ZEB1_GIBZE
ID ZEB1_GIBZE Reviewed; 565 AA.
AC A0A0E0RTV6; I1RFC5; Q2VLJ1;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 2.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=FAD-linked oxidoreductase ZEB1 {ECO:0000303|PubMed:16262793};
DE EC=1.-.-.- {ECO:0000305|PubMed:16262793};
DE AltName: Full=Zearalenone biosynthesis protein 1 {ECO:0000303|PubMed:16262793};
DE Flags: Precursor;
GN Name=ZEB1 {ECO:0000303|PubMed:16262793};
GN ORFNames=FGRAMPH1_01T05753, FGSG_02397;
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 [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE,
RP INDUCTION, AND PATHWAY.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=16262793; DOI=10.1111/j.1365-2958.2005.04884.x;
RA Kim Y.T., Lee Y.R., Jin J., Han K.H., Kim H., Kim J.C., Lee T., Yun S.H.,
RA Lee Y.W.;
RT "Two different polyketide synthase genes are required for synthesis of
RT zearalenone in Gibberella zeae.";
RL Mol. Microbiol. 58:1102-1113(2005).
RN [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION.
RX PubMed=16517624; DOI=10.1128/aem.72.3.1793-1799.2006;
RA Gaffoor I., Trail F.;
RT "Characterization of two polyketide synthase genes involved in zearalenone
RT biosynthesis in Gibberella zeae.";
RL Appl. Environ. Microbiol. 72:1793-1799(2006).
RN [6]
RP FUNCTION.
RX PubMed=16751498; DOI=10.1128/aem.00963-05;
RA Lysoee E., Klemsdal S.S., Bone K.R., Frandsen R.J., Johansen T., Thrane U.,
RA Giese H.;
RT "The PKS4 gene of Fusarium graminearum is essential for zearalenone
RT production.";
RL Appl. Environ. Microbiol. 72:3924-3932(2006).
RN [7]
RP FUNCTION.
RX PubMed=18427109; DOI=10.1073/pnas.0800657105;
RA Zhou H., Zhan J., Watanabe K., Xie X., Tang Y.;
RT "A polyketide macrolactone synthase from the filamentous fungus Gibberella
RT zeae.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:6249-6254(2008).
CC -!- FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that
CC mediates the biosynthesis of zearalenone (ZEA), a nonsteroid estrogen
CC that is a contaminant of cereal grains and causes estrogenic disorders
CC in humans and animals (PubMed:16262793, PubMed:16517624,
CC PubMed:18427109). The ZEA backbone is synthesized from a single acetyl-
CC CoA molecule and eight malonyl-CoA molecules (PubMed:16262793,
CC PubMed:16517624, PubMed:18427109). The reducing polyketide synthase
CC ZEA2 is proposed to synthesize a reduced hexaketide intermediate by
CC using different combinations of its reductive domains during each round
CC of condensation (PubMed:16262793, PubMed:16517624, PubMed:16751498,
CC PubMed:18427109). The hexaketide thioester is then transacylated to the
CC non-reducing polyketide synthase ZEA1 and is further condensed with
CC three malonyl-CoAs without reductive tailoring to yield a mixed
CC reduced/unreduced nonaketide (PubMed:16262793, PubMed:16517624,
CC PubMed:18427109). ZEA1 must be able to interact with ZEA2 to facilitate
CC starter-unit acyltransfer and initiate polyketide biosynthesis
CC (PubMed:18427109). ZEA1 also mediates the required C2-C7 cyclization to
CC form the resorcylate core and catalyzes the formation of the
CC macrolactone (PubMed:18427109). ZEB1 is then responsible for the
CC chemical conversion of beta-zearalenonol (beta-ZOL) to ZEA in the
CC biosynthetic pathway (PubMed:16262793). {ECO:0000269|PubMed:16262793,
CC ECO:0000269|PubMed:16751498, ECO:0000269|PubMed:17823352,
CC ECO:0000269|PubMed:18427109}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:16262793}.
CC -!- INDUCTION: Expression is positively regulated by the zearalenone
CC biosynthesis specific transcription factor ZEB2 (PubMed:16262793).
CC Conditions for carbon-, nitrogen-, or phosphorus-starvations lead to
CC very low expression (PubMed:16262793). Increase in pH results in
CC gradual reduction of the gene expression (PubMed:16262793).
CC {ECO:0000269|PubMed:16262793}.
CC -!- DISRUPTION PHENOTYPE: Results in the loss of zearalenone production but
CC still produces beta-zearalenonol (PubMed:16262793).
CC {ECO:0000269|PubMed:16262793}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CEF74681.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ESU07827.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ019316; ABB90284.1; -; Genomic_DNA.
DR EMBL; DS231663; ESU07827.1; ALT_SEQ; Genomic_DNA.
DR EMBL; HG970332; CEF74681.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_011318312.1; XM_011320010.1.
DR AlphaFoldDB; A0A0E0RTV6; -.
DR SMR; A0A0E0RTV6; -.
DR EnsemblFungi; ESU07827; ESU07827; FGSG_02397.
DR GeneID; 23549775; -.
DR KEGG; fgr:FGSG_02397; -.
DR eggNOG; ENOG502R8I5; Eukaryota.
DR PHI-base; PHI:716; -.
DR Proteomes; UP000070720; Chromosome 1.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0106150; P:zearalenone biosynthetic process; IMP:GO_Central.
DR Gene3D; 3.30.465.10; -; 2.
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 2: Evidence at transcript level;
KW FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..565
FT /note="FAD-linked oxidoreductase ZEB1"
FT /id="PRO_5008207791"
FT DOMAIN 115..293
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 565 AA; 61683 MW; 9298D1692C579E43 CRC64;
MKLSPSKYLP VLLGTLSLTI ANPSADCKCF PGDDCWPSAA EWKALNTSVS GNLIKTVPLG
APCHDPMFKG DVCQSLRQQW QNATIHFASS SSVMAPFFAN QSCDPFQPRI RPCELGNYVS
YAIAAETTSD VQNAIAFARA NHIRLVIRNT GHDYLGRSTG AGALGVWTHH LKNIEFVDWD
DDTYTGNAVK LGAGVQGFEV LEAARSRGLV VVGGECPTVG IAGGYSQGGG HSALSTSFGL
SVDNVLSWEV ITAKGELLTV NKDENPDLFW ALRGGGGGTF GVVISMTVKA HPGTITSGAS
LSFSTDTNSE EAFWAGIQVF QDTLEDMVDA GTMVIHIITN TSFLIAPLTA YNKTEAQVKV
IMKPFISSLT SKHVDFDVTY KESKTYYDHY NEFLGPLPYG KIRVGFEQYG GRLIPRSVVP
NFTETLRQVT NMGVTWVGVA TDVGPFGTRA TTSVHPAWRS TLVHALLSTP WDFTKPWHDM
IKLQDLMTNV IMPKVEAVTP GSGAYVNEAD FRQPNYQDVF WGDNYKDLLE VKEKWDPEHF
FFVPKGVGSE IWSIAEDGRM CKSAL
