ID A0A0L9VGS7_PHAAN Unreviewed; 515 AA.
AC A0A0L9VGS7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=LR48_Vigan09g256300 {ECO:0000313|EMBL:KOM53904.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM53904.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
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; CM003379; KOM53904.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L9VGS7; -.
DR STRING; 3914.A0A0L9VGS7; -.
DR EnsemblPlants; KOM53904; KOM53904; LR48_Vigan09g256300.
DR Gramene; KOM53904; KOM53904; LR48_Vigan09g256300.
DR OMA; AKRTFYW; -.
DR UniPathway; UPA00767; UER00752.
DR Proteomes; UP000053144; 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; 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:SF26; 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 FAD {ECO:0000256|RuleBase:RU367121};
KW Flavoprotein {ECO:0000256|RuleBase:RU367121};
KW Membrane {ECO:0000256|RuleBase:RU367121};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU367121};
KW Reference proteome {ECO:0000313|Proteomes:UP000053144};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367121};
KW Transmembrane helix {ECO:0000256|RuleBase:RU367121}.
FT TRANSMEM 445..464
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367121"
FT TRANSMEM 470..488
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367121"
FT DOMAIN 48..78
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 197..470
FT /note="Squalene epoxidase"
FT /evidence="ECO:0000259|Pfam:PF08491"
SQ SEQUENCE 515 AA; 56221 MW; 407AB59ED17EF79D CRC64;
MVLLFVLFNS ASKKEAKGLV HAENNGSSMI TTTAENGNQH QRISPTSDIV IVGAGVAGSA
LAYTLAKEGR RVHVIERDLT EPDRIVGELL QPGGYLKLIE LDLQDCVGEI DAQQVFGYAL
YKDGKNTKLS YPLEKFDSDV SGRSFHNGRF IQRMREKAST LPNVKLEQGT VTSLLEENGI
IRGVNYKTRN GQELTAKAPL TIVCDGCFSN LRRSLCNPKV DVPSHFVGLI LENCNLPYEN
HGHVILGDPS PILFYPISST EIRCLVDVPA DKKLPSLGNG DMARYLKTVV APQVPPELHA
SFIAAVDKGN IRSMPNRSMP ASPYSTPGAL LMGDAFNMRH PLTGGGMTVA LSDIVLLRNL
LRPLHDLHDA NALFKYLESF YTLRKPMAST INTLAGALYK VFCASPDPAS KEMRQACFDY
LSLGGVFSDG PISLLSGLNP RPLSLVLHFF AVAIYGVGRL LIPFPSPKSM WIGARIISGA
SAIIFPIIRA EGIRQMFFPV TVPAYYRTPP SNLHV
//
