ERG6B_GIBZE
ID ERG6B_GIBZE Reviewed; 380 AA.
AC A0A0E0SMA3;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Sterol 24-C-methyltransferase ERG6B {ECO:0000303|PubMed:22947191};
DE Short=SCMT {ECO:0000305};
DE Short=SMT {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q4W9V1};
DE AltName: Full=Delta(24)-sterol C-methyltransferase ERG6B {ECO:0000305};
DE AltName: Full=Ergosterol biosynthesis protein 6B {ECO:0000303|PubMed:22947191};
GN Name=ERG6B {ECO:0000303|PubMed:22947191};
GN ORFNames=FG05740, FGRAMPH1_01T18649;
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.
RX PubMed=22947191; DOI=10.1111/j.1364-3703.2012.00829.x;
RA Liu X., Jiang J., Yin Y., Ma Z.;
RT "Involvement of FgERG4 in ergosterol biosynthesis, vegetative
RT differentiation and virulence in Fusarium graminearum.";
RL Mol. Plant Pathol. 14:71-83(2013).
RN [5]
RP FUNCTION, 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 [6]
RP INDUCTION.
RX PubMed=30874562; DOI=10.1038/s41467-019-09145-6;
RA Liu Z., Jian Y., Chen Y., Kistler H.C., He P., Ma Z., Yin Y.;
RT "A phosphorylated transcription factor regulates sterol biosynthesis in
RT Fusarium graminearum.";
RL Nat. Commun. 10:1228-1228(2019).
CC -!- FUNCTION: Sterol 24-C-methyltransferase; part of the third module of
CC ergosterol biosynthesis pathway that includes the late steps of the
CC pathway (By similarity). ERG6A and ERG6B methylate lanosterol at C-24
CC to produce eburicol (By similarity). The third module or late pathway
CC involves the ergosterol synthesis itself through consecutive reactions
CC that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly,
CC the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl
CC pyrophosphate moieties to form squalene, which is the precursor of all
CC steroids. Squalene synthase is crucial for balancing the incorporation
CC of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene
CC synthesis. Secondly, squalene is converted into lanosterol by the
CC consecutive action of the squalene epoxidase ERG1 and the lanosterol
CC synthase ERG7. Then, the delta(24)-sterol C-methyltransferase ERG6
CC methylates lanosterol at C-24 to produce eburicol. Eburicol is the
CC substrate of the sterol 14-alpha demethylase encoded by CYP51A, CYP51B
CC and CYP51C, to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol.
CC CYP51B encodes the enzyme primarily responsible for sterol 14-alpha-
CC demethylation, and plays an essential role in ascospore formation.
CC CYP51A encodes an additional sterol 14-alpha-demethylase, induced on
CC ergosterol depletion and responsible for the intrinsic variation in
CC azole sensitivity. The third CYP51 isoform, CYP51C, does not encode a
CC sterol 14-alpha-demethylase, but is required for full virulence on host
CC wheat ears. The C-14 reductase ERG24 then reduces the C14=C15 double
CC bond which leads to 4,4-dimethylfecosterol. A sequence of further
CC demethylations at C-4, involving the C-4 demethylation complex
CC containing the C-4 methylsterol oxidases ERG25, the sterol-4-alpha-
CC carboxylate 3-dehydrogenase ERG26 and the 3-keto-steroid reductase
CC ERG27, leads to the production of fecosterol via 4-methylfecosterol.
CC ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to
CC the endoplasmic reticulum. The C-8 sterol isomerase ERG2 then catalyzes
CC the reaction which results in unsaturation at C-7 in the B ring of
CC sterols and thus converts fecosterol to episterol. The sterol-C5-
CC desaturases ERG3A and ERG3BB then catalyze the introduction of a C-5
CC double bond in the B ring to produce 5-dehydroepisterol. The C-22
CC sterol desaturases ERG5A and ERG5B further convert 5-dehydroepisterol
CC into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23)
CC double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-
CC tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to
CC produce ergosterol (Probable). {ECO:0000250|UniProtKB:Q4W9V1,
CC ECO:0000305|PubMed:23442154}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lanosterol + S-adenosyl-L-methionine = eburicol + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:52652, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16521, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:70315; Evidence={ECO:0000250|UniProtKB:Q4W9V1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52653;
CC Evidence={ECO:0000250|UniProtKB:Q4W9V1};
CC -!- PATHWAY: Steroid metabolism; ergosterol biosynthesis.
CC {ECO:0000305|PubMed:23442154}.
CC -!- INDUCTION: Expression is increased in the absence of the C-24(28)
CC sterol reductase ERG4 (PubMed:22947191). Expression is positively
CC regulated by the FgSR transcription factor that targets gene promoters
CC containing 2 conserved CGAA repeat sequences (PubMed:30874562).
CC {ECO:0000269|PubMed:22947191, ECO:0000269|PubMed:30874562}.
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 class I-like SAM-binding methyltransferase
CC superfamily. Erg6/SMT family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HG970334; CEF87566.1; -; Genomic_DNA.
DR STRING; 5518.FGSG_05740P0; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G18649; -.
DR eggNOG; KOG1269; Eukaryota.
DR UniPathway; UPA00768; -.
DR Proteomes; UP000070720; Chromosome 3.
DR GO; GO:0003838; F:sterol 24-C-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR030384; MeTrfase_SMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR013705; Sterol_MeTrfase_C.
DR Pfam; PF08241; Methyltransf_11; 1.
DR Pfam; PF08498; Sterol_MT_C; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51685; SAM_MT_ERG6_SMT; 1.
PE 2: Evidence at transcript level;
KW Lipid biosynthesis; Lipid metabolism; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transferase.
FT CHAIN 1..380
FT /note="Sterol 24-C-methyltransferase ERG6B"
FT /id="PRO_0000454368"
SQ SEQUENCE 380 AA; 42727 MW; 0595F7289DBA5892 CRC64;
MPTTELISYD EAQNSAFDNV LHGKSKESRG GMRAMMNKDN KAHAAAVDEY FQFFDNKKAE
DEVEAVRQER TDNYASLTRQ YYNLATDLYE YGWSQSFHFC RFAYGESFDR AIARHEHYLA
HNIGIKPGMK VLDVGCGVGG PAREIVKFTG AHVTGLNINE YQVGRAGIYA EKEGLSDKLK
FVQGDFMKMP FPDNSFDAVY AIEATVHAPS LEGVYSEIRR VLKPGGIFGV YEWLMTDIYD
NDDLEQRRIR LDIELGDGIA QMFKIDHGLS AIKAAGFELL HHEDLAATDD GTAPWYWPLD
SDMRYAQNLS DLLTVFRMNK WGRLVMHNLI GVLEACSIAP KGTRKTADGL AKGADALVEG
GKRKLFTPMY LMVGKKPEKI
