YANF_ASPNA
ID YANF_ASPNA Reviewed; 580 AA.
AC G3Y424;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=FAD-dependent monooxygenase yanF {ECO:0000303|PubMed:24684908};
DE EC=1.-.-.- {ECO:0000305|PubMed:24684908};
DE AltName: Full=Yanuthone D biosynthesis cluster protein F {ECO:0000303|PubMed:24684908};
GN Name=yanF {ECO:0000303|PubMed:24684908}; ORFNames=ASPNIDRAFT_44970;
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: FAD-dependent monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of yanuthone D, a fungal isoprenoid
CC epoxycyclohexenone that acts as an antibiotic against fungi and
CC bacteria (PubMed:24684908). The first step of the pathway is the
CC synthesis of 6-methylsalicylic acid (6-MSA) by the polyketide synthase
CC yanA (PubMed:24684908). 6-MSA is then converted to m-cresol by the
CC decarboxylase yanB (PubMed:24684908). The cytochrome P450 monooxygenase
CC yanC then catalyzes the oxidation of m-cresol to toluquinol
CC (PubMed:24684908). Epoxidation of toluquinol is then performed by the
CC short chain dehydrogenase yanD, with the help of yanE, and a further
CC prenylated by yanG leads to 7-deacetoxyyanuthone A (PubMed:24684908).
CC The next step is the hydroxylation of C-22 of 7-deacetoxyyanuthone A by
CC the cytochrome P450 monooxygenase yanH to yield 22-deacetylyanuthone A
CC (PubMed:24684908). O-Mevalon transferase yanI then attaches mevalon to
CC the hydroxyl group of 22-deacetylyanuthone A to produce yanuthone E
CC (PubMed:24684908). Finally, the FAD-dependent monooxygenase yanF
CC oxidizes the hydroxyl group at C15 of yanuthone E to form yanuthone D
CC (PubMed:24684908). Furthermore, several branching points in the pathway
CC lead to the production of yanuthones F and G from 7-deacetoxyyanuthone
CC A; yanuthones H and I from 22-deacetylyanuthone A; and yanuthone J from
CC yanuthone E (PubMed:24684908). {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, but
CC accumulates yanuthone E (PubMed:24684908).
CC {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 oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; ACJE01000012; EHA22201.1; -; Genomic_DNA.
DR AlphaFoldDB; G3Y424; -.
DR SMR; G3Y424; -.
DR EnsemblFungi; EHA22201; EHA22201; ASPNIDRAFT_44970.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1216498; -.
DR HOGENOM; CLU_018354_1_2_1; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000009038; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT CHAIN 1..580
FT /note="FAD-dependent monooxygenase yanF"
FT /id="PRO_0000436764"
FT DOMAIN 150..322
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 187
FT /note="Pros-8alpha-FAD histidine"
FT /evidence="ECO:0000250|UniProtKB:P08159"
SQ SEQUENCE 580 AA; 62014 MW; 7C8D0EF3F734DB09 CRC64;
MSSSAECRPI GWGGWGPDPN TSPTRAAIKW FADPRSLHHQ QCACGLWNAR RAMQWVIPAP
PRIWIDDQPR MVKLAYILGA VTVFLTSGNA ADVSPTSSVA ASTTPSAADS LSSLGLSLPA
GNVLVGNNET FTASSPYYEP LIDEAWSGNC RLNASCIVTP KSAQEVSLVI QVLSILDTKF
SIRSGGHSSS PGFSSIGSNG VLVALERLNT LSISADRKTL TVGPGNRWEA VYQYLEQYNL
TVLGGREPVV GVGGFVLGGG LSLFYNTNGL AIDTVTRFQV VTPNGTIVNA TPTEHADLYK
GLKGGLNNFG IIVEYDLTTN TGIDVWFEVK NYTRAETPAL LAAYATYLQN ADVRSNVEIQ
ANPAYTVVLY GYLDHVSAPS AFNAFSTVPS VSTVYPPTNA SLNEVLLEIG TAGVTGSSWT
YTVSFSFKVT NPDFLQESYK TYLEAAASLL PSGVLLEYVP QGIIPNLVTK GQAQNGGNLL
GLEATPQVWG EIFAQFPATV SQSTVASAVN DLLAKITSSA ESQGVHLPYI FANDAGPDQQ
VLRGYGEDNL KYIATVAERY DPKGVMQKLQ NDAYFVSKEL