ID A0A061DWU9_THECC Unreviewed; 985 AA.
AC A0A061DWU9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=squalene monooxygenase {ECO:0000256|ARBA:ARBA00012312};
DE EC=1.14.14.17 {ECO:0000256|ARBA:ARBA00012312};
GN ORFNames=TCM_006348 {ECO:0000313|EMBL:EOX97274.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOX97274.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOX97274.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Terpene metabolism; lanosterol biosynthesis; lanosterol from
CC farnesyl diphosphate: step 2/3. {ECO:0000256|ARBA:ARBA00005018}.
CC -!- SIMILARITY: Belongs to the squalene monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00008802}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001880; EOX97274.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061DWU9; -.
DR STRING; 3641.A0A061DWU9; -.
DR EnsemblPlants; EOX97274; EOX97274; TCM_006348.
DR Gramene; EOX97274; EOX97274; TCM_006348.
DR eggNOG; KOG1298; Eukaryota.
DR HOGENOM; CLU_302765_0_0_1; -.
DR InParanoid; A0A061DWU9; -.
DR UniPathway; UPA00767; UER00752.
DR Proteomes; UP000026915; Chromosome 2.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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; 2.
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:SF8; SQUALENE MONOOXYGENASE; 1.
DR Pfam; PF13450; NAD_binding_8; 2.
DR Pfam; PF08491; SE; 2.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Monooxygenase {ECO:0000313|EMBL:EOX97274.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 207..480
FT /note="Squalene epoxidase"
FT /evidence="ECO:0000259|Pfam:PF08491"
FT DOMAIN 672..945
FT /note="Squalene epoxidase"
FT /evidence="ECO:0000259|Pfam:PF08491"
SQ SEQUENCE 985 AA; 106761 MW; 2CE96E10B10D77AA CRC64;
MAYQYIVGGV IASLLGFVFW YNSLVRELKK TRTSSMEFPV ENRVKKTGNG EVAGAIDVII
VGAGVAGAAL AYTLGKDGRR VHVIERELNE PDRIAGEGLL PGGYVKLTEL GLEDCVAGID
AQRILGYDLY KDGKSTKISF PLEKFQSHVA GRTFHNGRFV QKLREKAASL PNVNLEQGTV
TSLLEENGTI LGVHYKNKSG QELTASAPLT IVCDGGFSNL RRSLCYRKVD IPSYFVGLVL
ENCKLPHANY GAIILEDPSP ILFYPISSTE IRCLVDVPSQ KLPSVSGGEM AHFLKTVIAP
KIPPALYIAF ISAVEKQNNI RTMANRTMPA APLPTPGALL MGDAFNMRHP ITGGGMTVAL
SDVVVIRDLL RPLHNLGNAS AVCRYLESFY TLRKPMASTI NTLADTLHKV FSASSDPAME
QMQQACFGYL SLGGVFSNGL SSLLSGLYPR PSSLAFHFFA MAVYGVGRLL LPFPSPNRIW
TGAKLIWVAS VRRLKKTRIS MEFPVENCVK KTGNGEVVGA TDIIIVGAGV AGAALAYSLG
KDGRRVHVIE RELNPPDRIA GEALLPGGYV KLIELGLDDC VDGIDAQRIS GYDLYKDGNG
TKISFPLEKF QSHVAGRNFH NGRFVQKLRE KAASLPNVNL EQGTVTSLLE ESGTIQGVHY
KNKSGQELTA SAPLTIVCDG GFSNLRRSLC YPKVDIPSYF VGLVLENCKL PHANYGAIIL
EDPSPILFYP ISSTEIRCLV DVPSQKLPSV SGGEMALFLK TVIAPQIPPE LYTAFISAVG
KQNNIRTMAN RTMPAAPLPT PGALLMGDAF NMRHPITGGG MTVALSDVVV IRDLLRPLHN
LGNASAVCRY LESFYTLRKP MASTINTLAD TLHKVFSASS DPAMQQMQQA CFGYLSLGGV
FSNGLSSLIS GLYPRPSSLA FHLFAMTVYG VGRLLLPFPS PNRMWTGAKL IWVASGILFP
LIKSEGVKQM FFPLTVPAYY RAPPF
//
