ID A0A167DKL7_9HYPO Unreviewed; 497 AA.
AC A0A167DKL7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-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=BBO_05180 {ECO:0000313|EMBL:OAA42517.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA42517.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA42517.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA42517.1,
RC ECO:0000313|Proteomes:UP000076863};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU367121}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU367121}. Microsome membrane
CC {ECO:0000256|ARBA:ARBA00004154}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004154}.
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:OAA42517.1}.
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DR EMBL; AZHA01000014; OAA42517.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167DKL7; -.
DR OrthoDB; 148348at2759; -.
DR UniPathway; UPA00767; UER00752.
DR Proteomes; UP000076863; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum 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:SF0; 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 Endoplasmic reticulum {ECO:0000256|RuleBase:RU367121};
KW FAD {ECO:0000256|RuleBase:RU367121};
KW Flavoprotein {ECO:0000256|RuleBase:RU367121};
KW Membrane {ECO:0000256|RuleBase:RU367121};
KW Microsome {ECO:0000256|ARBA:ARBA00022848};
KW Monooxygenase {ECO:0000313|EMBL:OAA42517.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU367121};
KW Transmembrane {ECO:0000256|RuleBase:RU367121};
KW Transmembrane helix {ECO:0000256|RuleBase:RU367121}.
FT TRANSMEM 21..38
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367121"
FT TRANSMEM 382..399
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367121"
FT TRANSMEM 435..453
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367121"
FT TRANSMEM 473..492
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367121"
FT DOMAIN 20..49
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 191..455
FT /note="Squalene epoxidase"
FT /evidence="ECO:0000259|Pfam:PF08491"
SQ SEQUENCE 497 AA; 54311 MW; 0ABDA1F46AF3E38C CRC64;
MATDTVEARR LQRETHHEAD VVVVGAGVFG CAAAYALAEQ GRSVLLLERW MHEPDRIVGE
LLQPGGIQAL KKLGLGHCVD NIDSITCRGY NVIYQGTDVL IPYPTMDDHG GVPHQWSGAG
KEGKREIGKG FHHGRFVMQL RETCLAHPNI TVRETEVIKT VRGEHSDHVL GVETRTTNRE
TGKKTADYFF GQLTVIADGY DSKFRKEVTD TQPVARSKFY ALELKDADLP APGYGHVIIG
DAFPTLLYQI GTHETRALFD VPHGIPEAAP AAGGVRNYLT NHAIPALPAS VRPAALAALE
DGKLRSMPNS WLPPTRQVPR GMVVLGDATN MRHPLTGAGM TVAFNDAVLL AELLHPNRVP
NLADAKAVQA ALSALYWRRK NYTAILNVLA QALYALFAAN DPQLHALRMG CFEYFRRGYT
DGPCGLLGGI IHRPVVLAYH FFSVAFLGIW MHVLETVTSG PGPLGVLKLP LALIDAVLIL
AKACVVFLPL IWREGFR
//
