ERG1_CANGA
ID ERG1_CANGA Reviewed; 489 AA.
AC O13306; Q6FVS7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Squalene monooxygenase;
DE EC=1.14.14.17 {ECO:0000250|UniProtKB:P32476};
DE AltName: Full=Squalene epoxidase;
DE Short=SE;
GN Name=ERG1; OrderedLocusNames=CAGL0D05940g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 139-344.
RC STRAIN=B57148;
RX PubMed=9333053; DOI=10.1128/aac.41.10.2229;
RA Marichal P., Vanden Bossche H., Odds F.C., Nobels G., Warnock D.W.,
RA Timmerman V., Van Broeckhoven C., Fay S., Mose-Larsen P.;
RT "Molecular biological characterization of an azole-resistant Candida
RT glabrata isolate.";
RL Antimicrob. Agents Chemother. 41:2229-2237(1997).
CC -!- FUNCTION: Catalyzes the stereospecific oxidation of squalene to (S)-
CC 2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in
CC steroid biosynthesis. {ECO:0000250|UniProtKB:P32476}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + reduced [NADPH--hemoprotein reductase] + squalene = (S)-
CC 2,3-epoxysqualene + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:25282, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15440, ChEBI:CHEBI:15441, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.14.17;
CC Evidence={ECO:0000250|UniProtKB:P32476};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q14534};
CC -!- PATHWAY: Terpene metabolism; lanosterol biosynthesis; lanosterol from
CC farnesyl diphosphate: step 2/3. {ECO:0000250|UniProtKB:P32476}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane
CC {ECO:0000250|UniProtKB:P32476}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P32476}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P32476}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P32476}.
CC -!- SIMILARITY: Belongs to the squalene monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; CR380950; CAG58578.1; -; Genomic_DNA.
DR EMBL; AF006033; AAB69189.1; -; Genomic_DNA.
DR RefSeq; XP_445667.1; XM_445667.1.
DR AlphaFoldDB; O13306; -.
DR SMR; O13306; -.
DR STRING; 5478.XP_445667.1; -.
DR EnsemblFungi; CAG58578; CAG58578; CAGL0D05940g.
DR GeneID; 2887028; -.
DR KEGG; cgr:CAGL0D05940g; -.
DR CGD; CAL0128393; ERG1.
DR VEuPathDB; FungiDB:CAGL0D05940g; -.
DR eggNOG; KOG1298; Eukaryota.
DR HOGENOM; CLU_026390_0_0_1; -.
DR InParanoid; O13306; -.
DR OMA; KSKFWGL; -.
DR UniPathway; UPA00767; UER00752.
DR Proteomes; UP000002428; Chromosome D.
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:0005811; C:lipid droplet; IEA:EnsemblFungi.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004506; F:squalene monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006696; P:ergosterol biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0008204; P:ergosterol metabolic process; IMP:CGD.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR013698; Squalene_epoxidase.
DR InterPro; IPR040125; Squalene_monox.
DR PANTHER; PTHR10835; PTHR10835; 1.
DR Pfam; PF08491; SE; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Microsome;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..489
FT /note="Squalene monooxygenase"
FT /id="PRO_0000209849"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 21..22
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 41..42
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 49
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 151
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 167
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 328
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 341
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT SITE 83
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT CONFLICT 140..141
FT /note="GL -> AF (in Ref. 2; AAB69189)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 489 AA; 54492 MW; 13465A35D983F83C CRC64;
MSLTNADETV TYDALIVGAG VIGPCVATAL ARKGKKVLIV EREWSQPDRI VGELMQPGGL
RALRSLGMIQ SINNIDAYPV TGYTVFYNGE HVDIPYPYKA DLKPVEKLPG LVRDGNDKVL
EDATVHKKDF EDDERERGVG LVHGRFLNNL RNICAAEPNV TRLQGNVVEI LKDKKNEVVG
AKVDVDSRGK VDFKAHLTFV CDGIFSRFRR ELHPDHVPTV NSSFVGMSLY HAHMPHDMHG
HVILGDKHMP ILVYQISPEE TRILCAYNAP KVPTDLKSWM TKDVQPYIPK TLRPSFDDAL
AQGKFKPMAN SWLPARQNDV TGLCVIGDAL NMRHPLTGGG MTVGLNDVVL LIKKIGDLDF
SDREKVLDEL LDYHFERKNY DAVVNVLSIS LYSLFAADSK NLKALQKGCF KYFQRGGDCV
NLPVAFLAGV LPKPLLLTRV FFAVAFYTIY LNMEERGFLG LPMALLEGIM ILITAIKVFT
PFLVRELIG
