ID E9CU07_COCPS Unreviewed; 485 AA.
AC E9CU07;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=CPSG_00942 {ECO:0000313|EMBL:EFW23043.1};
OS Coccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=443226 {ECO:0000313|Proteomes:UP000002497};
RN [1] {ECO:0000313|Proteomes:UP000002497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 757 / Silveira {ECO:0000313|Proteomes:UP000002497};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
RN [2] {ECO:0000313|Proteomes:UP000002497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 757 / Silveira {ECO:0000313|Proteomes:UP000002497};
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Orbach M., Henn M.R., Cole G.T., Galgiani J., Gardner M.J.,
RA Kirkland T.N., Taylor J.W., Young S.K., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Pearson M.,
RA Richards J., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., Walk T., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Coccidioides posadasii strain Silveira.";
RL Submitted (MAR-2010) 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; GL636486; EFW23043.1; -; Genomic_DNA.
DR STRING; 443226.E9CU07; -.
DR VEuPathDB; FungiDB:CPSG_00942; -.
DR VEuPathDB; FungiDB:D8B26_006577; -.
DR eggNOG; KOG1298; Eukaryota.
DR HOGENOM; CLU_026390_0_0_1; -.
DR OMA; AKRTFYW; -.
DR UniPathway; UPA00767; UER00752.
DR Proteomes; UP000002497; 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:UP000002497};
KW Transmembrane {ECO:0000256|RuleBase:RU367121};
KW Transmembrane helix {ECO:0000256|RuleBase:RU367121}.
FT TRANSMEM 432..449
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367121"
FT TRANSMEM 455..480
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367121"
SQ SEQUENCE 485 AA; 53137 MW; 4604F93738211379 CRC64;
MASQPLKNGL TNGSAHPKKQ YRDAAEERRC EQHEADIVII GAGIAGCSLA VALGNQGRSV
LLLEKSLKEP DRIVGELLQP GGVLALEKLG LRHCLEDIDA VKVLGYNVIY HGVPVRIDFP
MDSNEKLFEG RSFHHGRFIM KLREAAMSTP NVTVVETKAV SLVKSTHGEG VLGVECLTNG
KKDFFFAPLT VVADGYNSAF RKEFLPHAPR VKSKFWGLEL IDADLPMPCY GHVVLSDSPP
ILLYQIGTHE TRALVDIPEN LPSASVKNGG VKGHLRNTVL PSLPKSIQPS FAAAIDRGGL
RSMPNSFLPP ATNKTPGLMF LGDSLNMRHP LTGGGMTVAF NDIVALRVLL SPETVPNFSD
TNLVLKQLSK FHWKRKDSSS AINILAQSLY ALFAAGNSDL KVLQRGCFRY FQLGILDGPI
GLLSGLVHRP LVLFRHFYSV AFLSIWLLLR SAPPYMLPLT IFQCISVFIT ACRVILPFIF
AELKN
//
