AURS_GIBZE
ID AURS_GIBZE Reviewed; 407 AA.
AC I1RF63;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Aurofusarin biosynthesis cluster protein S {ECO:0000303|PubMed:21296881};
DE AltName: Full=Gibberella pigment protein 9 {ECO:0000303|PubMed:16461721};
DE Flags: Precursor;
GN Name=aurS {ECO:0000303|PubMed:21296881};
GN Synonyms=GIP9 {ECO:0000303|PubMed:16461721};
GN ORFNames=FG02329, FGRAMPH1_01T05603;
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, 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, DISRUPTION PHENOTYPE, 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: Part of the gene cluster that mediates the biosynthesis of
CC aurofusarin, a red mycelium pigment which is acting as a mycotoxin
CC (PubMed:15811992, PubMed:15809006, PubMed:16879655). The first step is
CC performed by the polyketide synthase which condenses one acetyl-CoA and
CC 6 malonyl-CoA units to form the first intermediate, the cyclic
CC heptaketide and yellow pigment YWA1 (PubMed:21296881, PubMed:23557488).
CC The C2 hydroxyl group in the pyrone ring of YWA1 is probably formed
CC during ring closure by an aldol-type cyclization reaction
CC (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 -!- 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:21296881). {ECO:0000269|PubMed:21296881}.
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DR EMBL; HG970332; CEF74606.1; -; Genomic_DNA.
DR RefSeq; XP_011318238.1; XM_011319936.1.
DR AlphaFoldDB; I1RF63; -.
DR SMR; I1RF63; -.
DR STRING; 229533.I1RF63; -.
DR GeneID; 23549711; -.
DR KEGG; fgr:FGSG_02329; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G05603; -.
DR eggNOG; KOG1437; Eukaryota.
DR HOGENOM; CLU_778873_0_0_1; -.
DR InParanoid; I1RF63; -.
DR Proteomes; UP000070720; Chromosome 1.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR Gene3D; 2.30.180.10; -; 2.
DR InterPro; IPR036378; FAS1_dom_sf.
DR InterPro; IPR000782; FAS1_domain.
DR Pfam; PF02469; Fasciclin; 2.
DR SMART; SM00554; FAS1; 2.
DR SUPFAM; SSF82153; SSF82153; 2.
DR PROSITE; PS50213; FAS1; 2.
PE 1: Evidence at protein level;
KW Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..407
FT /note="Aurofusarin biosynthesis cluster protein S"
FT /evidence="ECO:0000255"
FT /id="PRO_0000441090"
FT DOMAIN 52..192
FT /note="FAS1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 195..365
FT /note="FAS1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 407 AA; 45574 MW; 21DF233859F67FFF CRC64;
MSKQKPSLWR ALRALSFIIS IPLLIQYLVL KWYSTSQNTP TPVFHEPNHE TNLTVWEVLS
NDDRVSKFVD VIGKLPDIVR GLSAPQARFT VYAPVNEAFD SFYFPPDPPP FFGLFIAGCH
MGPGPVPAER LPSMGTVSSF VNGDIFFTYK QRISVQKDKS GLTLNRAARV LPVNASQSIA
VNGFVHHIDT VLELPNSTAH ALRTRPELSK LRRGLEATKL SESIYDTNAH VSQTIFAPTN
AAFDRLGKTA TKFLFSHGGR PYLRALLKYH VVANKTLFSD SYWPHGGAKL MDLSLIPNKD
SHQFDLPTLH NNLTLQVESR KIHKKWHLNV LKDQVAEGKS HDSIPVSMPD VILMDGVMHF
IDSILLPPAK SEQRKTSWLS RLKSSLGHNK QSIEDLVTLL GPYIDEP
