ERG3B_GIBZE
ID ERG3B_GIBZE Reviewed; 323 AA.
AC A0A0E0SNE8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Delta(7)-sterol 5(6)-desaturase ERG3B {ECO:0000305};
DE EC=1.14.19.20 {ECO:0000305|PubMed:23442154};
DE AltName: Full=C-5 sterol desaturase ERG3B {ECO:0000303|PubMed:24785759};
DE AltName: Full=Ergosterol Delta(5,6) desaturase ERG3B {ECO:0000303|PubMed:24785759};
DE AltName: Full=Ergosterol biosynthetic protein 3B {ECO:0000303|PubMed:24785759};
GN Name=ERG3B {ECO:0000303|PubMed:24785759};
GN ORFNames=FG04994, FGRAMPH1_01T16829;
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 INDUCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=23442154; DOI=10.1111/nph.12193;
RA Fan J., Urban M., Parker J.E., Brewer H.C., Kelly S.L.,
RA Hammond-Kosack K.E., Fraaije B.A., Liu X., Cools H.J.;
RT "Characterization of the sterol 14alpha-demethylases of Fusarium
RT graminearum identifies a novel genus-specific CYP51 function.";
RL New Phytol. 198:821-835(2013).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24785759; DOI=10.1016/j.fgb.2014.04.010;
RA Yun Y., Yin D., Dawood D.H., Liu X., Chen Y., Ma Z.;
RT "Functional characterization of FgERG3 and FgERG5 associated with
RT ergosterol biosynthesis, vegetative differentiation and virulence of
RT Fusarium graminearum.";
RL Fungal Genet. Biol. 68:60-70(2014).
CC -!- FUNCTION: C-5 sterol desaturase; part of the third module of ergosterol
CC biosynthesis pathway that includes the late steps of the pathway
CC (PubMed:24785759). ERG3A and ERG3BB catalyze the introduction of a C-5
CC double bond in the B ring to produce 5-dehydroepisterol (By
CC similarity). The third module or late pathway involves the ergosterol
CC synthesis itself through consecutive reactions that mainly occur in the
CC endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase
CC ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to
CC form squalene, which is the precursor of all steroids. Squalene
CC synthase is crucial for balancing the incorporation of farnesyl
CC diphosphate (FPP) into sterol and nonsterol isoprene synthesis.
CC Secondly, squalene is converted into lanosterol by the consecutive
CC action of the squalene epoxidase ERG1 and the lanosterol synthase ERG7.
CC Then, the delta(24)-sterol C-methyltransferase ERG6 methylates
CC lanosterol at C-24 to produce eburicol. Eburicol is the substrate of
CC the sterol 14-alpha demethylase encoded by CYP51A, CYP51B and CYP51C,
CC to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol. CYP51B encodes
CC the enzyme primarily responsible for sterol 14-alpha-demethylation, and
CC plays an essential role in ascospore formation. CYP51A encodes an
CC additional sterol 14-alpha-demethylase, induced on ergosterol depletion
CC and responsible for the intrinsic variation in azole sensitivity. The
CC third CYP51 isoform, CYP51C, does not encode a sterol 14-alpha-
CC demethylase, but is required for full virulence on host wheat ears. The
CC C-14 reductase ERG24 then reduces the C14=C15 double bond which leads
CC to 4,4-dimethylfecosterol. A sequence of further demethylations at C-4,
CC involving the C-4 demethylation complex containing the C-4 methylsterol
CC oxidases ERG25, the sterol-4-alpha-carboxylate 3-dehydrogenase ERG26
CC and the 3-keto-steroid reductase ERG27, leads to the production of
CC fecosterol via 4-methylfecosterol. ERG28 has a role as a scaffold to
CC help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum. The C-
CC 8 sterol isomerase ERG2 then catalyzes the reaction which results in
CC unsaturation at C-7 in the B ring of sterols and thus converts
CC fecosterol to episterol. The sterol-C5-desaturases ERG3A and ERG3BB
CC then catalyze the introduction of a C-5 double bond in the B ring to
CC produce 5-dehydroepisterol. The C-22 sterol desaturases ERG5A and ERG5B
CC further convert 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-
CC 3beta-ol by forming the C-22(23) double bond in the sterol side chain.
CC Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-
CC 24(28) sterol reductase ERG4 to produce ergosterol (Probable).
CC {ECO:0000250|UniProtKB:Q4WIX5, ECO:0000269|PubMed:24785759,
CC ECO:0000305|PubMed:23442154}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=episterol + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = 5-
CC dehydroepisterol + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:46560, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:23929, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:52972; EC=1.14.19.20;
CC Evidence={ECO:0000305|PubMed:23442154};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46561;
CC Evidence={ECO:0000305|PubMed:23442154};
CC -!- PATHWAY: Steroid metabolism; ergosterol biosynthesis.
CC {ECO:0000305|PubMed:23442154}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding. {ECO:0000250|UniProtKB:P53045}.
CC -!- DISRUPTION PHENOTYPE: Leads to a severe decrease in ergosterol
CC production and virulence when ERG3A is also deleted (PubMed:23442154).
CC Results in increased production of deoxynivalenol (DON)
CC (PubMed:24785759). {ECO:0000269|PubMed:23442154,
CC ECO:0000269|PubMed:24785759}.
CC -!- MISCELLANEOUS: In Fusarium, the biosynthesis pathway of the sterol
CC precursors leading to the prevalent sterol ergosterol differs from
CC yeast. The ringsystem of lanosterol in S.cerevisiae is firstly
CC demethylised in three enzymatic steps leading to the intermediate
CC zymosterol and secondly a methyl group is added to zymosterol by the
CC sterol 24-C-methyltransferase to form fecosterol. In Fusarium,
CC lanosterol is firstly transmethylated by the sterol 24-C-
CC methyltransferase leading to the intermediate eburicol and secondly
CC demethylated in three steps to form fecosterol.
CC {ECO:0000269|PubMed:23442154}.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
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DR EMBL; HG970334; CEF87961.1; -; Genomic_DNA.
DR STRING; 5518.FGSG_04994P0; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G16829; -.
DR eggNOG; KOG0872; Eukaryota.
DR UniPathway; UPA00768; -.
DR Proteomes; UP000070720; Chromosome 3.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0044255; P:cellular lipid metabolic process; IEA:UniProt.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
DR Pfam; PF04116; FA_hydroxylase; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Oxidoreductase; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..323
FT /note="Delta(7)-sterol 5(6)-desaturase ERG3B"
FT /id="PRO_0000454362"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 157..285
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT MOTIF 171..175
FT /note="Histidine box-1"
FT /evidence="ECO:0000250|UniProtKB:P53045"
FT MOTIF 184..188
FT /note="Histidine box-2"
FT /evidence="ECO:0000250|UniProtKB:P53045"
FT MOTIF 262..266
FT /note="Histidine box-3"
FT /evidence="ECO:0000250|UniProtKB:P53045"
SQ SEQUENCE 323 AA; 37742 MW; A2FC2ECF5C5FD27A CRC64;
MDAILEILDP YVFDYGYAYL FPQQTTQPSY GNSTGFAPSS ASKNFDDEYS LNFGSSLPRD
DIYRQSASIL MIAGFGAAFI YVISAALSYY FVFDRRLEHH PRFLKNQIKQ EIQSSFFAIP
IIDLLTLPFF LGEVRGHSLL YTNIDEYGWS WLAISTILYM VFNDLGIYWI HRLEHHPSIY
KYVHKPHHKW IVPTPWAAIA FHPVDGYVQS VPYHVFVYLC PMQKHLYMFL FVCVQIWTIL
IHDGDMITGH WLERFINSPA HHTLHHMYFT CNYGQYFTWA DNYWGSHRAP MPELDPIHEA
IRVMQEKGLA DKDGNPIEKS KSE
