GRA3_GIBZE
ID GRA3_GIBZE Reviewed; 740 AA.
AC I1S490; A0A098CZ17;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Gramillins biosynthetic cluster protein FGSG_11657 {ECO:0000303|PubMed:30395461};
GN ORFNames=FGRAMPH1_01T00139, FGSG_11657;
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: Part of the gene cluster that mediates the biosynthesis of
CC gramillins A and B, bicyclic lipopeptides that induce cell death in
CC maize leaves but not in wheat leaves (PubMed:30395461). The
CC nonribosomal peptide synthetase GRA1 incorporates respectively a
CC glutamic adic (Glu), a leucine (Leu), a serine (Ser), a
CC hydroxyglutamine (HOGln), a 2-amino decanoic acid, and 2 cysteins (CysB
CC and CysA) (Probable). The biosynthesis of 2-amino decanoic acid
CC incorporated in gramillins could be initiated by a fatty acid synthase
CC composed of the alpha and beta subunits FGSG_00036 and FGSG_11656
CC (Probable). The cytochrome P450 monooxygenase FGSG_15680 could
CC hydroxylate the fatty acid chain (Probable). Subsequent oxidation to
CC 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 -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:30395461}.
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DR EMBL; HG970332; CEF71869.1; -; Genomic_DNA.
DR RefSeq; XP_011315628.1; XM_011317326.1.
DR AlphaFoldDB; I1S490; -.
DR GeneID; 23558476; -.
DR KEGG; fgr:FGSG_11657; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G00139; -.
DR HOGENOM; CLU_375072_0_0_1; -.
DR Proteomes; UP000070720; Chromosome 1.
DR InterPro; IPR013860; AreA_GATA.
DR Pfam; PF08550; DUF1752; 1.
PE 4: Predicted;
KW Reference proteome; Virulence.
FT CHAIN 1..740
FT /note="Gramillins biosynthetic cluster protein FGSG_11657"
FT /id="PRO_0000450568"
FT REGION 353..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 740 AA; 81149 MW; 4B6FB9FD22B950DF CRC64;
MPTPVESHSL LHSGLTLCGS IISVNQDRRK TSTLGCVIQV GSGFYGLTAA HAVRKSRAYP
TLPLNSHTDE GLGAASDGPM TSHVLRNWQN PFMACKNAEA VELDDHSTSE VAVDESVEDV
DFVTDVEYED LREDDDNHGD DSTTSMPNDV FHEDYLTSAP QEGMMETQAM FLSIPELNDK
CLVSRRARPN MAHRVTHGDS GSIVIDARTN VVYGHVVASN PLGEIYISPI GATLEQIQSH
FPGSKVSLPD PLTILTGLAT FGHETIGRKR ARYPDKLRNL GLSPDTEYTR LVTPTANKSL
DFSNYPKFHY FHQCSEDSSS NRRVNEVEKS QPANLTLDCN TVELGLRQST WHQADSPVPL
SSVKEESGLG KLARSPAEPA PSRPLPGSSI PVVISQSTGR ELYSNGVTEA TLSSKLSDEA
EADTSIKPDS DAASPTDCRI IGHLRTRPVG LERDLSSTYN AALSMDQDPE ELLQQDIFPM
RVWRSLSTLK QRLPSQERLE NLTWRMTHIN LRKPKEQEEP KRHRTSNNSI VGSSDIADVG
KTSKQKAIQP NIVELDVVTS PENIPLPASL VPISSSEATW QVDKKSVSSV TFGQSSGCFP
PSYQGFRPDA PEKGNLPRAT TTSYHLPPQP IGWPTCIPSN MKWHSLVNMS TLAADEHEGE
GRADTNRHVS TQSNMPTEQS LLPQGDESVP PTCTNCFTLT CDILARNENV DQLAIDAPGH
ITSAKAVYNL YTFISYLLIF
