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Database: UniProt
Entry: B9S7X0_RICCO
LinkDB: B9S7X0_RICCO
Original site: B9S7X0_RICCO 
ID   B9S7X0_RICCO            Unreviewed;       295 AA.
AC   B9S7X0;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 54.
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=RCOM_1382340 {ECO:0000313|EMBL:EEF40286.1};
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN   [1] {ECO:0000313|Proteomes:UP000008311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX   PubMed=20729833; DOI=10.1038/nbt.1674;
RA   Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA   Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA   Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA   Rabinowicz P.D.;
RT   "Draft genome sequence of the oilseed species Ricinus communis.";
RL   Nat. Biotechnol. 28:951-956(2010).
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|ARBA:ARBA00002173,
CC       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|ARBA:ARBA00000331,
CC         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   -!- PATHWAY: Terpene metabolism; lanosterol biosynthesis; lanosterol from
CC       farnesyl diphosphate: step 2/3. {ECO:0000256|ARBA:ARBA00005018}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU367121}; Multi-
CC       pass membrane protein {ECO:0000256|RuleBase:RU367121}.
CC   -!- SIMILARITY: Belongs to the squalene monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00008802, ECO:0000256|RuleBase:RU367121}.
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DR   EMBL; EQ973887; EEF40286.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9S7X0; -.
DR   STRING; 3988.B9S7X0; -.
DR   eggNOG; KOG1298; Eukaryota.
DR   InParanoid; B9S7X0; -.
DR   UniPathway; UPA00767; UER00752.
DR   Proteomes; UP000008311; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004506; F:squalene monooxygenase activity; IBA:GO_Central.
DR   GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
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:SF27; SQUALENE MONOOXYGENASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF08491; SE; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|RuleBase:RU367121};
KW   Flavoprotein {ECO:0000256|RuleBase:RU367121};
KW   Membrane {ECO:0000256|ARBA:ARBA00022692};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU367121};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692}.
FT   DOMAIN          41..71
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          165..291
FT                   /note="Squalene epoxidase"
FT                   /evidence="ECO:0000259|Pfam:PF08491"
SQ   SEQUENCE   295 AA;  31655 MW;  008FC830F92260D2 CRC64;
     MLCSLKRKKN ITRASLNNCT DETLKSSSKE ICQPEIAASP DIIIVGAGVA GAALAYALGK
     DGRQVHVIER DLNEPDRIVG ELLQPGSYLK LIELGLEDCV EKIDAQQVFG YAIFKDGKES
     NVSGRSFHNG RFIQRMKEKA ASLPNLILQQ GTVTSLVEKK GTVKGAEIPS CFVALVLENC
     DLPYASHGHV IPADPSPILF YPISSTEVRC LVDIPGQNVP SISNGELAQY LKGTVAKQIP
     SELHDAFISA IGKGNIRTMP NRSMPASPHP TPGALLLGDA FNTRHPLTGG MIGTF
//
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