ID A0A175YF34_DAUCS Unreviewed; 484 AA.
AC A0A175YF34;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=DCAR_029850 {ECO:0000313|EMBL:KZM82266.1};
OS Daucus carota subsp. sativus (Carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=79200 {ECO:0000313|EMBL:KZM82266.1};
RN [1] {ECO:0000313|EMBL:KZM82266.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaf {ECO:0000313|EMBL:KZM82266.1};
RX PubMed=27158781; DOI=10.1038/ng.3565;
RA Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT "A high-quality carrot genome assembly provides new insights into
RT carotenoid accumulation and asterid genome evolution.";
RL Nat. Genet. 48:657-666(2016).
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 -!- 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZM82266.1}.
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DR EMBL; LNRQ01000009; KZM82266.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A175YF34; -.
DR STRING; 79200.A0A175YF34; -.
DR EnsemblPlants; KZM82266; KZM82266; DCAR_029850.
DR Gramene; KZM82266; KZM82266; DCAR_029850.
DR OMA; KNCEAPY; -.
DR UniPathway; UPA00767; UER00752.
DR Proteomes; UP000077755; Chromosome 9.
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; 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; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR013698; Squalene_epoxidase.
DR InterPro; IPR040125; Squalene_monox.
DR PANTHER; PTHR10835; SQUALENE MONOOXYGENASE; 1.
DR PANTHER; PTHR10835:SF19; SQUALENE MONOOXYGENASE; 1.
DR Pfam; PF13450; NAD_binding_8; 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 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:UP000077755};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}.
FT DOMAIN 171..440
FT /note="Squalene epoxidase"
FT /evidence="ECO:0000259|Pfam:PF08491"
SQ SEQUENCE 484 AA; 52843 MW; A1BD5657D5BB4169 CRC64;
MESIKPIENG ECQEEIARNP DIIIVGAGVA GSALACTLGK DGRRVLVIER DLAEPDRIVG
ELLQPGGYLK LIELGLEDCV NEIDAQEVFG YALFKDGKST KLSYPLKDFN PDVTGKSFHN
GRFIQRMREK AKTISNVRLE QGTVTSLVER KGTVKGVQYK TRGGQEMTAY APLTIVCDGC
FSNLRRSLCN PRVEIPSCFV ALILKDCQLP YPDHGHVLLA NPSPILLYRI SSTEIRCLVD
VPGKRIPSIV NGDMANYLKT LVAPQIPPEL YDAFITAVNE GNMKTMANRS MPASPYPTPG
ALLIGDSFNM RHPLTGGGMT VALSDIVVLR DLLRPLGNLN DASALCRYLE SFYTLRKPLA
STINTLAGAL YKVFCASPDL ARSEMRSACF DYLSLGGVCS SGPVALLSGL NPRPLSLVLH
FFSVAIYGVG RLLLPFPSLQ RLWLGIRLIM DATSIILPII RAEGVRQMFL PAVFPAYFSS
PLTC
//
