FUSA5_GIBZE
ID FUSA5_GIBZE Reviewed; 522 AA.
AC A0A098DDI4; A0A0E0RZ12;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 07-JAN-2015, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Cytochrome P450 monooxygenase FGSG_08207 {ECO:0000303|PubMed:25412204};
DE EC=1.-.-.- {ECO:0000305|PubMed:25412204};
DE AltName: Full=Fusaristatin A biosynthesis cluster protein FGSG_08207 {ECO:0000303|PubMed:25412204};
GN ORFNames=FGRAMPH1_01T09369, FGSG_08207 {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: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of the lipopeptide fusaristatin A
CC (PubMed:25412204). Fusaristatin A consists of a polyketide chain linked
CC to three amino acid residues glutamine (Gln), dehydroalanine (dehydro-
CC Ala), and beta-aminoisobutyric acid (PubMed:25412204). The biosynthesis
CC starts with formation of a linear polyketide chain by the highly
CC reducing polyketide synthase PKS6 (PubMed:25412204). The gene cluster
CC does not contain an acyl-CoA ligase or an acyl-transferase, and it is
CC therefore predicted that the polyketide is transferred directly to the
CC nonribosomal peptide synthetase NRPS7 (Probable). Modules 1-3 from
CC NRPS7 incorporate dehydro-Ala, Gln, and beta-aminoisobutyric acid in
CC the compound, which is released by cyclization (PubMed:25412204). The
CC beta-aminoisobutyric acid units are most likely not freely available to
CC the NRPS, but can be synthesized from thymine, which requires a
CC dehydrogenase, a monooxygenase, and an aminotransferase. The
CC fusaristatin A cluster contains a cytochrome P450 monooxygenase
CC (FGSG_08207) and an aminotransferase (FGSG_17085), which theoretically
CC can perform two of the enzymatic steps (Probable). The enzymes may
CC however also be involved in biosynthesis of dehydroalanine or
CC modification of the polyketide (Probable). The dehydro-Ala residue can
CC be a result of cyclization, where serine is dehydrated (Probable). The
CC last gene of the cluster encodes a protein with an A/B barrel domain
CC found in variable enzymes, which hampers functional prediction
CC (Probable). {ECO:0000269|PubMed:25412204, ECO:0000305|PubMed:25412204}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:25412204}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; HG970333; CEF76487.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A098DDI4; -.
DR SMR; A0A098DDI4; -.
DR STRING; 5518.FGSG_08207P0; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G09369; -.
DR eggNOG; KOG0684; Eukaryota.
DR Proteomes; UP000070720; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..522
FT /note="Cytochrome P450 monooxygenase FGSG_08207"
FT /id="PRO_0000445368"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 441
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 522 AA; 58938 MW; 1594A67D2956486B CRC64;
MALTEGISEL LLSKPVVLGL AACALLFLIG RAFEPTVDAL EPPMLRPSIP IFGHFYSMMK
DQEAFFKRLD KKYHMPIATV PILKYKMYAI TDPILVQSAY CNKNLSFTPF AINGAQKVTG
FDDDYHKVLM ETNVLPEYFK SLYDGTTAQH IHQLNVTSLK HVSQHINSIQ ENGMTIDNTY
LWLRNLMTVA TCEALYGPDN PIRSDSLVED IWTFETGLAY LFFHIFNSKT LQRTKEARRR
IQLALGKWCT NMRQDDERVS AYIRNRVGIL RNYGVEGQKL GDIEVGLIHV PTSNSIPTLF
WFFMHVFTRP DVVEQMRAEV EHIVQRGPDE TVTVNIDDIL ERCPLMISAY REASRLCNGF
TCNRIVMEET TITDRHGRSY LLKKGSSVKM PAGVMHASQE VWGEDAAVFR ADRFLDKGLT
SEQAKLRRAA LTPFGGGAHM CPGRNFATAE IYGFMTALLL GYNVEPVDGK WDAFKPPPMA
TCPQSTSVCK PEDEASVCGT RLIRRSGWEG AQWKFVSGKV TE