SWNR_ARTBC
ID SWNR_ARTBC Reviewed; 305 AA.
AC D4AN96;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Oxidoreductase swnR {ECO:0000303|PubMed:28381497};
DE EC=1.5.3.7 {ECO:0000250|UniProtKB:E9F8M2};
DE AltName: Full=Swainsonine biosynthesis gene cluster protein R {ECO:0000303|PubMed:28381497};
GN Name=swnR {ECO:0000303|PubMed:28381497}; ORFNames=ARB_05701;
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: Oxidoreductase; 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:E9F8L9, ECO:0000250|UniProtKB:E9F8M1,
CC ECO:0000250|UniProtKB:E9F8M2, ECO:0000250|UniProtKB:E9F8M3,
CC ECO:0000250|UniProtKB:E9F8M4, ECO:0000269|PubMed:28381497}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-pipecolate + O2 = H(+) + H2O2 + L-1-piperideine-6-
CC carboxylate; Xref=Rhea:RHEA:11992, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:58769,
CC ChEBI:CHEBI:61185; EC=1.5.3.7;
CC Evidence={ECO:0000250|UniProtKB:E9F8M2};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11994;
CC Evidence={ECO:0000250|UniProtKB:E9F8M2};
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; ABSU01000003; EFE35657.1; -; Genomic_DNA.
DR RefSeq; XP_003016302.1; XM_003016256.1.
DR AlphaFoldDB; D4AN96; -.
DR SMR; D4AN96; -.
DR EnsemblFungi; EFE35657; EFE35657; ARB_05701.
DR GeneID; 9524374; -.
DR KEGG; abe:ARB_05701; -.
DR eggNOG; ENOG502SJZF; Eukaryota.
DR HOGENOM; CLU_044876_5_0_1; -.
DR OMA; CIGWLAD; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0050031; F:L-pipecolate oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF13460; NAD_binding_10; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..305
FT /note="Oxidoreductase swnR"
FT /id="PRO_0000441187"
SQ SEQUENCE 305 AA; 34471 MW; BB673F39871C6C8F CRC64;
MKVAIAGYGD LTRYICEEFV QAGHELVILT RSFKPQIESP GISQAITDYT ISSLKATLAD
CEVLISTIGD MSNAYTSVHH TLIQACQESP KCKRFIPAEF AVNIETYPDE PGFYYAIHEP
VRETLRNQTN LEWTLVCIGW LADYFVPSKN RYIKDIDECH PINWKANKAV IPGTGNEPVD
FTWARDVAKG LASLIQAPTG SWEPYTFMSG ERSCWNDMAA LIKEKYRPDM PIEHVSLHAT
ANMIKAAKDE DTLILADYYL LSISQACAIP QDKAKAHKEK FFPHIHFRTL REGLSQFDEK
PNSIM
