(data stored in SCRATCH zone)

SWISSPROT: ERG6_ASPFU

ID   ERG6_ASPFU              Reviewed;         377 AA.
AC   Q4W9V1;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 83.
DE   RecName: Full=Sterol 24-C-methyltransferase {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000305|PubMed:16110826};
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=erg6 {ECO:0000303|PubMed:16110826}; ORFNames=AFUA_4G03630;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
RN   [2]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=16110826; DOI=10.1080/13693780400029114;
RA   Ferreira M.E., Colombo A.L., Paulsen I., Ren Q., Wortman J., Huang J.,
RA   Goldman M.H., Goldman G.H.;
RT   "The ergosterol biosynthesis pathway, transporter genes, and azole
RT   resistance in Aspergillus fumigatus.";
RL   Med. Mycol. 43:S313-S319(2005).
RN   [3]
RP   PATHWAY.
RX   PubMed=18191972; DOI=10.1016/j.steroids.2007.11.005;
RA   Alcazar-Fuoli L., Mellado E., Garcia-Effron G., Lopez J.F., Grimalt J.O.,
RA   Cuenca-Estrella J.M., Rodriguez-Tudela J.L.;
RT   "Ergosterol biosynthesis pathway in Aspergillus fumigatus.";
RL   Steroids 73:339-347(2008).
CC   -!- FUNCTION: Catalyzes the methyl transfer from S-adenosyl-methionine to
CC       the C-24 of lanosterol to form eburicol. {ECO:0000305|PubMed:16110826}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=lanosterol + S-adenosyl-L-methionine = 24-methylene-24-
CC         dihydrolanosterol + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:52652, ChEBI:CHEBI:15378, ChEBI:CHEBI:16521,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:70315;
CC   -!- PATHWAY: Steroid metabolism; ergosterol biosynthesis.
CC       {ECO:0000305|PubMed:16110826, ECO:0000305|PubMed:18191972}.
CC   -!- MISCELLANEOUS: In Aspergillus, 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 Aspergillus,
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:18191972}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Erg6/SMT family. {ECO:0000305}.
DR   EMBL; AAHF01000016; EAL84512.1; -; Genomic_DNA.
DR   RefSeq; XP_746550.1; XM_741457.1.
DR   SMR; Q4W9V1; -.
DR   STRING; 746128.CADAFUBP00009660; -.
DR   PRIDE; Q4W9V1; -.
DR   EnsemblFungi; EAL84512; EAL84512; AFUA_4G03630.
DR   GeneID; 3504016; -.
DR   KEGG; afm:AFUA_4G03630; -.
DR   EuPathDB; FungiDB:Afu4g03630; -.
DR   HOGENOM; HOG000171097; -.
DR   InParanoid; Q4W9V1; -.
DR   KO; K00559; -.
DR   OMA; GISNMCK; -.
DR   OrthoDB; 661953at2759; -.
DR   UniPathway; UPA00768; -.
DR   Proteomes; UP000002530; Chromosome 4.
DR   Proteomes; UP000002530; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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   InterPro; IPR013216; Methyltransf_11.
DR   InterPro; IPR030384; MeTrfase_SMT.
DR   InterPro; IPR029063; SAM-dependent_MTases.
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;
DR   PRODOM; Q4W9V1.
DR   SWISS-2DPAGE; Q4W9V1.
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..377
FT                   /note="Sterol 24-C-methyltransferase"
FT                   /id="PRO_0000442289"
SQ   SEQUENCE   377 AA;  42571 MW;  74396ADEEA766FA8 CRC64;
     MAPVALEQEN HLRDAEFNRA MHGKSAQFRG GFAALRGKDS AAQKAAVDEY FKHWDNKPAE
     DETEETRAAR RAEYATLTRH YYNLATDLYE YGWGTSFHFC RFAQGEPFYQ AIARHEHYLA
     HQMGIKEGMK VLDVGCGVGG PAREIVKFTD ANVVGLNNND YQIERATRYA EREGLSHKLS
     FVKGDFMQMK FPDNSFDAVY AIEATVHAPD LEGVYKEIFR VLKPGGVFGV YEWLMTDAYD
     NDNPEHRRIR LGIELGDGIS NMVKVSEGLT AFKNAGFELL HNEDLADRPD AIPWYYPLAG
     SFKHMTSPWD FFTIARMTWW GRGIAHRFCG AMETIGLFPK GTQKTADSLA IAGDCLVAGG
     EKKLFTPMYL MVGRKPE
//

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