ERG6_NEUCR
ID ERG6_NEUCR Reviewed; 379 AA.
AC Q9P3R1; Q1K936;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Sterol 24-C-methyltransferase erg-4 {ECO:0000303|PubMed:154056};
DE EC=2.1.1.- {ECO:0000305|PubMed:154056};
DE AltName: Full=Delta(24)-sterol C-methyltransferase;
DE AltName: Full=S-adenosyl-L-methionine:sterol C-24 methyl transferasee;
DE Short=SAM:SMT;
GN Name=erg-4 {ECO:0000303|PubMed:154056}; ORFNames=B24P7.240, NCU03006;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [3]
RP FUNCTION.
RX PubMed=154056; DOI=10.1007/bf00332531;
RA Grindle M., Farrow R.;
RT "Sterol content and enzyme defects of nystatin-resistant mutants of
RT Neurospora crassa.";
RL Mol. Gen. Genet. 165:305-308(1978).
RN [4]
RP FUNCTION, AND PATHWAY.
RX PubMed=1838342; DOI=10.1042/bst0190799;
RA Connerton I.F., Deane S.M., Butters J.A., Loeffler R.S., Hollomon D.W.;
RT "RIP (repeat induced point mutation) as a tool in the analysis of P-450 and
RT sterol biosynthesis in Neurospora crassa.";
RL Biochem. Soc. Trans. 19:799-802(1991).
CC -!- FUNCTION: Catalyzes the methyl transfer from S-adenosyl-methionine to
CC the C-24 of lanosterol to form eburicol. {ECO:0000269|PubMed:154056,
CC ECO:0000305|PubMed:1838342}.
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:0000305|PubMed:154056};
CC -!- PATHWAY: Steroid metabolism; ergosterol biosynthesis.
CC {ECO:0000305|PubMed:1838342}.
CC -!- MISCELLANEOUS: In Neurospora, 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 Neurospora,
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:0000305|PubMed:1838342}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Erg6/SMT family. {ECO:0000255|PROSITE-ProRule:PRU01022}.
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DR EMBL; AL389890; CAB97289.1; -; Genomic_DNA.
DR EMBL; CM002236; EAA36156.1; -; Genomic_DNA.
DR PIR; T50969; T50969.
DR RefSeq; XP_965392.1; XM_960299.3.
DR AlphaFoldDB; Q9P3R1; -.
DR SMR; Q9P3R1; -.
DR STRING; 5141.EFNCRP00000002261; -.
DR PRIDE; Q9P3R1; -.
DR EnsemblFungi; EAA36156; EAA36156; NCU03006.
DR GeneID; 3881542; -.
DR KEGG; ncr:NCU03006; -.
DR VEuPathDB; FungiDB:NCU03006; -.
DR HOGENOM; CLU_039068_5_3_1; -.
DR InParanoid; Q9P3R1; -.
DR OMA; ISNMCKV; -.
DR UniPathway; UPA00768; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005811; C:lipid droplet; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0003838; F:sterol 24-C-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0006696; P:ergosterol biosynthetic process; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
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 3: Inferred from homology;
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..379
FT /note="Sterol 24-C-methyltransferase erg-4"
FT /id="PRO_0000124795"
SQ SEQUENCE 379 AA; 42457 MW; AE572C3EE6AE27E3 CRC64;
MPSTIALEKE DHQRDAEFKK VMHGDSAKAA GGVAALLKKN TEAQQIAVDE YFKHFDNKTA
EAETQADREA RTKEYATLTR HYYNLATDIY EYGWGQCFHF CRYSPGESFY QAIARHEHYL
AAQIGIKKDM KVLDVGCGVG GPAREIAKFT DAHITGLNNN DYQIDRATHY AVRDGLSGQL
KFVKGDFMQM SFPDNSFDAV YAIEATVHAP KLEGVYGEIY RVLKPGGTFG VYEWLMTDNY
DNDNVEHRDI RLAIEVGNGI SNMVTISEGL AAMKNVGFEL VHHEDLADRN DPMPWYWPIA
GELRYMQSYL DFFTVVRMTH TARRILHGFA GILETVGLAP KGTKKTADAL ARGADGLVAG
AKKKLFTPMY LMVGKKPLN
