ID   FUSA4_GIBZE             Reviewed;         138 AA.
AC   I1RVD6;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Fusaristatin A biosynthesis cluster protein FGSG_08206 {ECO:0000303|PubMed:25412204};
GN   ORFNames=FGRAMPH1_01T09367, FGSG_08206 {ECO:0000303|PubMed:25412204};
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   IDENTIFICATION, FUNCTION, AND PATHWAY.
RX   PubMed=25412204; DOI=10.1021/np500436r;
RA   Soerensen J.L., Sondergaard T.E., Covarelli L., Fuertes P.R., Hansen F.T.,
RA   Frandsen R.J., Saei W., Lukassen M.B., Wimmer R., Nielsen K.F.,
RA   Gardiner D.M., Giese H.;
RT   "Identification of the biosynthetic gene clusters for the lipopeptides
RT   fusaristatin A and W493 B in Fusarium graminearum and F.
RT   pseudograminearum.";
RL   J. Nat. Prod. 77:2619-2625(2014).
CC   -!- FUNCTION: Part of the gene cluster that mediates the biosynthesis of
CC       the lipopeptide fusaristatin A (PubMed:25412204). Fusaristatin A
CC       consists of a polyketide chain linked to three amino acid residues
CC       glutamine (Gln), dehydroalanine (dehydro-Ala), and beta-aminoisobutyric
CC       acid (PubMed:25412204). The biosynthesis starts with formation of a
CC       linear polyketide chain by the highly reducing polyketide synthase PKS6
CC       (PubMed:25412204). The gene cluster does not contain an acyl-CoA ligase
CC       or an acyl-transferase, and it is therefore predicted that the
CC       polyketide is transferred directly to the nonribosomal peptide
CC       synthetase NRPS7 (Probable). Modules 1-3 from NRPS7 incorporate
CC       dehydro-Ala, Gln, and beta-aminoisobutyric acid in the compound, which
CC       is released by cyclization (PubMed:25412204). The beta-aminoisobutyric
CC       acid units are most likely not freely available to the NRPS, but can be
CC       synthesized from thymine, which requires a dehydrogenase, a
CC       monooxygenase, and an aminotransferase. The fusaristatin A cluster
CC       contains a cytochrome P450 monooxygenase (FGSG_08207) and an
CC       aminotransferase (FGSG_17085), which theoretically can perform two of
CC       the enzymatic steps (Probable). The enzymes may however also be
CC       involved in biosynthesis of dehydroalanine or modification of the
CC       polyketide (Probable). The dehydro-Ala residue can be a result of
CC       cyclization, where serine is dehydrated (Probable). The last gene of
CC       the cluster encodes a protein with an A/B barrel domain found in
CC       variable enzymes, which hampers functional prediction (Probable).
CC       {ECO:0000269|PubMed:25412204, ECO:0000305|PubMed:25412204}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:25412204}.
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DR   EMBL; HG970333; CEF76486.1; -; Genomic_DNA.
DR   RefSeq; XP_011320601.1; XM_011322299.1.
DR   AlphaFoldDB; I1RVD6; -.
DR   SMR; I1RVD6; -.
DR   STRING; 5518.FGSG_08206P0; -.
DR   GeneID; 23555231; -.
DR   KEGG; fgr:FGSG_08206; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G09367; -.
DR   eggNOG; ENOG502STNI; Eukaryota.
DR   HOGENOM; CLU_120569_0_1_1; -.
DR   InParanoid; I1RVD6; -.
DR   Proteomes; UP000070720; Chromosome 2.
DR   InterPro; IPR013097; Dabb.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   Pfam; PF07876; Dabb; 1.
DR   SMART; SM00886; Dabb; 1.
DR   SUPFAM; SSF54909; SSF54909; 1.
DR   PROSITE; PS51502; S_R_A_B_BARREL; 1.
PE   4: Predicted;
KW   Reference proteome.
FT   CHAIN           1..138
FT                   /note="Fusaristatin A biosynthesis cluster protein
FT                   FGSG_08206"
FT                   /id="PRO_0000445372"
FT   DOMAIN          33..130
FT                   /note="Stress-response A/B barrel"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00835"
SQ   SEQUENCE   138 AA;  15615 MW;  D332EADBD23579B4 CRC64;
     MFAFKRSSCY FQVSNKIVKN GQIRGYISVA DRVHRVTMFK MPKAEDQQRF LEQCRKMAAD
     NQRNGSPYIL SMVAGPAEDG PRTEGYTFVN KTEFASMEDM KYYETECPAH GEVKKVLGEI
     TIDGMMTVFF KPQATGGA