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YANE_ASPNA
ID   YANE_ASPNA              Reviewed;         257 AA.
AC   G3Y423;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   06-JUL-2016, sequence version 2.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Probable oxidoreductase yanE {ECO:0000250|UniProtKB:J5J930};
DE            EC=1.-.-.- {ECO:0000250|UniProtKB:J5J930};
DE   AltName: Full=Yanuthone D biosynthesis cluster protein E {ECO:0000303|PubMed:24684908};
GN   Name=yanE {ECO:0000303|PubMed:24684908}; ORFNames=ASPNIDRAFT_192604;
OS   Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS   NCTC 3858a / NRRL 328 / USDA 3528.7).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=380704;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL
RC   328 / USDA 3528.7;
RX   PubMed=21543515; DOI=10.1101/gr.112169.110;
RA   Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.I.,
RA   Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA   Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA   van Dijck P.W.M., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA   Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.J.,
RA   Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA   Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA   Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA   Martinez D., van Peij N.N.M.E., Roubos J.A., Nielsen J., Baker S.E.;
RT   "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT   versus enzyme-producing CBS 513.88.";
RL   Genome Res. 21:885-897(2011).
RN   [2]
RP   BIOTECHNOLOGY.
RX   PubMed=11031048; DOI=10.1021/jo0006831;
RA   Bugni T.S., Abbanat D., Bernan V.S., Maiese W.M., Greenstein M.,
RA   Van Wagoner R.M., Ireland C.M.;
RT   "Yanuthones: novel metabolites from a marine isolate of Aspergillus
RT   niger.";
RL   J. Org. Chem. 65:7195-7200(2000).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=24684908; DOI=10.1016/j.chembiol.2014.01.013;
RA   Holm D.K., Petersen L.M., Klitgaard A., Knudsen P.B., Jarczynska Z.D.,
RA   Nielsen K.F., Gotfredsen C.H., Larsen T.O., Mortensen U.H.;
RT   "Molecular and chemical characterization of the biosynthesis of the 6-MSA-
RT   derived meroterpenoid yanuthone D in Aspergillus niger.";
RL   Chem. Biol. 21:519-529(2014).
CC   -!- FUNCTION: Part of the gene cluster that mediates the biosynthesis of
CC       yanuthone D, a fungal isoprenoid epoxycyclohexenone that acts as an
CC       antibiotic against fungi and bacteria (PubMed:24684908). The first step
CC       of the pathway is the synthesis of 6-methylsalicylic acid (6-MSA) by
CC       the polyketide synthase yanA (PubMed:24684908). 6-MSA is then converted
CC       to m-cresol by the decarboxylase yanB (PubMed:24684908). The cytochrome
CC       P450 monooxygenase yanC then catalyzes the oxidation of m-cresol to
CC       toluquinol (PubMed:24684908). Epoxidation of toluquinol is then
CC       performed by the short chain dehydrogenase yanD, with the help of yanE,
CC       and a further prenylation by yanG leads to 7-deacetoxyyanuthone A
CC       (PubMed:24684908). The next step is the hydroxylation of C-22 of 7-
CC       deacetoxyyanuthone A by the cytochrome P450 monooxygenase yanH to yield
CC       22-deacetylyanuthone A (PubMed:24684908). O-Mevalon transferase yanI
CC       then attaches mevalon to the hydroxyl group of 22-deacetylyanuthone A
CC       to produce yanuthone E (PubMed:24684908). Finally, the FAD-dependent
CC       monooxygenase yanF oxidizes the hydroxyl group at C15 of yanuthone E to
CC       form yanuthone D (PubMed:24684908). Furthermore, several branching
CC       points in the pathway lead to the production of yanuthones F and G from
CC       7-deacetoxyyanuthone A; yanuthones H and I from 22-deacetylyanuthone A;
CC       and yanuthone J from yanuthone E (PubMed:24684908). YanE is also
CC       involved in the synthesis of yanuthone X1 which does not have 6-
CC       methylsalicylic acid (6-MSA) as precursor (PubMed:24684908).
CC       {ECO:0000269|PubMed:24684908}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:24684908}.
CC   -!- DISRUPTION PHENOTYPE: Loses the ability to produce yanuthone D
CC       (PubMed:24684908). Leads also to the loss of production of yanuthone X1
CC       which does not have 6-methylsalicylic acid (6-MSA) as a precursor
CC       (PubMed:24684908). {ECO:0000269|PubMed:24684908}.
CC   -!- BIOTECHNOLOGY: Yanuthone D is an antibiotic against C.albicans,
CC       methicillin-resistant S.aureus (MRSA), and vancomycin-resistant
CC       Enterococcus (PubMed:11031048). {ECO:0000269|PubMed:11031048}.
CC   -!- SIMILARITY: Belongs to the oxidoreductase OpS7 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EHA22200.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; ACJE01000012; EHA22200.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; G3Y423; -.
DR   EnsemblFungi; EHA22200; EHA22200; ASPNIDRAFT_192604.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1185488; -.
DR   HOGENOM; CLU_068080_1_0_1; -.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000009038; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   1: Evidence at protein level;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..257
FT                   /note="Probable oxidoreductase yanE"
FT                   /id="PRO_0000436769"
SQ   SEQUENCE   257 AA;  29214 MW;  0A5E1ED491B5089E CRC64;
     MAPCKPRTFT AGEDPLTKFD GAISVATMPR PADRQFLFHG IMRPSRGIYA KLVATGKKPP
     THFHPSQWEF FRVLRGNLTV DINGVPVHRT VDDGEMAVPP YTHHVIYGTP GTEMNEVEFL
     VSATDEEEGA TAMDQEFFEN WYGYQEDIFQ RGEKIDLIQV LAMFDAGGTY LSPPWWVPFR
     AWVGLILGIV IGRWIGGLLG YAPFYPEWTT NWDAACDRME QSWFQRRYAD RGAQQRAREK
     FQVQKGQGTV AKGEKSE
 
 
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