FDFT_CANGA
ID FDFT_CANGA Reviewed; 443 AA.
AC Q9HGZ6; Q6FJD8;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 25-MAY-2022, entry version 132.
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=ERG9; OrderedLocusNames=CAGL0M07095g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=10952588; DOI=10.1128/aac.44.9.2411-2418.2000;
RA Nakayama H., Izuta M., Nakayama N., Arisawa M., Aoki Y.;
RT "Depletion of the squalene synthase (ERG9) gene does not impair growth of
RT Candida glabrata in mice.";
RL Antimicrob. Agents Chemother. 44:2411-2418(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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.
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 {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phytoene/squalene synthase family.
CC {ECO:0000305}.
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DR EMBL; AB009978; BAB12207.1; -; Genomic_DNA.
DR EMBL; CR380959; CAG62632.1; -; Genomic_DNA.
DR RefSeq; XP_449656.1; XM_449656.1.
DR AlphaFoldDB; Q9HGZ6; -.
DR SMR; Q9HGZ6; -.
DR STRING; 5478.XP_449656.1; -.
DR PRIDE; Q9HGZ6; -.
DR EnsemblFungi; CAG62632; CAG62632; CAGL0M07095g.
DR GeneID; 2891705; -.
DR KEGG; cgr:CAGL0M07095g; -.
DR CGD; CAL0136937; ERG9.
DR VEuPathDB; FungiDB:CAGL0M07095g; -.
DR eggNOG; KOG1459; Eukaryota.
DR HOGENOM; CLU_031981_2_1_1; -.
DR InParanoid; Q9HGZ6; -.
DR OMA; RFWPKEI; -.
DR UniPathway; UPA00767; UER00751.
DR Proteomes; UP000002428; Chromosome M.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004310; F:farnesyl-diphosphate farnesyltransferase activity; IMP:CGD.
DR GO; GO:0051996; F:squalene synthase activity; IMP:CGD.
DR GO; GO:0006696; P:ergosterol biosynthetic process; IMP:CGD.
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..443
FT /note="Squalene synthase"
FT /id="PRO_0000067448"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 217
FT /note="M -> L (in Ref. 1; BAB12207)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 51397 MW; C23BC9D603E44C9F CRC64;
MGKVLDLALH PLELRAALKL KFIRQPLFST NDTRATPQLE RCYELLNLTS RSFAAVIMEL
HPELRNVIMV FYLILRALDT VEDDMTIDPQ LKVKVLREFD SKLDTTDWSF DGNDLKEKDR
VVLTEFPCIL GEYHKLKPEY QKVIKRITGL MGNGMADYIL DENFNLNGVQ TVKDYDKYCH
YVAGLVGDGL TELIVLAGFG SDDLYHGKNS FQLYESMGLF LQKTNIIRDY AEDLDDGRSF
WPKEIWSEYA TKLTDFRDPK NTQKGVDCIN HLVLNALTHV IDVLTYLSSI HEQSSFQFCA
IPQVMAIATL AKVFNNPEVL RKNVKIRKGT TCDLILNSRT LKGCVDIFQY YLRDMKQRLP
VEDPNYLKFN IQVAKIEQFI EEMFQDNLPA GVEPRETMIY LKVQERLKWD TQVIPRVQEE
DYKFNMALSV VFCVLLSFYF FTK
