FDFT_YARLI
ID FDFT_YARLI Reviewed; 445 AA.
AC Q9Y753;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Squalene synthase;
DE Short=SQS;
DE Short=SS;
DE EC=2.5.1.21;
DE AltName: Full=FPP:FPP farnesyltransferase;
DE AltName: Full=Farnesyl-diphosphate farnesyltransferase;
GN Name=SQS1; OrderedLocusNames=YALI0A10076g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=10649449;
RX DOI=10.1002/(sici)1097-0061(200002)16:3<197::aid-yea513>3.0.co;2-l;
RA Merkulov S., van Assema F., Springer J., Fernandez Del Carmen A.,
RA Mooibroek H.;
RT "Cloning and characterization of the Yarrowia lipolytica squalene synthase
RT (SQS1) gene and functional complementation of the Saccharomyces cerevisiae
RT erg9 mutation.";
RL Yeast 16:197-206(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Catalyzes the condensation of 2 two farnesyl pyrophosphate
CC moieties to form squalene. It is the first committed enzyme of the
CC sterol biosynthesis pathway. Required for the biosynthesis of
CC ergosterol. {ECO:0000269|PubMed:10649449}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADPH = 2 diphosphate
CC + NADP(+) + squalene; Xref=Rhea:RHEA:32295, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:175763; EC=2.5.1.21;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADH = 2 diphosphate +
CC NAD(+) + squalene; Xref=Rhea:RHEA:32299, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:175763; EC=2.5.1.21;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Terpene metabolism; lanosterol biosynthesis; lanosterol from
CC farnesyl diphosphate: step 1/3.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P29704}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the phytoene/squalene synthase family.
CC {ECO:0000305}.
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DR EMBL; AF092497; AAD22408.1; -; Genomic_DNA.
DR EMBL; CR382127; CAG83856.1; -; Genomic_DNA.
DR RefSeq; XP_499929.1; XM_499929.1.
DR AlphaFoldDB; Q9Y753; -.
DR SMR; Q9Y753; -.
DR STRING; 4952.CAG83856; -.
DR EnsemblFungi; CAG83856; CAG83856; YALI0_A10076g.
DR GeneID; 2906604; -.
DR KEGG; yli:YALI0A10076g; -.
DR VEuPathDB; FungiDB:YALI0_A10076g; -.
DR HOGENOM; CLU_031981_2_1_1; -.
DR OMA; RFWPKEI; -.
DR UniPathway; UPA00767; UER00751.
DR Proteomes; UP000001300; Chromosome A.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004310; F:farnesyl-diphosphate farnesyltransferase activity; IBA:GO_Central.
DR GO; GO:0051996; F:squalene synthase activity; IBA:GO_Central.
DR GO; GO:0006696; P:ergosterol biosynthetic process; IBA:GO_Central.
DR GO; GO:0045338; P:farnesyl diphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00683; Trans_IPPS_HH; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR002060; Squ/phyt_synthse.
DR InterPro; IPR006449; Squal_synth-like.
DR InterPro; IPR019845; Squalene/phytoene_synthase_CS.
DR InterPro; IPR044844; Trans_IPPS_euk-type.
DR InterPro; IPR033904; Trans_IPPS_HH.
DR PANTHER; PTHR11626; PTHR11626; 1.
DR Pfam; PF00494; SQS_PSY; 1.
DR SFLD; SFLDG01018; Squalene/Phytoene_Synthase_Lik; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR TIGRFAMs; TIGR01559; squal_synth; 1.
DR PROSITE; PS01044; SQUALEN_PHYTOEN_SYN_1; 1.
DR PROSITE; PS01045; SQUALEN_PHYTOEN_SYN_2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Isoprene biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Magnesium; Membrane; Multifunctional enzyme; NADP;
KW Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..445
FT /note="Squalene synthase"
FT /id="PRO_0000067453"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 445 AA; 51145 MW; 5028E55F0A66DC7D CRC64;
MGKLIELLLH PSELSAAIHY KLWRQPLHPR DLSKESTELR RCYELLDVCS RSFAAVIREL
HPEVRDAVML FYLILRALDT IEDDMTLSRD IKIPILRDFT KCMKTPGWKF TDSDPNERDR
VVLQEFPVVM TEFNKLKPKY QEVIYDITDR MGNGMADYVI DDDFNNNGVD TIAAYDLYCH
HVAGIVGEGL TRITILAGFG TDVLHENPRL QESMGLFLQK VNIIRDYRED IDVNRAFWPR
EIWHKYAEEM RDFKDPKYSK KALHCTSDLV ANALGHATDC LDYLDNVTDP STFTFCAIPQ
VMAIATLDLV YRNPDVFQKN VKLRKGTTVS LILEASNVSG VCDIFTRYAR KVYKKSDPND
PNYFRVSVLC GKIEQHAALI KRQRGPPAKT IAQLEGERKE MALSLIVCLA VIFSMSGLMA
YIAYVSGFRW SPREIFDSKM FPLRD
