ID A0A7M1IED8_9EURO Unreviewed; 453 AA. AC A0A7M1IED8; DT 03-MAY-2023, integrated into UniProtKB/TrEMBL. DT 03-MAY-2023, sequence version 1. DT 02-OCT-2024, entry version 7. 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}; DE Flags: Fragment; GN Name=erg1 {ECO:0000313|EMBL:QOQ37949.1}; OS Trichophyton indotineae. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton. OX NCBI_TaxID=2739387 {ECO:0000313|EMBL:QOQ37949.1}; RN [1] {ECO:0000313|EMBL:QOQ37949.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=205666/19 {ECO:0000313|EMBL:QOQ37943.1}, 205667/19 RC {ECO:0000313|EMBL:QOQ37944.1}, 209934/19 RC {ECO:0000313|EMBL:QOQ37946.1}, 211564/18 RC {ECO:0000313|EMBL:QOQ37934.1}, 216532/19 RC {ECO:0000313|EMBL:QOQ37949.1}, 218360/18 RC {ECO:0000313|EMBL:QOQ37936.1}, 600174/19 RC {ECO:0000313|EMBL:QOQ37942.1}, and 901538/18 RC {ECO:0000313|EMBL:QOQ37938.1}; RX PubMed=33027904; RA Nenoff P., Verma S.B., Ebert A., S A., Fischer E., Auerswald E., Dessoi S., RA Hofmann W., Schmidt S., Neubert K., Renner R., Sohl S., Hradetzky U., RA Krusche U., Wenzel H.C., Staginnus A., Schaller J., M V., Tauer C., RA Gebhardt M., Schubert K., Almustafa Z., Stadler R., Fuchs A., Sitaru C., RA Retzlaff C., Overbeck C., Neumann T., Kerschnitzki A., Krause S., RA Schaller M., Walker B., Walther T., K L., Albrecht M., Willing U., RA Monod M., Salamin K., Burmester A., Koch D., Kr C., Uhrla S.; RT "Spread of Terbinafine-Resistant Trichophyton mentagrophytes Type VIII RT (India) in Germany-'The Tip of the Iceberg?'."; RL J Fungi (Basel) 6:0-E207(2020). RN [2] {ECO:0000313|EMBL:QOQ37949.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=205666/19 {ECO:0000313|EMBL:QOQ37943.1}, 205667/19 RC {ECO:0000313|EMBL:QOQ37944.1}, 209934/19 RC {ECO:0000313|EMBL:QOQ37946.1}, 211564/18 RC {ECO:0000313|EMBL:QOQ37934.1}, 216532/19 RC {ECO:0000313|EMBL:QOQ37949.1}, 218360/18 RC {ECO:0000313|EMBL:QOQ37936.1}, 600174/19 RC {ECO:0000313|EMBL:QOQ37942.1}, and 901538/18 RC {ECO:0000313|EMBL:QOQ37938.1}; RA Burmester A., Uhrlass S.; RL Submitted (JUL-2020) 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}. 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; MT700502; QOQ37934.1; -; Genomic_DNA. DR EMBL; MT700504; QOQ37936.1; -; Genomic_DNA. DR EMBL; MT700506; QOQ37938.1; -; Genomic_DNA. DR EMBL; MT700510; QOQ37942.1; -; Genomic_DNA. DR EMBL; MT700511; QOQ37943.1; -; Genomic_DNA. DR EMBL; MT700512; QOQ37944.1; -; Genomic_DNA. DR EMBL; MT700514; QOQ37946.1; -; Genomic_DNA. DR EMBL; MT700517; QOQ37949.1; -; Genomic_DNA. DR UniPathway; UPA00767; UER00752. 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:0006696; P:ergosterol biosynthetic process; IEA:TreeGrafter. 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 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 20..39 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU367121" FT DOMAIN 21..51 FT /note="FAD dependent oxidoreductase" FT /evidence="ECO:0000259|Pfam:PF01266" FT DOMAIN 172..446 FT /note="Squalene epoxidase" FT /evidence="ECO:0000259|Pfam:PF08491" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:QOQ37949.1" FT NON_TER 453 FT /evidence="ECO:0000313|EMBL:QOQ37949.1" SQ SEQUENCE 453 AA; 49934 MW; B87AECDFC324FCDB CRC64; AKPKAYRDEA ERRRYEHHEA DVVIIGAGIA GCALAVALGN QGRSVILLER SLKEPDRIVG ELLQPGGVRA LEQLGLRDCL EGIDAVRTYG YDVIYFGNGV KIPFPSDAND KILEGRCFHH GRFIMRLREA AAANPNVTIV ETKAVSTIKS THTGDVLGVQ CQTDGKQDFY FGPLTVVADG YASTFRKEYL PIQPVAKSKF WGLELIDAKL PIPGHGHVVL GDFPPILIYQ IGEHETRILI DIPDNLPSAS VANGGVKGHM RNVVLPSLPE CIRPSFEAAL EKGGFRSMPN SFLRPVTNRI PGLMFLGDSL NMRHPLTGGG MTVAFNDVVL LRNLLSPEAV PDLSDTKLVL KQLSKFHWQR KSLISVINIL AQSLYSIFAA GDPNLKVLQR GCFRYFQLGL IDGPIGLLSG IIRSPLVLLR HFYSVAFLTI WLHLTSKPIY LLPLTLFECI IVF //