AURF_GIBZE
ID AURF_GIBZE Reviewed; 527 AA.
AC I1RF61;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Monooxygenase aurF {ECO:0000303|PubMed:16879655};
DE EC=1.-.-.- {ECO:0000305};
DE AltName: Full=Aurofusarin biosynthesis cluster protein F {ECO:0000303|PubMed:16879655};
DE AltName: Full=Gibberella pigment protein 8 {ECO:0000303|PubMed:16461721};
DE Flags: Precursor;
GN Name=aurF {ECO:0000303|PubMed:16879655};
GN Synonyms=GIP8 {ECO:0000303|PubMed:16461721};
GN ORFNames=FG02327, FGRAMPH1_01T05599;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP FUNCTION.
RX PubMed=15811992; DOI=10.1128/aem.71.4.1701-1708.2005;
RA Kim J.E., Han K.H., Jin J., Kim H., Kim J.C., Yun S.H., Lee Y.W.;
RT "Putative polyketide synthase and laccase genes for biosynthesis of
RT aurofusarin in Gibberella zeae.";
RL Appl. Environ. Microbiol. 71:1701-1708(2005).
RN [5]
RP FUNCTION, AND PATHWAY.
RX PubMed=15809006; DOI=10.1016/j.fgb.2005.01.010;
RA Malz S., Grell M.N., Thrane C., Maier F.J., Rosager P., Felk A.,
RA Albertsen K.S., Salomon S., Bohn L., Schaefer W., Giese H.;
RT "Identification of a gene cluster responsible for the biosynthesis of
RT aurofusarin in the Fusarium graminearum species complex.";
RL Fungal Genet. Biol. 42:420-433(2005).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND PATHWAY.
RX PubMed=16879655; DOI=10.1111/j.1365-2958.2006.05295.x;
RA Frandsen R.J., Nielsen N.J., Maolanon N., Soerensen J.C., Olsson S.,
RA Nielsen J., Giese H.;
RT "The biosynthetic pathway for aurofusarin in Fusarium graminearum reveals a
RT close link between the naphthoquinones and naphthopyrones.";
RL Mol. Microbiol. 61:1069-1080(2006).
RN [7]
RP INDUCTION.
RX PubMed=16461721; DOI=10.1128/aem.72.2.1645-1652.2006;
RA Kim J.E., Jin J., Kim H., Kim J.C., Yun S.H., Lee Y.W.;
RT "GIP2, a putative transcription factor that regulates the aurofusarin
RT biosynthetic gene cluster in Gibberella zeae.";
RL Appl. Environ. Microbiol. 72:1645-1652(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND PATHWAY.
RX PubMed=21296881; DOI=10.1074/jbc.m110.179853;
RA Frandsen R.J., Schuett C., Lund B.W., Staerk D., Nielsen J., Olsson S.,
RA Giese H.;
RT "Two novel classes of enzymes are required for the biosynthesis of
RT aurofusarin in Fusarium graminearum.";
RL J. Biol. Chem. 286:10419-10428(2011).
RN [9]
RP FUNCTION.
RX PubMed=23557488; DOI=10.1186/1475-2859-12-31;
RA Rugbjerg P., Naesby M., Mortensen U.H., Frandsen R.J.;
RT "Reconstruction of the biosynthetic pathway for the core fungal polyketide
RT scaffold rubrofusarin in Saccharomyces cerevisiae.";
RL Microb. Cell Fact. 12:31-31(2013).
CC -!- FUNCTION: Monooxygenase; part of the gene cluster that mediates the
CC biosynthesis of aurofusarin, a red mycelium pigment which is acting as
CC a mycotoxin (PubMed:15811992, PubMed:15809006, PubMed:16879655). The
CC first step is performed by the polyketide synthase which condenses one
CC acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the
CC cyclic heptaketide and yellow pigment YWA1 (PubMed:21296881,
CC PubMed:23557488). The C2 hydroxyl group in the pyrone ring of YWA1 is
CC probably formed during ring closure by an aldol-type cyclization
CC reaction (PubMed:21296881). The dehydratase aurZ then acts as the first
CC tailoring enzyme in the aurofusarin biosynthetic pathway by converting
CC YWA1 to nor-rubrofusarin (PubMed:21296881, PubMed:23557488). Nor-
CC rubrofusarin is then methylated to rubrofusarin by the O-
CC methyltransferase aurJ (PubMed:21296881, PubMed:23557488). Rubrofusarin
CC is then transported across the plasma membrane by the rubrofusarin-
CC specific pump aurT for further enzymatic processing by the
CC extracellular complex composed of GIP1, aurF, aurO and aurS to yield
CC aurofusarin (PubMed:21296881). {ECO:0000269|PubMed:15809006,
CC ECO:0000269|PubMed:15811992, ECO:0000269|PubMed:16879655,
CC ECO:0000269|PubMed:21296881, ECO:0000269|PubMed:23557488}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:15809006,
CC ECO:0000269|PubMed:16879655, ECO:0000269|PubMed:21296881}.
CC -!- SUBUNIT: Might be part of an extracellular enzyme complex composed of
CC GIP1, aurF, aurO and aurS (PubMed:21296881).
CC {ECO:0000305|PubMed:21296881}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:21296881}. Secreted,
CC extracellular space {ECO:0000305|PubMed:21296881}.
CC -!- INDUCTION: Expression is regulated by the aurofusarin biosynthesis
CC cluster-specific transcription factor aurR1/GIP2 (PubMed:16879655,
CC PubMed:16461721). {ECO:0000269|PubMed:16461721,
CC ECO:0000269|PubMed:16879655}.
CC -!- DISRUPTION PHENOTYPE: Impairs autofusarin biosynthesis and leads to a
CC yellow pigmentation via accumulation of the intermediate rubrofusarin
CC (PubMed:16879655). {ECO:0000269|PubMed:16879655}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR EMBL; HG970332; CEF74604.1; -; Genomic_DNA.
DR RefSeq; XP_011318236.1; XM_011319934.1.
DR AlphaFoldDB; I1RF61; -.
DR SMR; I1RF61; -.
DR STRING; 229533.I1RF61; -.
DR GeneID; 23549709; -.
DR KEGG; fgr:FGSG_02327; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G05599; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006909_8_1_1; -.
DR InParanoid; I1RF61; -.
DR BioCyc; MetaCyc:MON-19451; -.
DR Proteomes; UP000070720; Chromosome 1.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR Pfam; PF00743; FMO-like; 1.
DR PIRSF; PIRSF000332; FMO; 1.
DR PRINTS; PR00370; FMOXYGENASE.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Glycoprotein; Monooxygenase; NADP; Oxidoreductase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..527
FT /note="Monooxygenase aurF"
FT /evidence="ECO:0000255"
FT /id="PRO_0000441092"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 527 AA; 59656 MW; 531F973F7FCE80D6 CRC64;
MPNPTVAIVG LGALGLVTLK NLREEGFDAV GLDRNDYVGG LWHFEEGNKL TVMRSTLSNG
SKQRGCFTDF PFPEDSPDFI PAEGIDRYLK DYAKHFGLLE HCRLRTSFHG ARYDEKKQQW
RLSLSTPDAP EPHFEWFDKV VFAMGADQIP SRPKIEGIEK FKGHVEHSMS FKNPETLAGK
RVMVLGFGNT AADMATELAP IADQVYLAHR HGAIIVPRWV KGKPVDHVRT YRKYVILNLM
NRYTPGLWEK TMNSVIGKLV HNTFDLKPEW RFDPAPSITN QRPLVNDELI PSLEKGSIIS
THGLARVIDE NTVETSDGQR YEVDAILFCT GFTVDYSVVG MDADPCRATT TDWQKSRGFT
GRPLPRLYQN IFSLDHPETL AFIGHLSFMN PAFFMFDLAS MAVAQLWKDP SGFPSKAEMN
KQVDDQHAWV IDLAKKGPVT PSIVKASEWM EWVDRVIGSG LPEHLGYTMK GWNFWMRDRK
FCNIMMDGLL SPHAYRVFPG KRKAWPGARD AIIAMNADRE ARFGPMD
