CHRY5_GIBZE
ID CHRY5_GIBZE Reviewed; 506 AA.
AC I1S3L1; A0A098E3Z7;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=FAD-linked oxidoreductase chry5 {ECO:0000303|PubMed:28708398};
DE EC=1.-.-.- {ECO:0000305|PubMed:28708398};
DE AltName: Full=Chrysogine biosynthesis cluster protein 5 {ECO:0000303|PubMed:28708398};
DE Flags: Precursor;
GN Name=chry5 {ECO:0000303|PubMed:28708398};
GN ORFNames=FG11399, FGRAMPH1_01T21967;
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=28708398; DOI=10.1021/acs.jnatprod.6b00822;
RA Wollenberg R.D., Saei W., Westphal K.R., Klitgaard C.S., Nielsen K.L.,
RA Lysoee E., Gardiner D.M., Wimmer R., Sondergaard T.E., Soerensen J.L.;
RT "Chrysogine biosynthesis is mediated by a two-module nonribosomal peptide
RT synthetase.";
RL J. Nat. Prod. 80:2131-2135(2017).
CC -!- FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that
CC mediates the biosynthesis of the yellow pigment chrysogine
CC (PubMed:28708398). Pyruvic acid and anthranilic acid are likely
CC substrates for the nonribosomal peptide synthetase chry1/NRPS14, with
CC pyruvic acid adenylated by the first A domain and anthranilic acid by
CC the second (Probable). If pyruvic acid and anthranilic acid are merged
CC and released from chry1/NRPS14 by hydrolysis, a subsequent amidation
CC would lead to 2-pyruvoylaminobenzamide (Probable). This process is
CC probably catalyzed by the amidotransferase chry2 using glutamine as
CC amino donor (Probable). The dehydrogenase chry5 that has a terminal
CC berberine bridge domain for C-N cyclization could catalyze the
CC cyclization of 2-pyruvoylaminobenzamide to yield acetyl-4(3H)-
CC quinazolidinone (Probable). A final reduction of acetyl-4(3H)-
CC quinazolidinone catalyzed by the oxidoreductase chry4 would result in
CC chrysogine (Probable). {ECO:0000269|PubMed:28708398,
CC ECO:0000305|PubMed:28708398}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q5BEJ5};
CC -!- PATHWAY: Pigment biosynthesis. {ECO:0000305|PubMed:28708398}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; HG970334; CEF88821.1; -; Genomic_DNA.
DR RefSeq; XP_011325834.1; XM_011327532.1.
DR AlphaFoldDB; I1S3L1; -.
DR SMR; I1S3L1; -.
DR GeneID; 23558241; -.
DR KEGG; fgr:FGSG_11399; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G21967; -.
DR eggNOG; ENOG502SJ3M; Eukaryota.
DR HOGENOM; CLU_018354_0_1_1; -.
DR InParanoid; I1S3L1; -.
DR Proteomes; UP000070720; Chromosome 3.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..506
FT /note="FAD-linked oxidoreductase chry5"
FT /id="PRO_5010124794"
FT DOMAIN 59..241
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 506 AA; 55373 MW; 927E1A9F87EACAA3 CRC64;
MHLQALTGLA TLAVTAASQT LWSRDVDYKA LSKELSASAK VYFPGTEDFD AASKRWSNLD
KPTVNIVAVP ATENDVVEIT LDLTQANTLR QVKFANKKNL PFLAQNSAHG AITTLGQMKQ
GIEIYLNQLS GVKIAKDGKS VTILGGTASK KVTMGLWEAG KQTVTGCCEC VGYVGPALGG
GHGWLQGRHG LIADQFESMN IVLANGTLAT VDENSELWWA LKGAGHNFGI VTSVTSKTYD
AKIKNWAFAS LTFKGEKVEE LYETINKYIL KNGTQPTDLI NWSYWFNIPD LDPTGPIVQI
LLMQEGVDVV DKAYTGPFQE LKPLAVDAKK GVYTDLAKWV GVTTEDGPCQ KNGAMNPRFP
IYLQDYNPAA QKKAFNYFAD NIRGDSIFNG SLVTFDGYST EGVKAIDSKS TAFAYRNQNI
LVGPLLSYQS NGTATDEKAS EIGHKVRDIL HEGTGRDTVP VYVNYAFGDE GPKEWYGSEA
WRQSRLQELK EAYDPKGMFS FYAPIA
