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SWNH1_METRA
ID   SWNH1_METRA             Reviewed;         307 AA.
AC   E9F8L9;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Dioxygenase swnH1 {ECO:0000303|PubMed:28381497};
DE            EC=1.14.11.- {ECO:0000305|PubMed:28381497};
DE   AltName: Full=Swainsonine biosynthesis gene cluster protein H1 {ECO:0000303|PubMed:28381497};
GN   Name=swnH1 {ECO:0000303|PubMed:28381497}; ORFNames=MAA_08618;
OS   Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS   anisopliae (strain ARSEF 23)).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 23 / ATCC MYA-3075;
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.-H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.-Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.-J., St Leger R.J., Zhao G.-P., Pei Y., Feng M.-G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ARSEF 23 / ATCC MYA-3075;
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT   adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
RN   [3]
RP   FUNCTION, 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).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=32786262; DOI=10.1021/acschembio.0c00466;
RA   Luo F., Hong S., Chen B., Yin Y., Tang G., Hu F., Zhang H., Wang C.;
RT   "Unveiling of Swainsonine Biosynthesis via a Multibranched Pathway in
RT   Fungi.";
RL   ACS Chem. Biol. 15:2476-2484(2020).
CC   -!- FUNCTION: Dioxygenase; 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, PubMed:32786262).
CC       Swainsonine production occurs via a multibranched pathway and is
CC       dispensable for fungal colonization of plants and infection of insect
CC       hosts (PubMed:32786262). The first step of swainsonine biosynthesis is
CC       the production of the precursor pipecolic acid (PA) via conversion of
CC       L-lysine (Lys) to 1-piperideine-6-carboxylate (P6C) by the
CC       aminotransferase swnA, the latter being further reduced to PA by the
CC       reductase swnR (PubMed:32786262). PA can be converted from lysine by
CC       both the SW biosynthetic cluster and the unclustered genes such as
CC       lysine cyclodeaminase (PubMed:32786262). The PKS-NRPS hybrid synthetase
CC       swnK uptakes and condensates PA and malonyl-CoA with and without
CC       skipping of the ketoreductase (KR) domain in order to produce 3
CC       intermediates, 1-oxoindolizidine, (1S)-1-hydroxyindolizin, and (1R)-1-
CC       hydroxyindolizine; with the transisomer (1S)-1-hydroxyindolizin being
CC       predominant (PubMed:32786262). The terminal thioester reductase (TE)
CC       domain of swnK is involved in reduction of the thioester bond to
CC       release the intermediate aldehydes (PubMed:32786262). The
CC       oxidoreductase swnN could contribute to the reduction of 1-
CC       oxoindolizidine to (1S)-1-hydroxyindolizin and (1R)-1-
CC       hydroxyindolizine, contributing to the major route of SW production
CC       (Probable). 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
CC       (PubMed:32786262). The dioxygenase swnH1 then performs the conversion
CC       of the 1,2-dihydroxyindolizine epimers to SW (PubMed:32786262).
CC       {ECO:0000269|PubMed:28381497, ECO:0000269|PubMed:32786262,
CC       ECO:0000305|PubMed:32786262}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000250|UniProtKB:Q4WAW9};
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:32786262}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q4WAW9}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes the production of swainsonine but still
CC       produces the 1,2-dihydroxyindolizine epimers intermediates.
CC       {ECO:0000269|PubMed:32786262}.
CC   -!- SIMILARITY: Belongs to the PhyH family. {ECO:0000305}.
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DR   EMBL; ADNJ02000001; EFY95965.1; -; Genomic_DNA.
DR   RefSeq; XP_007824807.1; XM_007826616.1.
DR   AlphaFoldDB; E9F8L9; -.
DR   SMR; E9F8L9; -.
DR   EnsemblFungi; EFY95965; EFY95965; MAA_08618.
DR   GeneID; 19262904; -.
DR   KEGG; maj:MAA_08618; -.
DR   HOGENOM; CLU_047725_0_0_1; -.
DR   Proteomes; UP000002498; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR008775; Phytyl_CoA_dOase.
DR   Pfam; PF05721; PhyH; 1.
PE   3: Inferred from homology;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..307
FT                   /note="Dioxygenase swnH1"
FT                   /id="PRO_0000441182"
FT   BINDING         149
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:O14832"
FT   BINDING         151
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:O14832"
FT   BINDING         227
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:O14832"
SQ   SEQUENCE   307 AA;  33725 MW;  BE629E2416B1CF2B CRC64;
     MGAFPPPIDP SYIPSVSLTR LPATAPTADI IATLERDGAL ILVDLVSPQD VAAINAEIEP
     YIQKARAESH EAYDLIPKQT IMVPGVVGKS PTMARMAELD VIDTLRTRVL QRKCTATWED
     RTEDFSIDPL LNSSLTYHIS YGGPRQRLHR DDMIHGIYHR GGEYRLSDET MLGFMIAGSK
     TTRENGATMA IPGSHKWDHA RVPRVDEVCF AEMEPGSALV FLGTVYHGAG HNSVPDQVRK
     IYGLFFIPGT LRPEENQFLA IPRSKVLGMS DKMLSLLGYK KPGTWLGIVN NGDPAENLAE
     VLGMANS
 
 
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