SQE2_PANGI
ID SQE2_PANGI Reviewed; 545 AA.
AC B7TWW5;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Squalene monooxygenase SE2 {ECO:0000305};
DE EC=1.14.14.17 {ECO:0000250|UniProtKB:Q9SM02};
DE AltName: Full=Squalene epoxidase 2 {ECO:0000303|PubMed:19857882, ECO:0000303|PubMed:29509695};
DE Short=PgSQE2 {ECO:0000303|PubMed:19857882, ECO:0000303|PubMed:29509695};
DE Short=SE2 {ECO:0000303|PubMed:19857882};
GN Name=SQE2 {ECO:0000303|PubMed:19857882, ECO:0000303|PubMed:29509695};
OS Panax ginseng (Korean ginseng).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Araliaceae; Panax.
OX NCBI_TaxID=4054;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, REPRESSION BY
RP METHYL JASMONATE, AND INDUCTION BY SQUALENE.
RX PubMed=19857882; DOI=10.1016/j.phytochem.2009.09.031;
RA Han J.-Y., In J.-G., Kwon Y.-S., Choi Y.-E.;
RT "Regulation of ginsenoside and phytosterol biosynthesis by RNA
RT interferences of squalene epoxidase gene in Panax ginseng.";
RL Phytochemistry 71:36-46(2010).
RN [2]
RP REVIEW.
RX PubMed=29378087; DOI=10.1002/bab.1649;
RA Lu J., Li J., Wang S., Yao L., Liang W., Wang J., Gao W.;
RT "Advances in ginsenoside biosynthesis and metabolic regulation.";
RL Biotechnol. Appl. Biochem. 65:514-522(2018).
RN [3]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=29509695; DOI=10.3390/molecules23030589;
RA Yang J.-L., Hu Z.-F., Zhang T.-T., Gu A.-D., Gong T., Zhu P.;
RT "Progress on the studies of the key enzymes of ginsenoside biosynthesis.";
RL Molecules 23:0-0(2018).
CC -!- FUNCTION: Component of the triterpene saponins (e.g. ginsenosides or
CC panaxosides) and phytosterols biosynthetic pathways (PubMed:19857882,
CC PubMed:29378087). Catalyzes the first oxygenation step in sterol
CC biosynthesis and is suggested to be one of the rate-limiting enzymes in
CC this pathway (By similarity). {ECO:0000250|UniProtKB:Q9SM02,
CC ECO:0000269|PubMed:19857882, ECO:0000303|PubMed:29378087}.
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:0000250|UniProtKB:Q9SM02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25283;
CC Evidence={ECO:0000303|PubMed:29509695};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q14534};
CC -!- PATHWAY: Terpene metabolism; lanosterol biosynthesis; lanosterol from
CC farnesyl diphosphate: step 2/3.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Weak expression in petioles and flower buds and
CC barely detectable in roots and leaves. In petioles, preferentially
CC observed in vascular bundle tissue (phloem cells and parenchymatous
CC cells near xylem) and resin ducts. {ECO:0000269|PubMed:19857882}.
CC -!- INDUCTION: Repressed by methyl jasmonate (MeJA) (PubMed:19857882).
CC Accumulates in the presence of squalene (PubMed:19857882).
CC {ECO:0000269|PubMed:19857882}.
CC -!- SIMILARITY: Belongs to the squalene monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; FJ393274; ACJ24907.2; -; mRNA.
DR AlphaFoldDB; B7TWW5; -.
DR SMR; B7TWW5; -.
DR BRENDA; 1.14.99.7; 7895.
DR UniPathway; UPA00767; UER00752.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004506; F:squalene monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0016126; P:sterol biosynthetic process; IMP:UniProtKB.
DR GO; GO:0046246; P:terpene biosynthetic process; IMP:UniProtKB.
DR Gene3D; 3.50.50.60; -; 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; PTHR10835; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF08491; SE; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Isoprene biosynthesis; Membrane; Oxidoreductase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..545
FT /note="Squalene monooxygenase SE2"
FT /id="PRO_0000446960"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 86..87
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 106..107
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 114
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 185
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 201
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 364
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 377
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT SITE 148
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
SQ SEQUENCE 545 AA; 60209 MW; 9EC0E9A183FCFC2C CRC64;
MELERSYREN DEYFLMFAAT LLFGFVLYLF TLRRRRRRRE KKGGAGSMEI INGAYKMTSS
SEVNGHCTPE DIAGSSDDVI IVGAGVAGSA LAYTLAKDGR RVHVIERDLT EQDRIVGELL
QPGGYLKLVE LGLEDCVNEI DAQRVFGYAL YMDGKNTRLS YPLEKFHADV AGRSFHNGRF
IQRMREKAAS LPNVRMEQGT VTSLVEQKGT VKGVRYKTKN GQEMSAAYAP LTIVCDGCFS
NLRHSLCNPK VDVPSCFVGL ILENIDLPHI NHGHVILADP SPILFYKISS TEIRCLVDVP
GQKVPSIANG ELAHYLKTSV APQIPPELYK SFIAAIDKGK IKTMPNRSMP ADPHSTPGAL
LLGDAFNMRH PLTGGGMTVA LSDIVLIRDL LRPLRDLHDS STLCKYLESF YTLRKPVAST
INTLAGALYK VFCASPDKAR QEMRDACFDY LSLGGICSEG PIALLSGLNP RPMSLFFHFF
AVAIYGVGRL LIPFPSPRKM WLGARLISGA SGIIFPIIKS EGVRQMFFPA TVPAYYRAPP
ITKKM
