AURJ_GIBZE
ID AURJ_GIBZE Reviewed; 439 AA.
AC I1RF60;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=O-methyltransferase aurJ {ECO:0000303|PubMed:16879655};
DE EC=2.1.1.- {ECO:0000269|PubMed:23557488};
DE AltName: Full=Aurofusarin biosynthesis cluster protein J {ECO:0000303|PubMed:16879655};
DE AltName: Full=Gibberella pigment protein 7 {ECO:0000303|PubMed:16461721};
GN Name=aurJ {ECO:0000303|PubMed:23557488};
GN Synonyms=GIP7 {ECO:0000303|PubMed:16461721};
GN ORFNames=FG02326, FGRAMPH1_01T05597;
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.
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, CATALYTIC ACTIVITY, AND PATHWAY.
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: O-methyltransferase; part of the gene cluster that mediates
CC the biosynthesis of aurofusarin, a red mycelium pigment which is acting
CC as 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 -!- CATALYTIC ACTIVITY:
CC Reaction=norrubrofusarin + S-adenosyl-L-methionine = H(+) +
CC rubrofusarin + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:62684,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:145839, ChEBI:CHEBI:145894;
CC Evidence={ECO:0000269|PubMed:23557488};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62685;
CC Evidence={ECO:0000269|PubMed:23557488};
CC -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:15809006,
CC ECO:0000269|PubMed:16879655, ECO:0000269|PubMed:23557488}.
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 -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family. COMT
CC subfamily. {ECO:0000305}.
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DR EMBL; HG970332; CEF74603.1; -; Genomic_DNA.
DR RefSeq; XP_011318235.1; XM_011319933.1.
DR AlphaFoldDB; I1RF60; -.
DR SMR; I1RF60; -.
DR GeneID; 23549708; -.
DR KEGG; fgr:FGSG_02326; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G05597; -.
DR eggNOG; ENOG502SIYN; Eukaryota.
DR HOGENOM; CLU_005533_1_4_1; -.
DR InParanoid; I1RF60; -.
DR BioCyc; MetaCyc:MON-19449; -.
DR Proteomes; UP000070720; Chromosome 1.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00891; Methyltransf_2; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..439
FT /note="O-methyltransferase aurJ"
FT /id="PRO_0000441088"
FT ACT_SITE 338
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 283
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 439 AA; 48089 MW; F4C18EEAE425AE18 CRC64;
MGSISSPSLI IDLANAVSSA AKNLDTQLQS QGFPQPSFEA DGPTYVVPKD APKAAHEARV
ATAEAALKLF NLVSGPSELL PNMTASYHTI FALQWLHHFD VFSHIPLDGS LSYEKLATKA
NVPESLLKSV ARMAMTSNIL AEPTTGQVAH SANSAMFVKF PNMRDWASYM FTASIPTAAA
MVQATEKWPG SVKKTETAYN IAFNHDLPFF DHLSQSPVMT KQFSGYMRSV TDGQGMDLSH
LVNGFDWASL PDKSLIVDIG GSAGHASYAL AAAYPHLRFE VQDLDTVVNG EKAAKEHEEA
VSKHVIGTDN RVTFKAHNFF EAQPTKDATV YMLRMIIHDW PDAEAKTILG NLVPALESAK
ATLLIMDTVL PSPGSIPSVR ERVIRTRDLT MRQVFNAKER GVDDWEAILR ETDSRLTLKN
LRQPEGSNMC LLTISLQDD
