(data stored in ACNUC8465 zone)

SWISSPROT: 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   30-AUG-2017, entry version 113.
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 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; 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
RT   of 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.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   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
CC       pyrophosphate moieties to form squalene. It is the first committed
CC       enzyme of the sterol biosynthesis pathway. Required for the
CC       biosynthesis of ergosterol.
CC   -!- CATALYTIC ACTIVITY: 2 farnesyl diphosphate + NAD(P)H = squalene +
CC       2 diphosphate + NAD(P)(+).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Terpene metabolism; lanosterol biosynthesis; lanosterol
CC       from farnesyl diphosphate: step 1/3.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phytoene/squalene synthase family.
CC       {ECO:0000305}.
DR   EMBL; AB009978; BAB12207.1; -; Genomic_DNA.
DR   EMBL; CR380959; CAG62632.1; -; Genomic_DNA.
DR   RefSeq; XP_449656.1; XM_449656.1.
DR   ProteinModelPortal; Q9HGZ6; -.
DR   SMR; Q9HGZ6; -.
DR   STRING; 284593.XP_449656.1; -.
DR   EnsemblFungi; CAG62632; CAG62632; CAGL0M07095g.
DR   KEGG; cgr:CAGL0M07095g; -.
DR   CGD; CAL0136937; ERG9.
DR   EuPathDB; FungiDB:CAGL0M07095g; -.
DR   eggNOG; KOG1459; Eukaryota.
DR   eggNOG; COG1562; LUCA.
DR   HOGENOM; HOG000186940; -.
DR   InParanoid; Q9HGZ6; -.
DR   KO; K00801; -.
DR   OMA; FNFVAIP; -.
DR   OrthoDB; EOG092C2IU6; -.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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.
DR   InterPro; IPR002060; Squ/phyt_synthse.
DR   InterPro; IPR006449; Squal_synth.
DR   InterPro; IPR019845; Squalene/phytoene_synthase_CS.
DR   InterPro; IPR033904; Trans_IPPS_HH.
DR   Pfam; PF00494; SQS_PSY; 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;
DR   PRODOM; Q9HGZ6.
DR   SWISS-2DPAGE; Q9HGZ6.
KW   Complete proteome; Endoplasmic reticulum; Isoprene biosynthesis;
KW   Lipid biosynthesis; Lipid metabolism; Magnesium; Membrane;
KW   Multifunctional enzyme; NADP; Oxidoreductase; Reference proteome;
KW   Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW   Sterol metabolism; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN         1    443       Squalene synthase.
FT                                /FTId=PRO_0000067448.
FT   TRANSMEM    181    201       Helical. {ECO:0000255}.
FT   TRANSMEM    294    314       Helical. {ECO:0000255}.
FT   CONFLICT    217    217       M -> L (in Ref. 1; BAB12207).
FT                                {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
//

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