GRA15_GIBZE
ID GRA15_GIBZE Reviewed; 381 AA.
AC I1R9B5; A0A098D0B1;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=2-oxoglutarate-dependent dioxygenase FGSG_00048 {ECO:0000303|PubMed:30395461};
DE EC=1.14.-.- {ECO:0000305|PubMed:30395461};
DE AltName: Full=Gramillins biosynthesis cluster protein FGSG_00048 {ECO:0000303|PubMed:30395461};
GN ORFNames=FG00048, FGRAMPH1_01T00155, FGSG_00048;
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, AND PATHWAY.
RX PubMed=30395461; DOI=10.1021/jacs.8b10017;
RA Bahadoor A., Brauer E.K., Bosnich W., Schneiderman D., Johnston A.,
RA Aubin Y., Blackwell B., Melanson J.E., Harris L.J.;
RT "Gramillin A and B: cyclic lipopeptides identified as the nonribosomal
RT biosynthetic products of Fusarium graminearum.";
RL J. Am. Chem. Soc. 140:16783-16791(2018).
CC -!- FUNCTION: 2-oxoglutarate-dependent dioxygenase; part of the gene
CC cluster that mediates the biosynthesis of gramillins A and B, bicyclic
CC lipopeptides that induce cell death in maize leaves but not in wheat
CC leaves (PubMed:30395461). The nonribosomal peptide synthetase GRA1
CC incorporates respectively a glutamic adic (Glu), a leucine (Leu), a
CC serine (Ser), a hydroxyglutamine (HOGln), a 2-amino decanoic acid, and
CC 2 cysteins (CysB and CysA) (Probable). The biosynthesis of 2-amino
CC decanoic acid incorporated in gramillins could be initiated by a fatty
CC acid synthase composed of the alpha and beta subunits FGSG_00036 and
CC FGSG_11656 (Probable). The cytochrome P450 monooxygenase FGSG_15680
CC could hydroxylate the fatty acid chain (Probable). Subsequent oxidation
CC to the ketone by the oxidoreductase FGSG_00048 and transamination by
CC aminotransferase FGSG_00049 could form 2-amino-decanoic acid
CC (Probable). On the other hand, FGSG_15680 could also be responsible for
CC the HO-modified glutamine at the gamma-position (Probable). Whether
CC hydroxylation occurs on the fully assembled product or on the Gln
CC residue prior to assembly into the gramillins requires further proof
CC (Probable). The thioredoxin FGSG_00043 could also be required for the
CC disulfide-bond formation between CysA and CysB (Probable). The specific
CC involvement of the remaining proteins from the cluster is more
CC difficult to discern, but could have broader regulatory (FGSG_00040 and
CC FGSG_11657) or enzymatic functions (FGSG_00044 and FGSG_00045)
CC (Probable). The final C-domain of GRA1 does not possess the expected
CC sequence of a termination CT domain, often implicated in
CC macrocyclization and release of a cyclopeptidein fungal NRPs; and the
CC thioesterase FGSG_00047 may act in concert with the terminal C-domain
CC of GRA1 to catalyze the formation of the macrocyclic anhydride and
CC release of the products (Probable). {ECO:0000269|PubMed:30395461,
CC ECO:0000305|PubMed:30395461}.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:30395461}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HG970332; CEF71877.1; -; Genomic_DNA.
DR RefSeq; XP_011315637.1; XM_011317335.1.
DR AlphaFoldDB; I1R9B5; -.
DR SMR; I1R9B5; -.
DR STRING; 5518.FGSG_00048P0; -.
DR GeneID; 23547564; -.
DR KEGG; fgr:FGSG_00048; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G00155; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_1_1_1; -.
DR InParanoid; I1R9B5; -.
DR Proteomes; UP000070720; Chromosome 1.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW Virulence.
FT CHAIN 1..381
FT /note="2-oxoglutarate-dependent dioxygenase FGSG_00048"
FT /id="PRO_0000450566"
SQ SEQUENCE 381 AA; 42393 MW; 5F9AB43062C2D924 CRC64;
MASNFTSIPV LDYPSSLSPS TKPAFLAELR DALVKVGFFQ VRDPPIPLKL QQDALRLSAQ
FFDLPTEKKL DIENVHSKRF LGYSRINSES TASGTDYLES ILLGPNLPEL GPEEPVYLHL
QGPSQWPDEV SVPGFRDVLE SYHSQIQDFS IEFARLIAEA LEMPLDTLTK LLGQPLFSRL
KPTRYLPPSM NPAAEDGSHG IGPHKDIAFM TYLLQGGTHN CLEVQNKLGH WVPVPPVPGA
LVVNIGRLLE VITGGVCVAT THRVILKRQG FVDGDGKSLG PRISLPFFQF VNPRLTVDDV
LVDVPHHIKD LVPDQVATTE AETFFSGLFN NCIGDNIFVN HLTTYPRVGK RWYPDLMQLA
SEKQAESKRL DEQRRATEGH I
