ID A0A2J6STW0_9HELO Unreviewed; 497 AA.
AC A0A2J6STW0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Squalene monooxygenase {ECO:0000256|ARBA:ARBA00012312, ECO:0000256|RuleBase:RU367121};
DE EC=1.14.14.17 {ECO:0000256|ARBA:ARBA00012312, ECO:0000256|RuleBase:RU367121};
GN ORFNames=K444DRAFT_618670 {ECO:0000313|EMBL:PMD54214.1};
OS Hyaloscypha bicolor E.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD54214.1, ECO:0000313|Proteomes:UP000235371};
RN [1] {ECO:0000313|EMBL:PMD54214.1, ECO:0000313|Proteomes:UP000235371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E {ECO:0000313|EMBL:PMD54214.1,
RC ECO:0000313|Proteomes:UP000235371};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the stereospecific oxidation of squalene to
CC (S)-2,3-epoxysqualene, and is considered to be a rate-limiting enzyme
CC in steroid biosynthesis. {ECO:0000256|RuleBase:RU367121}.
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:0000256|RuleBase:RU367121};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU367121};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU367121}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU367121}. Microsome membrane
CC {ECO:0000256|ARBA:ARBA00004154}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004154}.
CC -!- SIMILARITY: Belongs to the squalene monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00008802, ECO:0000256|RuleBase:RU367121}.
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DR EMBL; KZ613866; PMD54214.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6STW0; -.
DR STRING; 1095630.A0A2J6STW0; -.
DR InParanoid; A0A2J6STW0; -.
DR OrthoDB; 148348at2759; -.
DR UniPathway; UPA00767; UER00752.
DR Proteomes; UP000235371; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004506; F:squalene monooxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR013698; Squalene_epoxidase.
DR InterPro; IPR040125; Squalene_monox.
DR PANTHER; PTHR10835; SQUALENE MONOOXYGENASE; 1.
DR PANTHER; PTHR10835:SF0; SQUALENE MONOOXYGENASE; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF08491; SE; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU367121};
KW FAD {ECO:0000256|RuleBase:RU367121};
KW Flavoprotein {ECO:0000256|RuleBase:RU367121};
KW Membrane {ECO:0000256|RuleBase:RU367121};
KW Microsome {ECO:0000256|ARBA:ARBA00022848};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU367121};
KW Reference proteome {ECO:0000313|Proteomes:UP000235371};
KW Transmembrane {ECO:0000256|RuleBase:RU367121};
KW Transmembrane helix {ECO:0000256|RuleBase:RU367121}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367121"
FT TRANSMEM 383..400
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367121"
FT TRANSMEM 438..456
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367121"
FT TRANSMEM 476..492
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367121"
FT DOMAIN 21..50
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 191..458
FT /note="Squalene epoxidase"
FT /evidence="ECO:0000259|Pfam:PF08491"
SQ SEQUENCE 497 AA; 54508 MW; 7A1711B0AF6CC0D9 CRC64;
MSDSVLQASN EQRRRLNHEA DVVVVGAGIF GCAAAFALAK QGRSVLLLER WLKEPDRIVG
ELLQPGGVSA LEKLGLAHCL EGIDSITVKG YEVIYYGQGV EIPYPMNAGA ANGDTQEYTN
EKGGRPEGRA FHHGRFITQL RKACASQPNI TIVETEVTDT VTSTHNPQVL GVVSRTLNPA
TGEKEDDFYF GQLTIVADGY ASKFRKQYIG KSPIVKSKFY ALELIDCPLP SPNHGTVVLG
DAAPVLLYQI GTHETRALID VPEHCPTASV EVGGVRGHMR NVILPSLPKQ VQPCFEKALE
DGKIPRSMPN SFLPPTTQLE KGIVILGDAM NMRHPLTGGG MTVAFNDVVL LSRLLAPERI
PNLGDTAAIQ KAMKEFHWKR KRLSSIINIL AMALYSLFAA NDRQLKSLQK GCFEYFQKGG
NCIDGPVGLL AGIIRQPFIL FYHFFAVAFL SIWIVISDTV GGLLGLWKFP VAIEQSLLVF
WKACVVIFPF IFSEMRS
//
