEV EVQVMLSMLS NAHDLPGKNL AELFPEVHVT
     NIEDFLRAGW EMKQGLKP