ID C0NDV1_AJECG Unreviewed; 484 AA.
AC C0NDV1;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=HCBG_02044 {ECO:0000313|EMBL:EEH10399.1};
OS Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=447093 {ECO:0000313|EMBL:EEH10399.1, ECO:0000313|Proteomes:UP000001631};
RN [1] {ECO:0000313|Proteomes:UP000001631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432
RC {ECO:0000313|Proteomes:UP000001631};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU367121}.
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DR EMBL; GG663364; EEH10399.1; -; Genomic_DNA.
DR AlphaFoldDB; C0NDV1; -.
DR STRING; 447093.C0NDV1; -.
DR VEuPathDB; FungiDB:I7I50_00426; -.
DR HOGENOM; CLU_026390_0_0_1; -.
DR InParanoid; C0NDV1; -.
DR OrthoDB; 148348at2759; -.
DR UniPathway; UPA00767; UER00752.
DR Proteomes; UP000001631; 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; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR040131; MnmG_N.
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; PF01134; GIDA; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU367121};
KW Reference proteome {ECO:0000313|Proteomes:UP000001631};
KW Transmembrane {ECO:0000256|RuleBase:RU367121};
KW Transmembrane helix {ECO:0000256|RuleBase:RU367121}.
FT TRANSMEM 454..479
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367121"
FT DOMAIN 35..178
FT /note="MnmG N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01134"
FT DOMAIN 186..458
FT /note="Squalene epoxidase"
FT /evidence="ECO:0000259|Pfam:PF08491"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 484 AA; 53918 MW; 3BC42A5AEB3D4154 CRC64;
MAMPPQLPNG NGALKTPRVY SDEGERRRCE DHEADVVIVG AGIAGCALAV ALGKQGRSVL
LLERWLKEPD RIVGELLQPG GVRALDQLGL KHCLEDIDAV ECHGMDVIYH GNEVPIRYPM
DEQGSPFKGR SFHHGRFIMR LRESARATPN VTIVETTAVS VIHSSTDNEV LGVQCTTNGQ
KDYFYAPLTF IADGYASKFR KQYLPTTPRV KSKFWGLELI DAELPRKNFG HVVLPDGPPV
LLYQIGTRET RILVDIPENL PSASVENGGV KGHLRKVVLP SLPKCVQPSF DKALEKGGLR
SMPNSFLPPT TNKTPGLVFL GDSLNMRHPL TGGGMTVAFS DVVLLRTLLS PENVPDFSNK
QQVLKQMSKF HWERKGLTSV INILAQALYS LYAADDPYLK VLQQGCFRYF QLGQVDGPIG
LLAAVTPRPW VLLRHFYSVA FLSIWEFIHS QPGYMFPVTF VQCFIVFWTA CRVIFPYIFA
ELRS
//
