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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
 
 
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